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HEADER HYDROLASE 10-MAR-19 6QZ2
TITLE STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_0224;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCJ136
KEYWDS MHETASE, PET DEGRADATION, STRUCTURAL GENOMICS, PLASTIC-BINDING
KEYWDS 2 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 30-SEP-20 6QZ2 0
JRNL AUTH M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL STRUCTURE OF FROM MHETASE FROM IDEONELLA SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 506771
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 24886
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 57.6459 - 5.9017 0.96 16428 864 0.1686 0.1717
REMARK 3 2 5.9017 - 4.6850 0.94 16053 924 0.1611 0.1792
REMARK 3 3 4.6850 - 4.0930 0.95 16157 892 0.1466 0.1597
REMARK 3 4 4.0930 - 3.7188 0.95 16286 867 0.1625 0.1695
REMARK 3 5 3.7188 - 3.4523 0.95 16409 771 0.1703 0.1867
REMARK 3 6 3.4523 - 3.2488 0.95 16318 798 0.1776 0.1866
REMARK 3 7 3.2488 - 3.0861 0.95 16450 775 0.1835 0.2070
REMARK 3 8 3.0861 - 2.9518 0.95 16187 839 0.1790 0.1925
REMARK 3 9 2.9518 - 2.8381 0.95 16392 828 0.1885 0.2133
REMARK 3 10 2.8381 - 2.7402 0.95 16386 889 0.1875 0.2134
REMARK 3 11 2.7402 - 2.6545 0.95 16207 817 0.1937 0.2170
REMARK 3 12 2.6545 - 2.5787 0.94 16428 671 0.1920 0.2136
REMARK 3 13 2.5787 - 2.5108 0.94 16068 840 0.1905 0.2188
REMARK 3 14 2.5108 - 2.4495 0.93 16014 920 0.1907 0.2242
REMARK 3 15 2.4495 - 2.3938 0.93 15861 814 0.1938 0.2262
REMARK 3 16 2.3938 - 2.3429 0.93 15907 824 0.1945 0.2201
REMARK 3 17 2.3429 - 2.2960 0.92 15878 831 0.1983 0.2258
REMARK 3 18 2.2960 - 2.2527 0.93 15878 853 0.1961 0.2226
REMARK 3 19 2.2527 - 2.2125 0.93 15995 860 0.1962 0.2262
REMARK 3 20 2.2125 - 2.1749 0.93 16056 814 0.2044 0.2310
REMARK 3 21 2.1749 - 2.1399 0.93 15907 831 0.2053 0.2308
REMARK 3 22 2.1399 - 2.1069 0.93 15839 844 0.2094 0.2339
REMARK 3 23 2.1069 - 2.0760 0.92 15728 852 0.2154 0.2520
REMARK 3 24 2.0760 - 2.0467 0.92 15766 810 0.2252 0.2585
REMARK 3 25 2.0467 - 2.0190 0.93 16000 848 0.2277 0.2658
REMARK 3 26 2.0190 - 1.9928 0.93 15986 800 0.2267 0.2519
REMARK 3 27 1.9928 - 1.9679 0.92 15725 827 0.2320 0.2605
REMARK 3 28 1.9679 - 1.9442 0.93 16026 801 0.2439 0.2795
REMARK 3 29 1.9442 - 1.9216 0.92 15823 808 0.2499 0.2734
REMARK 3 30 1.9216 - 1.9000 0.92 15727 774 0.2647 0.2976
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 42546
REMARK 3 ANGLE : 0.576 57971
REMARK 3 CHIRALITY : 0.041 6082
REMARK 3 PLANARITY : 0.004 7761
REMARK 3 DIHEDRAL : 4.955 24792
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6QZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1292101165.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 506864
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 95.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6QZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE (PH 5.5), 1.0 M
REMARK 280 AMMONIUM PHOSPHATE MONOBASIC, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 MET A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 CYS A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 LEU A 604
REMARK 465 GLU A 605
REMARK 465 HIS A 606
REMARK 465 HIS A 607
REMARK 465 HIS A 608
REMARK 465 HIS A 609
REMARK 465 HIS A 610
REMARK 465 HIS A 611
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 VAL B 5
REMARK 465 THR B 6
REMARK 465 THR B 7
REMARK 465 MET B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 ALA B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 ALA B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 CYS B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 GLU B 37
REMARK 465 PRO B 38
REMARK 465 PRO B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 PRO B 42
REMARK 465 LEU B 604
REMARK 465 GLU B 605
REMARK 465 HIS B 606
REMARK 465 HIS B 607
REMARK 465 HIS B 608
REMARK 465 HIS B 609
REMARK 465 HIS B 610
REMARK 465 HIS B 611
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 THR C 3
REMARK 465 THR C 4
REMARK 465 VAL C 5
REMARK 465 THR C 6
REMARK 465 THR C 7
REMARK 465 MET C 8
REMARK 465 LEU C 9
REMARK 465 LEU C 10
REMARK 465 ALA C 11
REMARK 465 SER C 12
REMARK 465 VAL C 13
REMARK 465 ALA C 14
REMARK 465 LEU C 15
REMARK 465 ALA C 16
REMARK 465 ALA C 17
REMARK 465 CYS C 18
REMARK 465 ALA C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 PRO C 25
REMARK 465 LEU C 26
REMARK 465 PRO C 27
REMARK 465 LEU C 28
REMARK 465 PRO C 29
REMARK 465 GLN C 30
REMARK 465 GLN C 31
REMARK 465 GLN C 32
REMARK 465 PRO C 33
REMARK 465 PRO C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 GLU C 37
REMARK 465 PRO C 38
REMARK 465 PRO C 39
REMARK 465 PRO C 40
REMARK 465 PRO C 41
REMARK 465 PRO C 42
REMARK 465 LEU C 604
REMARK 465 GLU C 605
REMARK 465 HIS C 606
REMARK 465 HIS C 607
REMARK 465 HIS C 608
REMARK 465 HIS C 609
REMARK 465 HIS C 610
REMARK 465 HIS C 611
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 THR D 3
REMARK 465 THR D 4
REMARK 465 VAL D 5
REMARK 465 THR D 6
REMARK 465 THR D 7
REMARK 465 MET D 8
REMARK 465 LEU D 9
REMARK 465 LEU D 10
REMARK 465 ALA D 11
REMARK 465 SER D 12
REMARK 465 VAL D 13
REMARK 465 ALA D 14
REMARK 465 LEU D 15
REMARK 465 ALA D 16
REMARK 465 ALA D 17
REMARK 465 CYS D 18
REMARK 465 ALA D 19
REMARK 465 GLY D 20
REMARK 465 GLY D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 THR D 24
REMARK 465 PRO D 25
REMARK 465 LEU D 26
REMARK 465 PRO D 27
REMARK 465 LEU D 28
REMARK 465 PRO D 29
REMARK 465 GLN D 30
REMARK 465 GLN D 31
REMARK 465 GLN D 32
REMARK 465 PRO D 33
REMARK 465 PRO D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 GLU D 37
REMARK 465 PRO D 38
REMARK 465 PRO D 39
REMARK 465 PRO D 40
REMARK 465 PRO D 41
REMARK 465 PRO D 42
REMARK 465 LEU D 604
REMARK 465 GLU D 605
REMARK 465 HIS D 606
REMARK 465 HIS D 607
REMARK 465 HIS D 608
REMARK 465 HIS D 609
REMARK 465 HIS D 610
REMARK 465 HIS D 611
REMARK 465 MET E 1
REMARK 465 GLN E 2
REMARK 465 THR E 3
REMARK 465 THR E 4
REMARK 465 VAL E 5
REMARK 465 THR E 6
REMARK 465 THR E 7
REMARK 465 MET E 8
REMARK 465 LEU E 9
REMARK 465 LEU E 10
REMARK 465 ALA E 11
REMARK 465 SER E 12
REMARK 465 VAL E 13
REMARK 465 ALA E 14
REMARK 465 LEU E 15
REMARK 465 ALA E 16
REMARK 465 ALA E 17
REMARK 465 CYS E 18
REMARK 465 ALA E 19
REMARK 465 GLY E 20
REMARK 465 GLY E 21
REMARK 465 GLY E 22
REMARK 465 SER E 23
REMARK 465 THR E 24
REMARK 465 PRO E 25
REMARK 465 LEU E 26
REMARK 465 PRO E 27
REMARK 465 LEU E 28
REMARK 465 PRO E 29
REMARK 465 GLN E 30
REMARK 465 GLN E 31
REMARK 465 GLN E 32
REMARK 465 PRO E 33
REMARK 465 PRO E 34
REMARK 465 GLN E 35
REMARK 465 GLN E 36
REMARK 465 GLU E 37
REMARK 465 PRO E 38
REMARK 465 PRO E 39
REMARK 465 PRO E 40
REMARK 465 PRO E 41
REMARK 465 PRO E 42
REMARK 465 LEU E 604
REMARK 465 GLU E 605
REMARK 465 HIS E 606
REMARK 465 HIS E 607
REMARK 465 HIS E 608
REMARK 465 HIS E 609
REMARK 465 HIS E 610
REMARK 465 HIS E 611
REMARK 465 MET F 1
REMARK 465 GLN F 2
REMARK 465 THR F 3
REMARK 465 THR F 4
REMARK 465 VAL F 5
REMARK 465 THR F 6
REMARK 465 THR F 7
REMARK 465 MET F 8
REMARK 465 LEU F 9
REMARK 465 LEU F 10
REMARK 465 ALA F 11
REMARK 465 SER F 12
REMARK 465 VAL F 13
REMARK 465 ALA F 14
REMARK 465 LEU F 15
REMARK 465 ALA F 16
REMARK 465 ALA F 17
REMARK 465 CYS F 18
REMARK 465 ALA F 19
REMARK 465 GLY F 20
REMARK 465 GLY F 21
REMARK 465 GLY F 22
REMARK 465 SER F 23
REMARK 465 THR F 24
REMARK 465 PRO F 25
REMARK 465 LEU F 26
REMARK 465 PRO F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLN F 30
REMARK 465 GLN F 31
REMARK 465 GLN F 32
REMARK 465 PRO F 33
REMARK 465 PRO F 34
REMARK 465 GLN F 35
REMARK 465 GLN F 36
REMARK 465 GLU F 37
REMARK 465 PRO F 38
REMARK 465 PRO F 39
REMARK 465 PRO F 40
REMARK 465 PRO F 41
REMARK 465 PRO F 42
REMARK 465 LEU F 604
REMARK 465 GLU F 605
REMARK 465 HIS F 606
REMARK 465 HIS F 607
REMARK 465 HIS F 608
REMARK 465 HIS F 609
REMARK 465 HIS F 610
REMARK 465 HIS F 611
REMARK 465 MET G 1
REMARK 465 GLN G 2
REMARK 465 THR G 3
REMARK 465 THR G 4
REMARK 465 VAL G 5
REMARK 465 THR G 6
REMARK 465 THR G 7
REMARK 465 MET G 8
REMARK 465 LEU G 9
REMARK 465 LEU G 10
REMARK 465 ALA G 11
REMARK 465 SER G 12
REMARK 465 VAL G 13
REMARK 465 ALA G 14
REMARK 465 LEU G 15
REMARK 465 ALA G 16
REMARK 465 ALA G 17
REMARK 465 CYS G 18
REMARK 465 ALA G 19
REMARK 465 GLY G 20
REMARK 465 GLY G 21
REMARK 465 GLY G 22
REMARK 465 SER G 23
REMARK 465 THR G 24
REMARK 465 PRO G 25
REMARK 465 LEU G 26
REMARK 465 PRO G 27
REMARK 465 LEU G 28
REMARK 465 PRO G 29
REMARK 465 GLN G 30
REMARK 465 GLN G 31
REMARK 465 GLN G 32
REMARK 465 PRO G 33
REMARK 465 PRO G 34
REMARK 465 GLN G 35
REMARK 465 GLN G 36
REMARK 465 GLU G 37
REMARK 465 PRO G 38
REMARK 465 PRO G 39
REMARK 465 PRO G 40
REMARK 465 PRO G 603
REMARK 465 LEU G 604
REMARK 465 GLU G 605
REMARK 465 HIS G 606
REMARK 465 HIS G 607
REMARK 465 HIS G 608
REMARK 465 HIS G 609
REMARK 465 HIS G 610
REMARK 465 HIS G 611
REMARK 465 MET H 1
REMARK 465 GLN H 2
REMARK 465 THR H 3
REMARK 465 THR H 4
REMARK 465 VAL H 5
REMARK 465 THR H 6
REMARK 465 THR H 7
REMARK 465 MET H 8
REMARK 465 LEU H 9
REMARK 465 LEU H 10
REMARK 465 ALA H 11
REMARK 465 SER H 12
REMARK 465 VAL H 13
REMARK 465 ALA H 14
REMARK 465 LEU H 15
REMARK 465 ALA H 16
REMARK 465 ALA H 17
REMARK 465 CYS H 18
REMARK 465 ALA H 19
REMARK 465 GLY H 20
REMARK 465 GLY H 21
REMARK 465 GLY H 22
REMARK 465 SER H 23
REMARK 465 THR H 24
REMARK 465 PRO H 25
REMARK 465 LEU H 26
REMARK 465 PRO H 27
REMARK 465 LEU H 28
REMARK 465 PRO H 29
REMARK 465 GLN H 30
REMARK 465 GLN H 31
REMARK 465 GLN H 32
REMARK 465 PRO H 33
REMARK 465 PRO H 34
REMARK 465 GLN H 35
REMARK 465 GLN H 36
REMARK 465 GLU H 37
REMARK 465 PRO H 38
REMARK 465 PRO H 39
REMARK 465 PRO H 40
REMARK 465 PRO H 41
REMARK 465 LEU H 604
REMARK 465 GLU H 605
REMARK 465 HIS H 606
REMARK 465 HIS H 607
REMARK 465 HIS H 608
REMARK 465 HIS H 609
REMARK 465 HIS H 610
REMARK 465 HIS H 611
REMARK 465 MET I 1
REMARK 465 GLN I 2
REMARK 465 THR I 3
REMARK 465 THR I 4
REMARK 465 VAL I 5
REMARK 465 THR I 6
REMARK 465 THR I 7
REMARK 465 MET I 8
REMARK 465 LEU I 9
REMARK 465 LEU I 10
REMARK 465 ALA I 11
REMARK 465 SER I 12
REMARK 465 VAL I 13
REMARK 465 ALA I 14
REMARK 465 LEU I 15
REMARK 465 ALA I 16
REMARK 465 ALA I 17
REMARK 465 CYS I 18
REMARK 465 ALA I 19
REMARK 465 GLY I 20
REMARK 465 GLY I 21
REMARK 465 GLY I 22
REMARK 465 SER I 23
REMARK 465 THR I 24
REMARK 465 PRO I 25
REMARK 465 LEU I 26
REMARK 465 PRO I 27
REMARK 465 LEU I 28
REMARK 465 PRO I 29
REMARK 465 GLN I 30
REMARK 465 GLN I 31
REMARK 465 GLN I 32
REMARK 465 PRO I 33
REMARK 465 PRO I 34
REMARK 465 GLN I 35
REMARK 465 GLN I 36
REMARK 465 GLU I 37
REMARK 465 PRO I 38
REMARK 465 PRO I 39
REMARK 465 PRO I 40
REMARK 465 PRO I 41
REMARK 465 PRO I 42
REMARK 465 LEU I 604
REMARK 465 GLU I 605
REMARK 465 HIS I 606
REMARK 465 HIS I 607
REMARK 465 HIS I 608
REMARK 465 HIS I 609
REMARK 465 HIS I 610
REMARK 465 HIS I 611
REMARK 465 MET J 1
REMARK 465 GLN J 2
REMARK 465 THR J 3
REMARK 465 THR J 4
REMARK 465 VAL J 5
REMARK 465 THR J 6
REMARK 465 THR J 7
REMARK 465 MET J 8
REMARK 465 LEU J 9
REMARK 465 LEU J 10
REMARK 465 ALA J 11
REMARK 465 SER J 12
REMARK 465 VAL J 13
REMARK 465 ALA J 14
REMARK 465 LEU J 15
REMARK 465 ALA J 16
REMARK 465 ALA J 17
REMARK 465 CYS J 18
REMARK 465 ALA J 19
REMARK 465 GLY J 20
REMARK 465 GLY J 21
REMARK 465 GLY J 22
REMARK 465 SER J 23
REMARK 465 THR J 24
REMARK 465 PRO J 25
REMARK 465 LEU J 26
REMARK 465 PRO J 27
REMARK 465 LEU J 28
REMARK 465 PRO J 29
REMARK 465 GLN J 30
REMARK 465 GLN J 31
REMARK 465 GLN J 32
REMARK 465 PRO J 33
REMARK 465 PRO J 34
REMARK 465 GLN J 35
REMARK 465 GLN J 36
REMARK 465 GLU J 37
REMARK 465 PRO J 38
REMARK 465 PRO J 39
REMARK 465 PRO J 40
REMARK 465 PRO J 41
REMARK 465 PRO J 42
REMARK 465 PRO J 603
REMARK 465 LEU J 604
REMARK 465 GLU J 605
REMARK 465 HIS J 606
REMARK 465 HIS J 607
REMARK 465 HIS J 608
REMARK 465 HIS J 609
REMARK 465 HIS J 610
REMARK 465 HIS J 611
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH E 1378 O HOH E 1536 1.51
REMARK 500 O HOH A 1511 O HOH A 1572 1.80
REMARK 500 O HOH A 1666 O HOH A 1674 1.81
REMARK 500 O HOH C 1226 O HOH C 1569 1.81
REMARK 500 O HOH G 1253 O HOH G 1296 1.81
REMARK 500 O HOH E 1364 O HOH E 1497 1.81
REMARK 500 O HOH F 1671 O HOH F 1673 1.82
REMARK 500 O HOH D 953 O HOH D 1280 1.83
REMARK 500 O HOH A 1417 O HOH A 1445 1.83
REMARK 500 O HOH B 1325 O HOH B 1423 1.84
REMARK 500 O HOH E 1392 O HOH E 1460 1.84
REMARK 500 O HOH B 1428 O HOH B 1498 1.85
REMARK 500 O HOH D 1456 O HOH F 1597 1.85
REMARK 500 O HOH E 1259 O HOH E 1411 1.85
REMARK 500 O HOH D 1404 O HOH H 1207 1.85
REMARK 500 O HOH C 1617 O HOH C 1640 1.85
REMARK 500 O HOH C 1331 O HOH C 1451 1.86
REMARK 500 O HOH F 1344 O HOH F 1565 1.86
REMARK 500 OG SER D 405 O HOH D 901 1.86
REMARK 500 O HOH C 965 O HOH C 1593 1.86
REMARK 500 O HOH C 1242 O HOH C 1486 1.86
REMARK 500 O HOH B 1490 O HOH B 1524 1.87
REMARK 500 O PRO E 602 O HOH E 901 1.87
REMARK 500 O HOH J 1112 O HOH J 1113 1.88
REMARK 500 O HOH G 1009 O HOH G 1369 1.88
REMARK 500 O HOH D 1307 O HOH D 1460 1.88
REMARK 500 O HOH F 1578 O HOH F 1618 1.88
REMARK 500 O HOH C 1236 O HOH C 1605 1.89
REMARK 500 O HOH D 1001 O HOH D 1482 1.89
REMARK 500 O HOH H 999 O HOH H 1273 1.89
REMARK 500 NH1 ARG C 48 O HOH C 901 1.90
REMARK 500 O HOH H 1291 O HOH H 1308 1.90
REMARK 500 O HOH D 958 O HOH D 1462 1.90
REMARK 500 O HOH H 934 O HOH H 946 1.90
REMARK 500 O HOH F 902 O HOH F 919 1.91
REMARK 500 N THR E 388 O HOH E 902 1.92
REMARK 500 O HOH C 1419 O HOH C 1455 1.92
REMARK 500 O HOH F 1419 O HOH F 1538 1.92
REMARK 500 O HOH F 1463 O HOH F 1608 1.92
REMARK 500 OE2 GLU I 549 O HOH I 901 1.93
REMARK 500 O HOH D 1445 O HOH D 1520 1.93
REMARK 500 O HOH A 1613 O HOH A 1630 1.93
REMARK 500 O HOH D 1174 O HOH D 1398 1.93
REMARK 500 O HOH B 1504 O HOH C 1421 1.94
REMARK 500 O HOH A 1634 O HOH A 1641 1.94
REMARK 500 O HOH E 1517 O HOH E 1552 1.94
REMARK 500 NE2 GLN I 336 O HOH I 902 1.94
REMARK 500 O HOH E 924 O HOH E 1546 1.94
REMARK 500 O HOH D 1408 O HOH D 1436 1.94
REMARK 500 O HOH B 1504 O HOH C 1624 1.95
REMARK 500
REMARK 500 THIS ENTRY HAS 329 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH E 1449 O HOH H 1218 1655 1.83
REMARK 500 O HOH D 1450 O HOH E 1566 1455 1.92
REMARK 500 O HOH A 1307 O HOH G 1262 1655 1.93
REMARK 500 O HOH A 1530 O HOH G 1310 1655 2.01
REMARK 500 O HOH D 1176 O HOH E 1039 1455 2.02
REMARK 500 O HOH E 1548 O HOH H 1292 1655 2.02
REMARK 500 O HOH C 1669 O HOH D 1586 1645 2.05
REMARK 500 O HOH C 1188 O HOH E 1226 1545 2.06
REMARK 500 O HOH B 1369 O HOH F 1518 1556 2.08
REMARK 500 O HOH E 1591 O HOH H 1342 1655 2.09
REMARK 500 O HOH E 904 O HOH J 1039 1655 2.13
REMARK 500 O HOH C 1261 O HOH E 1262 1545 2.18
REMARK 500 O HOH A 1480 O HOH G 1347 1655 2.19
REMARK 500 O HOH A 1307 O HOH G 1372 1655 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 67 35.27 -91.02
REMARK 500 ASN A 134 -145.38 60.27
REMARK 500 TYR A 194 -30.33 -151.03
REMARK 500 SER A 225 -119.50 66.30
REMARK 500 ALA A 249 53.91 36.52
REMARK 500 ASP A 311 16.04 -148.28
REMARK 500 TYR A 373 -95.70 -139.63
REMARK 500 SER A 383 -144.92 -142.06
REMARK 500 ASN A 408 14.95 -141.78
REMARK 500 VAL A 412 -60.65 -98.71
REMARK 500 ASN A 527 -148.55 -83.96
REMARK 500 CYS A 529 -23.48 69.07
REMARK 500 ALA B 67 32.98 -86.07
REMARK 500 ASN B 134 -148.28 58.25
REMARK 500 TYR B 194 -29.90 -152.78
REMARK 500 SER B 225 -119.55 66.94
REMARK 500 ALA B 249 57.97 33.85
REMARK 500 ASP B 311 10.24 -149.91
REMARK 500 TYR B 373 -94.18 -143.55
REMARK 500 SER B 383 -141.40 -137.37
REMARK 500 ASN B 408 10.34 -145.00
REMARK 500 VAL B 412 -61.24 -95.84
REMARK 500 SER B 456 105.46 -164.14
REMARK 500 SER B 491 32.04 -97.90
REMARK 500 ASN B 527 -148.68 -86.72
REMARK 500 CYS B 529 -33.51 71.27
REMARK 500 ALA C 67 42.88 -92.30
REMARK 500 ASN C 134 -146.58 57.82
REMARK 500 ASN C 171 55.97 -91.68
REMARK 500 TYR C 194 -30.20 -151.32
REMARK 500 SER C 225 -119.35 70.42
REMARK 500 ALA C 249 56.19 33.51
REMARK 500 ASP C 311 10.96 -141.20
REMARK 500 TYR C 373 -94.43 -147.40
REMARK 500 SER C 383 -142.52 -136.96
REMARK 500 VAL C 412 -60.51 -94.67
REMARK 500 SER C 456 107.08 -161.55
REMARK 500 SER C 491 32.93 -99.67
REMARK 500 ASN C 527 -150.02 -86.95
REMARK 500 CYS C 529 -31.17 70.66
REMARK 500 ALA D 67 35.25 -94.92
REMARK 500 ASN D 134 -149.54 57.95
REMARK 500 TYR D 194 -29.68 -150.15
REMARK 500 SER D 225 -121.48 65.28
REMARK 500 ALA D 249 57.34 32.07
REMARK 500 TYR D 373 -95.71 -146.59
REMARK 500 SER D 383 -137.52 -136.79
REMARK 500 SER D 456 114.46 -162.78
REMARK 500 ASN D 527 -154.98 -88.45
REMARK 500 CYS D 529 -30.35 69.53
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1671 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A1672 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A1673 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A1674 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A1675 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A1676 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH A1677 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH B1648 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B1649 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B1650 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1651 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1652 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B1653 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B1654 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B1655 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B1656 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B1657 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B1658 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B1659 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH C1673 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH C1674 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C1675 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH C1676 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C1677 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C1678 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH C1679 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH C1680 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH C1681 DISTANCE = 8.35 ANGSTROMS
REMARK 525 HOH C1682 DISTANCE = 8.78 ANGSTROMS
REMARK 525 HOH C1683 DISTANCE = 9.07 ANGSTROMS
REMARK 525 HOH C1684 DISTANCE = 9.73 ANGSTROMS
REMARK 525 HOH C1685 DISTANCE = 10.08 ANGSTROMS
REMARK 525 HOH D1602 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D1603 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH D1604 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH D1605 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH D1606 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH E1614 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH E1615 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH E1616 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH E1617 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH E1618 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH E1619 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH E1620 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH E1621 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH E1622 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH E1623 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH E1624 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH F1660 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH F1661 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH F1662 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH F1663 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH F1664 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH F1665 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH F1666 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH F1667 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH F1668 DISTANCE = 8.20 ANGSTROMS
REMARK 525 HOH F1669 DISTANCE = 12.16 ANGSTROMS
REMARK 525 HOH F1670 DISTANCE = 12.57 ANGSTROMS
REMARK 525 HOH F1671 DISTANCE = 13.03 ANGSTROMS
REMARK 525 HOH F1672 DISTANCE = 13.27 ANGSTROMS
REMARK 525 HOH F1673 DISTANCE = 13.60 ANGSTROMS
REMARK 525 HOH G1461 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH G1462 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH G1463 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH G1464 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH G1465 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH G1466 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH G1467 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH H1359 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH H1360 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH H1361 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH I1241 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH J1128 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH J1129 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH J1130 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH J1131 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH J1132 DISTANCE = 6.58 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 68.7
REMARK 620 3 ASP A 307 OD1 71.9 135.0
REMARK 620 4 ASP A 307 OD2 79.2 136.1 51.4
REMARK 620 5 LEU A 309 O 82.0 83.0 70.7 122.1
REMARK 620 6 ASP A 311 OD1 141.4 73.8 135.8 137.4 84.6
REMARK 620 7 ILE A 313 O 99.3 77.3 130.6 79.3 158.1 80.9
REMARK 620 8 HOH A 911 O 145.9 144.9 75.1 73.8 95.0 71.1 95.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 69.7
REMARK 620 3 ASP B 307 OD1 73.2 137.8
REMARK 620 4 ASP B 307 OD2 77.5 135.1 50.0
REMARK 620 5 LEU B 309 O 78.9 82.9 70.7 120.2
REMARK 620 6 ASP B 311 OD1 142.4 74.0 134.2 138.3 87.3
REMARK 620 7 ILE B 313 O 98.3 76.5 129.0 79.0 158.8 82.4
REMARK 620 8 HOH B1034 O 145.3 144.4 72.7 75.8 95.9 70.3 97.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 70.8
REMARK 620 3 ASP C 307 OD1 68.9 134.4
REMARK 620 4 ASP C 307 OD2 73.5 132.6 50.5
REMARK 620 5 LEU C 309 O 81.2 82.5 71.2 121.4
REMARK 620 6 ASP C 311 OD1 146.0 76.7 134.7 139.0 85.3
REMARK 620 7 ILE C 313 O 97.9 80.0 125.7 75.1 161.7 85.6
REMARK 620 8 HOH C 943 O 142.4 146.2 74.4 77.1 94.8 69.5 96.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 304 O
REMARK 620 2 ASP D 304 OD1 70.7
REMARK 620 3 ASP D 307 OD1 75.3 141.3
REMARK 620 4 ASP D 307 OD2 77.9 134.8 50.2
REMARK 620 5 LEU D 309 O 82.7 86.6 71.1 121.0
REMARK 620 6 ASP D 311 OD1 142.5 72.9 134.1 137.0 86.7
REMARK 620 7 ILE D 313 O 99.2 77.6 126.4 76.4 162.4 81.2
REMARK 620 8 HOH D1027 O 144.1 145.1 69.8 73.4 93.9 72.3 94.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 304 O
REMARK 620 2 ASP E 304 OD1 69.7
REMARK 620 3 ASP E 307 OD1 72.5 137.3
REMARK 620 4 ASP E 307 OD2 79.5 136.3 50.7
REMARK 620 5 LEU E 309 O 80.5 82.0 72.7 123.2
REMARK 620 6 ASP E 311 OD1 142.7 74.6 133.8 136.5 84.0
REMARK 620 7 ILE E 313 O 98.7 77.6 127.9 77.3 158.4 83.8
REMARK 620 8 HOH E 915 O 143.8 146.3 72.5 71.2 97.9 71.9 95.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 304 O
REMARK 620 2 ASP F 304 OD1 69.5
REMARK 620 3 ASP F 307 OD1 72.4 135.9
REMARK 620 4 ASP F 307 OD2 77.9 136.3 50.7
REMARK 620 5 LEU F 309 O 78.0 80.6 70.4 120.6
REMARK 620 6 ASP F 311 OD1 143.3 76.1 130.7 138.2 84.3
REMARK 620 7 ILE F 313 O 102.6 80.3 129.9 79.3 159.2 83.3
REMARK 620 8 HOH F 933 O 142.6 146.6 70.8 73.8 95.8 70.5 95.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 304 O
REMARK 620 2 ASP G 304 OD1 69.3
REMARK 620 3 ASP G 307 OD1 73.1 140.1
REMARK 620 4 ASP G 307 OD2 78.2 129.4 51.4
REMARK 620 5 LEU G 309 O 79.1 85.7 74.6 125.4
REMARK 620 6 ASP G 311 OD1 142.3 75.3 135.3 137.0 85.7
REMARK 620 7 ILE G 313 O 99.3 71.3 128.6 77.2 155.7 80.9
REMARK 620 8 HOH G 962 O 144.8 145.9 72.9 73.5 100.5 71.8 94.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 304 O
REMARK 620 2 ASP H 304 OD1 72.0
REMARK 620 3 ASP H 307 OD1 74.8 142.9
REMARK 620 4 ASP H 307 OD2 77.4 132.6 51.7
REMARK 620 5 LEU H 309 O 77.1 83.8 73.1 123.3
REMARK 620 6 ASP H 311 OD1 145.2 76.9 127.6 136.8 84.7
REMARK 620 7 ILE H 313 O 102.4 76.2 127.4 76.2 159.0 84.6
REMARK 620 8 HOH H 969 O 143.1 144.7 69.0 74.8 98.6 68.4 94.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 304 O
REMARK 620 2 ASP I 304 OD1 77.1
REMARK 620 3 ASP I 307 OD1 73.8 146.1
REMARK 620 4 ASP I 307 OD2 74.8 136.1 49.8
REMARK 620 5 LEU I 309 O 78.3 87.5 69.8 118.4
REMARK 620 6 ASP I 311 OD1 150.4 78.6 121.7 134.9 83.9
REMARK 620 7 ILE I 313 O 114.4 83.4 124.6 78.3 162.1 79.1
REMARK 620 8 HOH I 963 O 134.6 148.2 63.5 66.4 99.9 71.6 80.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA J 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 304 O
REMARK 620 2 ASP J 304 OD1 77.4
REMARK 620 3 ASP J 307 OD1 76.5 151.3
REMARK 620 4 ASP J 307 OD2 80.8 135.0 50.8
REMARK 620 5 LEU J 309 O 75.8 88.9 73.2 122.9
REMARK 620 6 ASP J 311 OD1 148.1 76.0 123.7 130.9 86.5
REMARK 620 7 ILE J 313 O 112.3 76.2 125.3 76.5 160.5 77.8
REMARK 620 8 HOH J 968 O 142.2 139.2 65.7 75.7 92.6 63.4 90.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA I 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA J 801
DBREF1 6QZ2 A 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 A A0A0K8P8E7 1 603
DBREF1 6QZ2 B 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 B A0A0K8P8E7 1 603
DBREF1 6QZ2 C 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 C A0A0K8P8E7 1 603
DBREF1 6QZ2 D 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 D A0A0K8P8E7 1 603
DBREF1 6QZ2 E 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 E A0A0K8P8E7 1 603
DBREF1 6QZ2 F 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 F A0A0K8P8E7 1 603
DBREF1 6QZ2 G 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 G A0A0K8P8E7 1 603
DBREF1 6QZ2 H 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 H A0A0K8P8E7 1 603
DBREF1 6QZ2 I 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 I A0A0K8P8E7 1 603
DBREF1 6QZ2 J 1 603 UNP MHETH_IDESA
DBREF2 6QZ2 J A0A0K8P8E7 1 603
SEQADV 6QZ2 LEU A 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU A 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS A 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU B 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU B 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS B 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU C 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU C 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS C 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU D 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU D 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS D 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU E 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU E 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS E 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU F 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU F 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS F 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU G 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU G 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS G 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU H 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU H 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS H 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU I 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU I 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS I 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 LEU J 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 GLU J 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ2 HIS J 611 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 A 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 A 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 A 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 A 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 A 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 A 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 A 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 A 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 A 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 A 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 A 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 A 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 A 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 A 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 A 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 A 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 A 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 A 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 A 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 A 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 A 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 A 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 A 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 A 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 A 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 A 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 A 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 A 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 A 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 A 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 A 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 A 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 A 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 A 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 A 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 A 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 A 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 A 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 A 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 A 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 A 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 A 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 A 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 A 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 A 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 A 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 B 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 B 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 B 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 B 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 B 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 B 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 B 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 B 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 B 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 B 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 B 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 B 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 B 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 B 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 B 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 B 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 B 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 B 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 B 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 B 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 B 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 B 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 B 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 B 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 B 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 B 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 B 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 B 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 B 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 B 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 B 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 B 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 B 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 B 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 B 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 B 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 B 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 B 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 B 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 B 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 B 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 B 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 B 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 B 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 B 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 B 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 C 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 C 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 C 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 C 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 C 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 C 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 C 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 C 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 C 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 C 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 C 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 C 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 C 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 C 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 C 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 C 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 C 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 C 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 C 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 C 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 C 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 C 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 C 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 C 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 C 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 C 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 C 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 C 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 C 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 C 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 C 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 C 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 C 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 C 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 C 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 C 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 C 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 C 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 C 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 C 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 C 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 C 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 C 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 C 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 C 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 C 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 D 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 D 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 D 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 D 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 D 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 D 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 D 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 D 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 D 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 D 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 D 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 D 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 D 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 D 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 D 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 D 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 D 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 D 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 D 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 D 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 D 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 D 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 D 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 D 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 D 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 D 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 D 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 D 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 D 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 D 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 D 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 D 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 D 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 D 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 D 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 D 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 D 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 D 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 D 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 D 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 D 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 D 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 D 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 D 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 D 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 D 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 E 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 E 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 E 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 E 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 E 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 E 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 E 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 E 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 E 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 E 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 E 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 E 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 E 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 E 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 E 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 E 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 E 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 E 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 E 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 E 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 E 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 E 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 E 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 E 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 E 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 E 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 E 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 E 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 E 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 E 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 E 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 E 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 E 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 E 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 E 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 E 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 E 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 E 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 E 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 E 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 E 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 E 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 E 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 E 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 E 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 E 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 F 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 F 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 F 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 F 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 F 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 F 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 F 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 F 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 F 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 F 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 F 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 F 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 F 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 F 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 F 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 F 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 F 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 F 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 F 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 F 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 F 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 F 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 F 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 F 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 F 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 F 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 F 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 F 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 F 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 F 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 F 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 F 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 F 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 F 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 F 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 F 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 F 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 F 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 F 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 F 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 F 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 F 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 F 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 F 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 F 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 F 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 G 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 G 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 G 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 G 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 G 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 G 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 G 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 G 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 G 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 G 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 G 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 G 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 G 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 G 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 G 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 G 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 G 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 G 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 G 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 G 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 G 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 G 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 G 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 G 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 G 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 G 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 G 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 G 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 G 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 G 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 G 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 G 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 G 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 G 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 G 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 G 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 G 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 G 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 G 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 G 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 G 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 G 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 G 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 G 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 G 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 G 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 H 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 H 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 H 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 H 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 H 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 H 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 H 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 H 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 H 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 H 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 H 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 H 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 H 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 H 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 H 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 H 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 H 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 H 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 H 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 H 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 H 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 H 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 H 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 H 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 H 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 H 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 H 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 H 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 H 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 H 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 H 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 H 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 H 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 H 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 H 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 H 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 H 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 H 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 H 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 H 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 H 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 H 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 H 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 H 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 H 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 H 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 I 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 I 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 I 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 I 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 I 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 I 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 I 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 I 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 I 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 I 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 I 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 I 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 I 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 I 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 I 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 I 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 I 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 I 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 I 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 I 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 I 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 I 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 I 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 I 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 I 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 I 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 I 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 I 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 I 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 I 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 I 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 I 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 I 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 I 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 I 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 I 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 I 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 I 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 I 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 I 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 I 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 I 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 I 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 I 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 I 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 I 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 I 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 J 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 J 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 J 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 J 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 J 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 J 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 J 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 J 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 J 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 J 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 J 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 J 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 J 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 J 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 J 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 J 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 J 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 J 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 J 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 J 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 J 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 J 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 J 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 J 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 J 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 J 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 J 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 J 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 J 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 J 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 J 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 J 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 J 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 J 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 J 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 J 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 J 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 J 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 J 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 J 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 J 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 J 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 J 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 J 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 J 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 J 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 J 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
HET CA A 801 1
HET CA B 801 1
HET CA C 801 1
HET CA D 801 1
HET CA E 801 1
HET CA F 801 1
HET CA G 801 1
HET CA H 801 1
HET CA I 801 1
HET CA J 801 1
HETNAM CA CALCIUM ION
FORMUL 11 CA 10(CA 2+)
FORMUL 21 HOH *6125(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 SER A 286 5 5
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 TRP A 394 LEU A 399 1 6
HELIX 17 AB8 GLY A 414 PHE A 424 1 11
HELIX 18 AB9 PRO A 432 THR A 434 5 3
HELIX 19 AC1 GLN A 435 LYS A 442 1 8
HELIX 20 AC2 ILE A 447 TRP A 453 5 7
HELIX 21 AC3 SER A 462 HIS A 467 1 6
HELIX 22 AC4 LEU A 474 ARG A 480 1 7
HELIX 23 AC5 SER A 496 MET A 511 1 16
HELIX 24 AC6 GLY A 513 GLY A 516 5 4
HELIX 25 AC7 MET A 540 GLY A 551 1 12
HELIX 26 AC8 THR A 563 GLY A 568 5 6
HELIX 27 AC9 THR A 593 ALA A 595 5 3
HELIX 28 AD1 SER B 47 ALA B 53 1 7
HELIX 29 AD2 ALA B 152 ASN B 156 5 5
HELIX 30 AD3 ASN B 173 LEU B 184 5 12
HELIX 31 AD4 ASP B 185 TYR B 194 1 10
HELIX 32 AD5 TYR B 194 GLY B 213 1 20
HELIX 33 AD6 SER B 225 PHE B 238 1 14
HELIX 34 AD7 GLN B 253 PRO B 255 5 3
HELIX 35 AD8 LYS B 256 ALA B 269 1 14
HELIX 36 AD9 PRO B 270 ALA B 272 5 3
HELIX 37 AE1 LEU B 282 SER B 286 5 5
HELIX 38 AE2 SER B 288 ASP B 304 1 17
HELIX 39 AE3 ALA B 305 GLY B 308 5 4
HELIX 40 AE4 ASN B 316 PHE B 324 1 9
HELIX 41 AE5 SER B 350 GLY B 363 1 14
HELIX 42 AE6 ASP B 379 SER B 383 5 5
HELIX 43 AE7 TRP B 394 LEU B 399 1 6
HELIX 44 AE8 GLY B 414 PHE B 424 1 11
HELIX 45 AE9 PRO B 432 THR B 434 5 3
HELIX 46 AF1 GLN B 435 LYS B 442 1 8
HELIX 47 AF2 ILE B 447 TRP B 453 5 7
HELIX 48 AF3 SER B 462 HIS B 467 1 6
HELIX 49 AF4 LEU B 474 ARG B 480 1 7
HELIX 50 AF5 SER B 496 MET B 511 1 16
HELIX 51 AF6 GLY B 513 GLY B 516 5 4
HELIX 52 AF7 MET B 540 GLY B 551 1 12
HELIX 53 AF8 THR B 563 GLY B 568 5 6
HELIX 54 AF9 THR B 593 ALA B 595 5 3
HELIX 55 AG1 SER C 47 ALA C 53 1 7
HELIX 56 AG2 ALA C 152 ASN C 156 5 5
HELIX 57 AG3 LEU C 177 LEU C 184 5 8
HELIX 58 AG4 ASP C 185 TYR C 194 1 10
HELIX 59 AG5 TYR C 194 GLY C 213 1 20
HELIX 60 AG6 SER C 225 PHE C 238 1 14
HELIX 61 AG7 GLN C 253 PRO C 255 5 3
HELIX 62 AG8 LYS C 256 ALA C 269 1 14
HELIX 63 AG9 PRO C 270 ALA C 272 5 3
HELIX 64 AH1 LEU C 282 SER C 286 5 5
HELIX 65 AH2 SER C 288 ASP C 304 1 17
HELIX 66 AH3 ALA C 305 GLY C 308 5 4
HELIX 67 AH4 ASN C 316 PHE C 324 1 9
HELIX 68 AH5 SER C 350 GLY C 363 1 14
HELIX 69 AH6 ASP C 379 SER C 383 5 5
HELIX 70 AH7 TRP C 394 LEU C 399 1 6
HELIX 71 AH8 GLY C 414 PHE C 424 1 11
HELIX 72 AH9 PRO C 432 THR C 434 5 3
HELIX 73 AI1 GLN C 435 LYS C 442 1 8
HELIX 74 AI2 ILE C 447 TRP C 453 5 7
HELIX 75 AI3 SER C 462 GLY C 468 1 7
HELIX 76 AI4 LEU C 474 ARG C 480 1 7
HELIX 77 AI5 SER C 496 MET C 511 1 16
HELIX 78 AI6 GLY C 513 GLY C 516 5 4
HELIX 79 AI7 MET C 540 GLY C 551 1 12
HELIX 80 AI8 THR C 563 GLY C 568 5 6
HELIX 81 AI9 THR C 593 ALA C 595 5 3
HELIX 82 AJ1 SER D 47 ALA D 53 1 7
HELIX 83 AJ2 ALA D 152 ASN D 156 5 5
HELIX 84 AJ3 LEU D 177 LEU D 184 5 8
HELIX 85 AJ4 ASP D 185 TYR D 194 1 10
HELIX 86 AJ5 TYR D 194 GLY D 213 1 20
HELIX 87 AJ6 SER D 225 PHE D 238 1 14
HELIX 88 AJ7 GLN D 253 PRO D 255 5 3
HELIX 89 AJ8 LYS D 256 ALA D 269 1 14
HELIX 90 AJ9 PRO D 270 ALA D 272 5 3
HELIX 91 AK1 LEU D 282 SER D 286 5 5
HELIX 92 AK2 SER D 288 ASP D 304 1 17
HELIX 93 AK3 ALA D 305 GLY D 308 5 4
HELIX 94 AK4 ASN D 316 PHE D 324 1 9
HELIX 95 AK5 SER D 350 GLY D 363 1 14
HELIX 96 AK6 ASP D 379 SER D 383 5 5
HELIX 97 AK7 TRP D 394 LEU D 399 1 6
HELIX 98 AK8 GLY D 414 PHE D 424 1 11
HELIX 99 AK9 PRO D 432 THR D 434 5 3
HELIX 100 AL1 GLN D 435 PHE D 443 1 9
HELIX 101 AL2 ILE D 447 TRP D 453 5 7
HELIX 102 AL3 SER D 462 HIS D 467 1 6
HELIX 103 AL4 LEU D 474 ARG D 480 1 7
HELIX 104 AL5 SER D 496 MET D 511 1 16
HELIX 105 AL6 GLY D 513 GLY D 516 5 4
HELIX 106 AL7 MET D 540 GLY D 551 1 12
HELIX 107 AL8 THR D 563 GLY D 568 5 6
HELIX 108 AL9 THR D 593 ALA D 595 5 3
HELIX 109 AM1 SER E 47 ALA E 53 1 7
HELIX 110 AM2 ALA E 152 ASN E 156 5 5
HELIX 111 AM3 LEU E 177 LEU E 184 5 8
HELIX 112 AM4 ASP E 185 TYR E 194 1 10
HELIX 113 AM5 TYR E 194 GLY E 213 1 20
HELIX 114 AM6 SER E 225 PHE E 238 1 14
HELIX 115 AM7 GLN E 253 PRO E 255 5 3
HELIX 116 AM8 LYS E 256 ALA E 269 1 14
HELIX 117 AM9 PRO E 270 ALA E 272 5 3
HELIX 118 AN1 LEU E 282 PHE E 287 5 6
HELIX 119 AN2 SER E 288 ASP E 304 1 17
HELIX 120 AN3 ALA E 305 GLY E 308 5 4
HELIX 121 AN4 ASN E 316 PHE E 324 1 9
HELIX 122 AN5 SER E 350 GLY E 363 1 14
HELIX 123 AN6 ASP E 379 SER E 383 5 5
HELIX 124 AN7 TRP E 394 LEU E 399 1 6
HELIX 125 AN8 GLY E 414 PHE E 424 1 11
HELIX 126 AN9 PRO E 432 THR E 434 5 3
HELIX 127 AO1 GLN E 435 LYS E 442 1 8
HELIX 128 AO2 ILE E 447 TRP E 453 5 7
HELIX 129 AO3 SER E 462 GLY E 468 1 7
HELIX 130 AO4 LEU E 474 ARG E 480 1 7
HELIX 131 AO5 SER E 496 MET E 511 1 16
HELIX 132 AO6 GLY E 513 GLY E 516 5 4
HELIX 133 AO7 MET E 540 GLY E 551 1 12
HELIX 134 AO8 THR E 563 GLY E 568 5 6
HELIX 135 AO9 THR E 593 ALA E 595 5 3
HELIX 136 AP1 SER F 47 ALA F 53 1 7
HELIX 137 AP2 LEU F 177 LEU F 184 5 8
HELIX 138 AP3 ASP F 185 TYR F 194 1 10
HELIX 139 AP4 TYR F 194 GLY F 213 1 20
HELIX 140 AP5 SER F 225 PHE F 238 1 14
HELIX 141 AP6 GLN F 253 PRO F 255 5 3
HELIX 142 AP7 LYS F 256 ALA F 269 1 14
HELIX 143 AP8 PRO F 270 ALA F 272 5 3
HELIX 144 AP9 LEU F 282 SER F 286 5 5
HELIX 145 AQ1 SER F 288 ASP F 304 1 17
HELIX 146 AQ2 ALA F 305 GLY F 308 5 4
HELIX 147 AQ3 ASN F 316 PHE F 324 1 9
HELIX 148 AQ4 SER F 350 GLY F 363 1 14
HELIX 149 AQ5 ASP F 379 SER F 383 5 5
HELIX 150 AQ6 TRP F 394 LEU F 399 1 6
HELIX 151 AQ7 GLY F 414 PHE F 424 1 11
HELIX 152 AQ8 PRO F 432 THR F 434 5 3
HELIX 153 AQ9 GLN F 435 LYS F 442 1 8
HELIX 154 AR1 ILE F 447 TRP F 453 5 7
HELIX 155 AR2 SER F 462 GLY F 468 1 7
HELIX 156 AR3 LEU F 474 ARG F 480 1 7
HELIX 157 AR4 SER F 496 MET F 511 1 16
HELIX 158 AR5 GLY F 513 GLY F 516 5 4
HELIX 159 AR6 MET F 540 GLY F 551 1 12
HELIX 160 AR7 THR F 563 GLY F 568 5 6
HELIX 161 AR8 THR F 593 ALA F 595 5 3
HELIX 162 AR9 SER G 47 LEU G 54 1 8
HELIX 163 AS1 ALA G 152 ASN G 156 5 5
HELIX 164 AS2 LEU G 177 LEU G 184 5 8
HELIX 165 AS3 ASP G 185 TYR G 194 1 10
HELIX 166 AS4 TYR G 194 GLY G 213 1 20
HELIX 167 AS5 SER G 225 PHE G 238 1 14
HELIX 168 AS6 GLN G 253 PRO G 255 5 3
HELIX 169 AS7 LYS G 256 ALA G 269 1 14
HELIX 170 AS8 PRO G 270 ALA G 272 5 3
HELIX 171 AS9 LEU G 282 PHE G 287 5 6
HELIX 172 AT1 SER G 288 ASP G 304 1 17
HELIX 173 AT2 ALA G 305 GLY G 308 5 4
HELIX 174 AT3 ASN G 316 PHE G 324 1 9
HELIX 175 AT4 SER G 350 GLY G 363 1 14
HELIX 176 AT5 ASP G 379 SER G 383 5 5
HELIX 177 AT6 TRP G 394 LEU G 399 1 6
HELIX 178 AT7 GLY G 414 PHE G 424 1 11
HELIX 179 AT8 PRO G 432 THR G 434 5 3
HELIX 180 AT9 GLN G 435 LYS G 442 1 8
HELIX 181 AU1 ILE G 447 TRP G 453 5 7
HELIX 182 AU2 SER G 462 GLY G 468 1 7
HELIX 183 AU3 LEU G 474 ARG G 480 1 7
HELIX 184 AU4 SER G 496 MET G 511 1 16
HELIX 185 AU5 GLY G 513 GLY G 516 5 4
HELIX 186 AU6 MET G 540 GLY G 551 1 12
HELIX 187 AU7 THR G 563 GLY G 568 5 6
HELIX 188 AU8 THR G 593 ALA G 595 5 3
HELIX 189 AU9 SER H 47 LEU H 54 1 8
HELIX 190 AV1 ALA H 152 ASN H 156 5 5
HELIX 191 AV2 LEU H 177 LEU H 184 5 8
HELIX 192 AV3 ASP H 185 TYR H 194 1 10
HELIX 193 AV4 TYR H 194 GLY H 213 1 20
HELIX 194 AV5 SER H 225 PHE H 238 1 14
HELIX 195 AV6 GLN H 253 PRO H 255 5 3
HELIX 196 AV7 LYS H 256 ALA H 269 1 14
HELIX 197 AV8 PRO H 270 ALA H 272 5 3
HELIX 198 AV9 LEU H 282 SER H 286 5 5
HELIX 199 AW1 SER H 288 ASP H 304 1 17
HELIX 200 AW2 ALA H 305 GLY H 308 5 4
HELIX 201 AW3 ASN H 316 PHE H 324 1 9
HELIX 202 AW4 SER H 350 GLY H 363 1 14
HELIX 203 AW5 ASP H 379 SER H 383 5 5
HELIX 204 AW6 TRP H 394 LEU H 399 1 6
HELIX 205 AW7 GLY H 414 ASP H 423 1 10
HELIX 206 AW8 PRO H 432 THR H 434 5 3
HELIX 207 AW9 GLN H 435 LYS H 442 1 8
HELIX 208 AX1 ILE H 447 TRP H 453 5 7
HELIX 209 AX2 SER H 462 HIS H 467 1 6
HELIX 210 AX3 LEU H 474 ARG H 480 1 7
HELIX 211 AX4 SER H 496 MET H 511 1 16
HELIX 212 AX5 GLY H 513 GLY H 516 5 4
HELIX 213 AX6 MET H 540 GLY H 551 1 12
HELIX 214 AX7 THR H 563 GLY H 568 5 6
HELIX 215 AX8 THR H 593 ALA H 595 5 3
HELIX 216 AX9 SER I 47 ALA I 53 1 7
HELIX 217 AY1 LEU I 177 LEU I 184 5 8
HELIX 218 AY2 ASP I 185 TYR I 194 1 10
HELIX 219 AY3 TYR I 194 GLY I 213 1 20
HELIX 220 AY4 SER I 225 PHE I 238 1 14
HELIX 221 AY5 GLN I 253 PRO I 255 5 3
HELIX 222 AY6 LYS I 256 ALA I 269 1 14
HELIX 223 AY7 PRO I 270 ALA I 272 5 3
HELIX 224 AY8 LEU I 282 SER I 286 5 5
HELIX 225 AY9 SER I 288 ASP I 304 1 17
HELIX 226 AZ1 ALA I 305 GLY I 308 5 4
HELIX 227 AZ2 ASN I 316 PHE I 324 1 9
HELIX 228 AZ3 SER I 350 GLY I 363 1 14
HELIX 229 AZ4 ASP I 379 SER I 383 5 5
HELIX 230 AZ5 TRP I 394 LEU I 399 1 6
HELIX 231 AZ6 GLY I 414 PHE I 424 1 11
HELIX 232 AZ7 PRO I 432 THR I 434 5 3
HELIX 233 AZ8 GLN I 435 LYS I 442 1 8
HELIX 234 AZ9 ILE I 447 TRP I 453 5 7
HELIX 235 BA1 SER I 462 GLY I 468 1 7
HELIX 236 BA2 LEU I 474 ARG I 480 1 7
HELIX 237 BA3 SER I 496 MET I 511 1 16
HELIX 238 BA4 GLY I 513 GLY I 516 5 4
HELIX 239 BA5 MET I 540 GLY I 551 1 12
HELIX 240 BA6 THR I 563 GLY I 568 5 6
HELIX 241 BA7 THR I 593 ALA I 595 5 3
HELIX 242 BA8 SER J 47 GLU J 52 1 6
HELIX 243 BA9 ALA J 53 LYS J 55 5 3
HELIX 244 BB1 ALA J 152 ASN J 156 5 5
HELIX 245 BB2 LEU J 177 LEU J 184 5 8
HELIX 246 BB3 ASP J 185 TYR J 194 1 10
HELIX 247 BB4 TYR J 194 TYR J 212 1 19
HELIX 248 BB5 SER J 225 PHE J 238 1 14
HELIX 249 BB6 GLN J 253 PRO J 255 5 3
HELIX 250 BB7 LYS J 256 ALA J 269 1 14
HELIX 251 BB8 PRO J 270 ALA J 272 5 3
HELIX 252 BB9 LEU J 282 PHE J 287 5 6
HELIX 253 BC1 SER J 288 ASP J 304 1 17
HELIX 254 BC2 ALA J 305 GLY J 308 5 4
HELIX 255 BC3 ASN J 316 PHE J 324 1 9
HELIX 256 BC4 SER J 350 GLY J 363 1 14
HELIX 257 BC5 ASP J 379 SER J 383 5 5
HELIX 258 BC6 TRP J 394 LEU J 399 1 6
HELIX 259 BC7 GLY J 414 ASP J 423 1 10
HELIX 260 BC8 PRO J 432 THR J 434 5 3
HELIX 261 BC9 GLN J 435 PHE J 443 1 9
HELIX 262 BD1 ILE J 447 TRP J 453 5 7
HELIX 263 BD2 SER J 462 HIS J 467 1 6
HELIX 264 BD3 LEU J 474 ARG J 480 1 7
HELIX 265 BD4 SER J 496 MET J 511 1 16
HELIX 266 BD5 GLY J 513 GLY J 516 5 4
HELIX 267 BD6 MET J 540 GLY J 551 1 12
HELIX 268 BD7 THR J 563 GLY J 568 5 6
HELIX 269 BD8 THR J 593 ALA J 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O HIS A 91 N ARG A 76
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O VAL A 523 N HIS A 488
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 600 N ILE A 582
SHEET 1 AA5 9 THR B 68 ARG B 76 0
SHEET 2 AA5 9 HIS B 91 THR B 102 -1 O HIS B 91 N ARG B 76
SHEET 3 AA5 9 PRO B 108 PRO B 118 -1 O LEU B 115 N VAL B 94
SHEET 4 AA5 9 ALA B 158 THR B 162 -1 O THR B 159 N ARG B 116
SHEET 5 AA5 9 ARG B 124 GLU B 128 1 N PHE B 126 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O ARG B 519 N LEU B 486
SHEET 1 AA6 2 LEU B 385 SER B 386 0
SHEET 2 AA6 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA7 2 ILE B 557 TRP B 560 0
SHEET 2 AA7 2 THR B 573 LEU B 576 -1 O LEU B 576 N ILE B 557
SHEET 1 AA8 2 ILE B 582 TYR B 585 0
SHEET 2 AA8 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SHEET 1 AA9 9 THR C 68 ARG C 76 0
SHEET 2 AA9 9 HIS C 91 THR C 102 -1 O HIS C 91 N ARG C 76
SHEET 3 AA9 9 PRO C 108 PRO C 118 -1 O LEU C 115 N VAL C 94
SHEET 4 AA9 9 ALA C 158 THR C 162 -1 O THR C 159 N ARG C 116
SHEET 5 AA9 9 ARG C 124 GLU C 128 1 N ARG C 124 O ALA C 158
SHEET 6 AA9 9 LYS C 218 CYS C 224 1 O TYR C 220 N PHE C 125
SHEET 7 AA9 9 GLY C 244 GLY C 248 1 O GLY C 248 N GLY C 223
SHEET 8 AA9 9 LYS C 483 GLY C 489 1 O ILE C 485 N ILE C 245
SHEET 9 AA9 9 ALA C 518 VAL C 523 1 O ARG C 519 N LEU C 486
SHEET 1 AB1 2 LEU C 385 SER C 386 0
SHEET 2 AB1 2 THR C 389 TYR C 390 -1 O THR C 389 N SER C 386
SHEET 1 AB2 2 ILE C 557 TRP C 560 0
SHEET 2 AB2 2 THR C 573 LEU C 576 -1 O LEU C 576 N ILE C 557
SHEET 1 AB3 2 ILE C 582 TYR C 585 0
SHEET 2 AB3 2 PHE C 597 ALA C 600 -1 O ALA C 600 N ILE C 582
SHEET 1 AB4 9 THR D 68 ARG D 76 0
SHEET 2 AB4 9 HIS D 91 THR D 102 -1 O HIS D 91 N ARG D 76
SHEET 3 AB4 9 PRO D 108 PRO D 118 -1 O LEU D 115 N VAL D 94
SHEET 4 AB4 9 ALA D 158 THR D 162 -1 O THR D 159 N ARG D 116
SHEET 5 AB4 9 ARG D 124 GLU D 128 1 N PHE D 126 O ALA D 158
SHEET 6 AB4 9 LYS D 218 CYS D 224 1 O TYR D 220 N PHE D 125
SHEET 7 AB4 9 GLY D 244 GLY D 248 1 O GLY D 248 N GLY D 223
SHEET 8 AB4 9 LYS D 483 GLY D 489 1 O ILE D 485 N ILE D 245
SHEET 9 AB4 9 ALA D 518 VAL D 523 1 O ARG D 519 N LEU D 486
SHEET 1 AB5 2 LEU D 385 SER D 386 0
SHEET 2 AB5 2 THR D 389 TYR D 390 -1 O THR D 389 N SER D 386
SHEET 1 AB6 3 ARG D 537 PHE D 538 0
SHEET 2 AB6 3 ILE D 557 TRP D 560 -1 O TRP D 560 N ARG D 537
SHEET 3 AB6 3 THR D 573 LEU D 576 -1 O LEU D 576 N ILE D 557
SHEET 1 AB7 2 ILE D 582 TYR D 585 0
SHEET 2 AB7 2 PHE D 597 ALA D 600 -1 O ALA D 600 N ILE D 582
SHEET 1 AB8 9 THR E 68 ARG E 76 0
SHEET 2 AB8 9 HIS E 91 THR E 102 -1 O HIS E 91 N ARG E 76
SHEET 3 AB8 9 PRO E 108 PRO E 118 -1 O LEU E 115 N VAL E 94
SHEET 4 AB8 9 ALA E 158 THR E 162 -1 O THR E 159 N ARG E 116
SHEET 5 AB8 9 ARG E 124 GLU E 128 1 N PHE E 126 O ALA E 158
SHEET 6 AB8 9 LYS E 218 CYS E 224 1 O TYR E 220 N PHE E 125
SHEET 7 AB8 9 GLY E 244 GLY E 248 1 O GLY E 248 N GLY E 223
SHEET 8 AB8 9 LYS E 483 GLY E 489 1 O ILE E 485 N ILE E 245
SHEET 9 AB8 9 ALA E 518 VAL E 523 1 O ARG E 519 N LEU E 486
SHEET 1 AB9 2 LEU E 385 SER E 386 0
SHEET 2 AB9 2 THR E 389 TYR E 390 -1 O THR E 389 N SER E 386
SHEET 1 AC1 2 ILE E 557 TRP E 560 0
SHEET 2 AC1 2 THR E 573 LEU E 576 -1 O LEU E 576 N ILE E 557
SHEET 1 AC2 2 ILE E 582 TYR E 585 0
SHEET 2 AC2 2 PHE E 597 ALA E 600 -1 O ALA E 600 N ILE E 582
SHEET 1 AC3 9 THR F 68 ARG F 76 0
SHEET 2 AC3 9 HIS F 91 THR F 102 -1 O HIS F 91 N ARG F 76
SHEET 3 AC3 9 PRO F 108 PRO F 118 -1 O LEU F 115 N VAL F 94
SHEET 4 AC3 9 ALA F 158 THR F 162 -1 O THR F 159 N ARG F 116
SHEET 5 AC3 9 ARG F 124 GLU F 128 1 N ARG F 124 O ALA F 158
SHEET 6 AC3 9 LYS F 218 CYS F 224 1 O TYR F 220 N PHE F 125
SHEET 7 AC3 9 GLY F 244 GLY F 248 1 O GLY F 248 N GLY F 223
SHEET 8 AC3 9 LYS F 483 GLY F 489 1 O ILE F 485 N ILE F 245
SHEET 9 AC3 9 ALA F 518 VAL F 523 1 O ARG F 519 N LEU F 486
SHEET 1 AC4 2 LEU F 385 SER F 386 0
SHEET 2 AC4 2 THR F 389 TYR F 390 -1 O THR F 389 N SER F 386
SHEET 1 AC5 2 ILE F 557 TRP F 560 0
SHEET 2 AC5 2 THR F 573 LEU F 576 -1 O LEU F 576 N ILE F 557
SHEET 1 AC6 2 ILE F 582 TYR F 585 0
SHEET 2 AC6 2 PHE F 597 ALA F 600 -1 O ALA F 600 N ILE F 582
SHEET 1 AC7 9 THR G 68 ARG G 76 0
SHEET 2 AC7 9 HIS G 91 THR G 102 -1 O HIS G 91 N ARG G 76
SHEET 3 AC7 9 PRO G 108 PRO G 118 -1 O LEU G 115 N VAL G 94
SHEET 4 AC7 9 ALA G 158 THR G 162 -1 O THR G 159 N ARG G 116
SHEET 5 AC7 9 ARG G 124 GLU G 128 1 N PHE G 126 O ALA G 158
SHEET 6 AC7 9 LYS G 218 CYS G 224 1 O TYR G 220 N PHE G 125
SHEET 7 AC7 9 GLY G 244 GLY G 248 1 O GLY G 248 N GLY G 223
SHEET 8 AC7 9 LYS G 483 GLY G 489 1 O ILE G 485 N ILE G 245
SHEET 9 AC7 9 ALA G 518 VAL G 523 1 O ARG G 519 N LEU G 486
SHEET 1 AC8 2 LEU G 385 SER G 386 0
SHEET 2 AC8 2 THR G 389 TYR G 390 -1 O THR G 389 N SER G 386
SHEET 1 AC9 2 ILE G 557 TRP G 560 0
SHEET 2 AC9 2 THR G 573 LEU G 576 -1 O ARG G 574 N ALA G 559
SHEET 1 AD1 2 ILE G 582 TYR G 585 0
SHEET 2 AD1 2 PHE G 597 ALA G 600 -1 O ALA G 600 N ILE G 582
SHEET 1 AD2 9 THR H 68 ARG H 76 0
SHEET 2 AD2 9 HIS H 91 THR H 102 -1 O ALA H 97 N VAL H 69
SHEET 3 AD2 9 PRO H 108 PRO H 118 -1 O LEU H 115 N VAL H 94
SHEET 4 AD2 9 ALA H 158 THR H 162 -1 O THR H 159 N ARG H 116
SHEET 5 AD2 9 ARG H 124 GLU H 128 1 N PHE H 126 O ALA H 158
SHEET 6 AD2 9 LYS H 218 CYS H 224 1 O TYR H 220 N PHE H 125
SHEET 7 AD2 9 GLY H 244 GLY H 248 1 O GLY H 248 N GLY H 223
SHEET 8 AD2 9 LYS H 483 GLY H 489 1 O ILE H 485 N ILE H 245
SHEET 9 AD2 9 ALA H 518 VAL H 523 1 O ARG H 519 N LEU H 486
SHEET 1 AD3 2 LEU H 385 SER H 386 0
SHEET 2 AD3 2 THR H 389 TYR H 390 -1 O THR H 389 N SER H 386
SHEET 1 AD4 2 ILE H 557 TRP H 560 0
SHEET 2 AD4 2 THR H 573 LEU H 576 -1 O LEU H 576 N ILE H 557
SHEET 1 AD5 2 ILE H 582 TYR H 585 0
SHEET 2 AD5 2 PHE H 597 ALA H 600 -1 O ALA H 600 N ILE H 582
SHEET 1 AD6 9 THR I 68 ARG I 76 0
SHEET 2 AD6 9 HIS I 91 THR I 102 -1 O HIS I 91 N ARG I 76
SHEET 3 AD6 9 PRO I 108 PRO I 118 -1 O LEU I 115 N VAL I 94
SHEET 4 AD6 9 ALA I 158 THR I 162 -1 O THR I 159 N ARG I 116
SHEET 5 AD6 9 ARG I 124 GLU I 128 1 N PHE I 126 O ALA I 158
SHEET 6 AD6 9 LYS I 218 CYS I 224 1 O TYR I 220 N PHE I 125
SHEET 7 AD6 9 GLY I 244 GLY I 248 1 O GLY I 248 N GLY I 223
SHEET 8 AD6 9 LYS I 483 GLY I 489 1 O ILE I 485 N ILE I 245
SHEET 9 AD6 9 ALA I 518 VAL I 523 1 O ARG I 519 N LEU I 486
SHEET 1 AD7 2 LEU I 385 SER I 386 0
SHEET 2 AD7 2 THR I 389 TYR I 390 -1 O THR I 389 N SER I 386
SHEET 1 AD8 2 ILE I 557 TRP I 560 0
SHEET 2 AD8 2 THR I 573 LEU I 576 -1 O LEU I 576 N ILE I 557
SHEET 1 AD9 2 ILE I 582 TYR I 585 0
SHEET 2 AD9 2 PHE I 597 ALA I 600 -1 O ALA I 600 N ILE I 582
SHEET 1 AE1 9 THR J 68 ARG J 76 0
SHEET 2 AE1 9 HIS J 91 THR J 102 -1 O HIS J 91 N ARG J 76
SHEET 3 AE1 9 PRO J 108 PRO J 118 -1 O LEU J 115 N VAL J 94
SHEET 4 AE1 9 ALA J 158 THR J 162 -1 O THR J 159 N ARG J 116
SHEET 5 AE1 9 ARG J 124 GLU J 128 1 N PHE J 126 O ALA J 158
SHEET 6 AE1 9 LYS J 218 CYS J 224 1 O TYR J 220 N PHE J 125
SHEET 7 AE1 9 GLY J 244 GLY J 248 1 O VAL J 246 N PHE J 221
SHEET 8 AE1 9 LYS J 483 GLY J 489 1 O LYS J 483 N ILE J 245
SHEET 9 AE1 9 ALA J 518 VAL J 523 1 O ARG J 519 N LEU J 486
SHEET 1 AE2 2 LEU J 385 SER J 386 0
SHEET 2 AE2 2 THR J 389 TYR J 390 -1 O THR J 389 N SER J 386
SHEET 1 AE3 3 ARG J 537 PHE J 538 0
SHEET 2 AE3 3 ILE J 557 TRP J 560 -1 O TRP J 560 N ARG J 537
SHEET 3 AE3 3 THR J 573 LEU J 576 -1 O LEU J 576 N ILE J 557
SHEET 1 AE4 2 ILE J 582 TYR J 585 0
SHEET 2 AE4 2 PHE J 597 ALA J 600 -1 O ALA J 600 N ILE J 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.05
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.04
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.04
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.04
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.04
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.04
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.04
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.03
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.04
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.04
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.05
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.04
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.03
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.04
SSBOND 16 CYS D 51 CYS D 92 1555 1555 2.04
SSBOND 17 CYS D 224 CYS D 529 1555 1555 2.05
SSBOND 18 CYS D 303 CYS D 320 1555 1555 2.04
SSBOND 19 CYS D 340 CYS D 348 1555 1555 2.03
SSBOND 20 CYS D 577 CYS D 599 1555 1555 2.03
SSBOND 21 CYS E 51 CYS E 92 1555 1555 2.04
SSBOND 22 CYS E 224 CYS E 529 1555 1555 2.05
SSBOND 23 CYS E 303 CYS E 320 1555 1555 2.04
SSBOND 24 CYS E 340 CYS E 348 1555 1555 2.03
SSBOND 25 CYS E 577 CYS E 599 1555 1555 2.04
SSBOND 26 CYS F 51 CYS F 92 1555 1555 2.04
SSBOND 27 CYS F 224 CYS F 529 1555 1555 2.05
SSBOND 28 CYS F 303 CYS F 320 1555 1555 2.04
SSBOND 29 CYS F 340 CYS F 348 1555 1555 2.03
SSBOND 30 CYS F 577 CYS F 599 1555 1555 2.04
SSBOND 31 CYS G 51 CYS G 92 1555 1555 2.03
SSBOND 32 CYS G 224 CYS G 529 1555 1555 2.05
SSBOND 33 CYS G 303 CYS G 320 1555 1555 2.04
SSBOND 34 CYS G 340 CYS G 348 1555 1555 2.03
SSBOND 35 CYS G 577 CYS G 599 1555 1555 2.03
SSBOND 36 CYS H 51 CYS H 92 1555 1555 2.03
SSBOND 37 CYS H 224 CYS H 529 1555 1555 2.05
SSBOND 38 CYS H 303 CYS H 320 1555 1555 2.04
SSBOND 39 CYS H 340 CYS H 348 1555 1555 2.03
SSBOND 40 CYS H 577 CYS H 599 1555 1555 2.03
SSBOND 41 CYS I 51 CYS I 92 1555 1555 2.03
SSBOND 42 CYS I 224 CYS I 529 1555 1555 2.04
SSBOND 43 CYS I 303 CYS I 320 1555 1555 2.09
SSBOND 44 CYS I 340 CYS I 348 1555 1555 2.03
SSBOND 45 CYS I 577 CYS I 599 1555 1555 2.04
SSBOND 46 CYS J 51 CYS J 92 1555 1555 2.03
SSBOND 47 CYS J 224 CYS J 529 1555 1555 2.04
SSBOND 48 CYS J 303 CYS J 320 1555 1555 2.03
SSBOND 49 CYS J 340 CYS J 348 1555 1555 2.03
SSBOND 50 CYS J 577 CYS J 599 1555 1555 2.03
LINK O ASP A 304 CA CA A 801 1555 1555 2.50
LINK OD1 ASP A 304 CA CA A 801 1555 1555 2.48
LINK OD1 ASP A 307 CA CA A 801 1555 1555 2.63
LINK OD2 ASP A 307 CA CA A 801 1555 1555 2.42
LINK O LEU A 309 CA CA A 801 1555 1555 2.38
LINK OD1 ASP A 311 CA CA A 801 1555 1555 2.57
LINK O ILE A 313 CA CA A 801 1555 1555 2.36
LINK CA CA A 801 O HOH A 911 1555 1555 2.50
LINK O ASP B 304 CA CA B 801 1555 1555 2.45
LINK OD1 ASP B 304 CA CA B 801 1555 1555 2.49
LINK OD1 ASP B 307 CA CA B 801 1555 1555 2.66
LINK OD2 ASP B 307 CA CA B 801 1555 1555 2.52
LINK O LEU B 309 CA CA B 801 1555 1555 2.42
LINK OD1 ASP B 311 CA CA B 801 1555 1555 2.59
LINK O ILE B 313 CA CA B 801 1555 1555 2.44
LINK CA CA B 801 O HOH B1034 1555 1555 2.46
LINK O ASP C 304 CA CA C 801 1555 1555 2.52
LINK OD1 ASP C 304 CA CA C 801 1555 1555 2.39
LINK OD1 ASP C 307 CA CA C 801 1555 1555 2.55
LINK OD2 ASP C 307 CA CA C 801 1555 1555 2.57
LINK O LEU C 309 CA CA C 801 1555 1555 2.41
LINK OD1 ASP C 311 CA CA C 801 1555 1555 2.48
LINK O ILE C 313 CA CA C 801 1555 1555 2.36
LINK CA CA C 801 O HOH C 943 1555 1555 2.64
LINK O ASP D 304 CA CA D 801 1555 1555 2.43
LINK OD1 ASP D 304 CA CA D 801 1555 1555 2.44
LINK OD1 ASP D 307 CA CA D 801 1555 1555 2.63
LINK OD2 ASP D 307 CA CA D 801 1555 1555 2.55
LINK O LEU D 309 CA CA D 801 1555 1555 2.35
LINK OD1 ASP D 311 CA CA D 801 1555 1555 2.50
LINK O ILE D 313 CA CA D 801 1555 1555 2.45
LINK CA CA D 801 O HOH D1027 1555 1555 2.46
LINK O ASP E 304 CA CA E 801 1555 1555 2.48
LINK OD1 ASP E 304 CA CA E 801 1555 1555 2.50
LINK OD1 ASP E 307 CA CA E 801 1555 1555 2.62
LINK OD2 ASP E 307 CA CA E 801 1555 1555 2.49
LINK O LEU E 309 CA CA E 801 1555 1555 2.35
LINK OD1 ASP E 311 CA CA E 801 1555 1555 2.53
LINK O ILE E 313 CA CA E 801 1555 1555 2.41
LINK CA CA E 801 O HOH E 915 1555 1555 2.55
LINK O ASP F 304 CA CA F 801 1555 1555 2.51
LINK OD1 ASP F 304 CA CA F 801 1555 1555 2.44
LINK OD1 ASP F 307 CA CA F 801 1555 1555 2.61
LINK OD2 ASP F 307 CA CA F 801 1555 1555 2.51
LINK O LEU F 309 CA CA F 801 1555 1555 2.45
LINK OD1 ASP F 311 CA CA F 801 1555 1555 2.51
LINK O ILE F 313 CA CA F 801 1555 1555 2.30
LINK CA CA F 801 O HOH F 933 1555 1555 2.46
LINK O ASP G 304 CA CA G 801 1555 1555 2.57
LINK OD1 ASP G 304 CA CA G 801 1555 1555 2.48
LINK OD1 ASP G 307 CA CA G 801 1555 1555 2.50
LINK OD2 ASP G 307 CA CA G 801 1555 1555 2.56
LINK O LEU G 309 CA CA G 801 1555 1555 2.32
LINK OD1 ASP G 311 CA CA G 801 1555 1555 2.51
LINK O ILE G 313 CA CA G 801 1555 1555 2.45
LINK CA CA G 801 O HOH G 962 1555 1555 2.50
LINK O ASP H 304 CA CA H 801 1555 1555 2.47
LINK OD1 ASP H 304 CA CA H 801 1555 1555 2.38
LINK OD1 ASP H 307 CA CA H 801 1555 1555 2.50
LINK OD2 ASP H 307 CA CA H 801 1555 1555 2.54
LINK O LEU H 309 CA CA H 801 1555 1555 2.35
LINK OD1 ASP H 311 CA CA H 801 1555 1555 2.62
LINK O ILE H 313 CA CA H 801 1555 1555 2.39
LINK CA CA H 801 O HOH H 969 1555 1555 2.44
LINK O ASP I 304 CA CA I 801 1555 1555 2.30
LINK OD1 ASP I 304 CA CA I 801 1555 1555 2.21
LINK OD1 ASP I 307 CA CA I 801 1555 1555 2.65
LINK OD2 ASP I 307 CA CA I 801 1555 1555 2.55
LINK O LEU I 309 CA CA I 801 1555 1555 2.32
LINK OD1 ASP I 311 CA CA I 801 1555 1555 2.56
LINK O ILE I 313 CA CA I 801 1555 1555 2.40
LINK CA CA I 801 O HOH I 963 1555 1555 2.06
LINK O ASP J 304 CA CA J 801 1555 1555 2.40
LINK OD1 ASP J 304 CA CA J 801 1555 1555 2.40
LINK OD1 ASP J 307 CA CA J 801 1555 1555 2.57
LINK OD2 ASP J 307 CA CA J 801 1555 1555 2.55
LINK O LEU J 309 CA CA J 801 1555 1555 2.34
LINK OD1 ASP J 311 CA CA J 801 1555 1555 2.70
LINK O ILE J 313 CA CA J 801 1555 1555 2.30
LINK CA CA J 801 O HOH J 968 1555 1555 2.15
CISPEP 1 THR A 426 PRO A 427 0 -1.02
CISPEP 2 TYR A 579 PRO A 580 0 5.36
CISPEP 3 THR B 426 PRO B 427 0 -2.44
CISPEP 4 TYR B 579 PRO B 580 0 3.82
CISPEP 5 THR C 426 PRO C 427 0 -2.21
CISPEP 6 TYR C 579 PRO C 580 0 5.61
CISPEP 7 THR D 426 PRO D 427 0 -0.96
CISPEP 8 TYR D 579 PRO D 580 0 2.93
CISPEP 9 THR E 426 PRO E 427 0 -0.82
CISPEP 10 TYR E 579 PRO E 580 0 3.34
CISPEP 11 THR F 426 PRO F 427 0 -2.48
CISPEP 12 TYR F 579 PRO F 580 0 5.50
CISPEP 13 THR G 426 PRO G 427 0 -0.06
CISPEP 14 TYR G 579 PRO G 580 0 3.79
CISPEP 15 THR H 426 PRO H 427 0 -0.24
CISPEP 16 TYR H 579 PRO H 580 0 3.03
CISPEP 17 THR I 426 PRO I 427 0 -0.51
CISPEP 18 TYR I 579 PRO I 580 0 2.04
CISPEP 19 THR J 426 PRO J 427 0 -2.63
CISPEP 20 TYR J 579 PRO J 580 0 1.52
SITE 1 AC1 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC1 6 ILE A 313 HOH A 911
SITE 1 AC2 6 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AC2 6 ILE B 313 HOH B1034
SITE 1 AC3 6 ASP C 304 ASP C 307 LEU C 309 ASP C 311
SITE 2 AC3 6 ILE C 313 HOH C 943
SITE 1 AC4 6 ASP D 304 ASP D 307 LEU D 309 ASP D 311
SITE 2 AC4 6 ILE D 313 HOH D1027
SITE 1 AC5 6 ASP E 304 ASP E 307 LEU E 309 ASP E 311
SITE 2 AC5 6 ILE E 313 HOH E 915
SITE 1 AC6 6 ASP F 304 ASP F 307 LEU F 309 ASP F 311
SITE 2 AC6 6 ILE F 313 HOH F 933
SITE 1 AC7 6 ASP G 304 ASP G 307 LEU G 309 ASP G 311
SITE 2 AC7 6 ILE G 313 HOH G 962
SITE 1 AC8 6 ASP H 304 ASP H 307 LEU H 309 ASP H 311
SITE 2 AC8 6 ILE H 313 HOH H 969
SITE 1 AC9 6 ASP I 304 ASP I 307 LEU I 309 ASP I 311
SITE 2 AC9 6 ILE I 313 HOH I 963
SITE 1 AD1 6 ASP J 304 ASP J 307 LEU J 309 ASP J 311
SITE 2 AD1 6 ILE J 313 HOH J 968
CRYST1 110.490 135.630 138.150 83.09 67.91 67.57 P 1 10
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009051 -0.003736 -0.003776 0.00000
SCALE2 0.000000 0.007976 0.000216 0.00000
SCALE3 0.000000 0.000000 0.007815 0.00000
TER 4148 PRO A 603
TER 8289 PRO B 603
TER 12430 PRO C 603
TER 16571 PRO D 603
TER 20712 PRO E 603
TER 24853 PRO F 603
TER 29001 PRO G 602
TER 33149 PRO H 603
TER 37290 PRO I 603
TER 41424 PRO J 602
MASTER 1200 0 10 269 152 0 20 647549 10 200 470
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