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HEADER HYDROLASE 26-SEP-05 2B4K
TITLE ACETOBACTER TURBIDANS ALPHA-AMINO ACID ESTER HYDROLASE
TITLE 2 COMPLEXED WITH PHENYLGLYCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMINO ACID ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.43;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACETOBACTER PASTEURIANUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: AEHA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,C.WILLIAMS,
AUTHOR 2 G.WYBENGA,D.B.JANSSEN,B.W.DIJKSTRA
REVDAT 1 27-DEC-05 2B4K 0
JRNL AUTH T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,
JRNL AUTH 2 C.WILLIAMS,G.WYBENGA,D.B.JANSSEN,B.W.DIJKSTRA
JRNL TITL ACETOBACTER TURBIDANS AEH: HOW A SINGLE MUTATION
JRNL TITL 2 IMPROVES AN ANTIBIOTIC-PRODUCING ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 91758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.258
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4836
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6498
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 370
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 19594
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.29
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.669
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.450
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.330
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.366
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.853
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.813
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20225 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27614 ; 0.954 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2464 ; 1.850 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2855 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16117 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10883 ; 0.198 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 811 ; 0.165 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 42 ; 0.166 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.136 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B4K COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-2005.
REMARK 100 THE RCSB ID CODE IS RCSB034666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121384
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.18600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.91700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1NX9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PEG4000,
REMARK 280 PHENYLGLYCINE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 1/2+X,1/2+Y,1/2+Z
REMARK 290 14555 1/2-X,1/2-Y,1/2+Z
REMARK 290 15555 1/2-X,1/2+Y,1/2-Z
REMARK 290 16555 1/2+X,1/2-Y,1/2-Z
REMARK 290 17555 1/2+Z,1/2+X,1/2+Y
REMARK 290 18555 1/2+Z,1/2-X,1/2-Y
REMARK 290 19555 1/2-Z,1/2-X,1/2+Y
REMARK 290 20555 1/2-Z,1/2+X,1/2-Y
REMARK 290 21555 1/2+Y,1/2+Z,1/2+X
REMARK 290 22555 1/2-Y,1/2+Z,1/2-X
REMARK 290 23555 1/2+Y,1/2-Z,1/2-X
REMARK 290 24555 1/2-Y,1/2-Z,1/2+X
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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 170.45450
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 170.45450
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 170.45450
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 170.45450
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 170.45450
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 170.45450
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 ALA A 44
REMARK 465 ASP A 45
REMARK 465 ALA A 46
REMARK 465 ALA A 47
REMARK 465 GLN A 48
REMARK 465 ALA A 49
REMARK 465 GLN A 667
REMARK 465 LYS A 668
REMARK 465 LEU A 669
REMARK 465 GLY A 670
REMARK 465 PRO A 671
REMARK 465 GLU A 672
REMARK 465 GLN A 673
REMARK 465 LYS A 674
REMARK 465 LEU A 675
REMARK 465 ILE A 676
REMARK 465 SER A 677
REMARK 465 GLU A 678
REMARK 465 GLU A 679
REMARK 465 ASP A 680
REMARK 465 LEU A 681
REMARK 465 ASN A 682
REMARK 465 SER A 683
REMARK 465 ALA A 684
REMARK 465 VAL A 685
REMARK 465 ASP A 686
REMARK 465 HIS A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 ALA B 44
REMARK 465 ASP B 45
REMARK 465 ALA B 46
REMARK 465 ALA B 47
REMARK 465 GLN B 48
REMARK 465 ALA B 49
REMARK 465 GLN B 667
REMARK 465 LYS B 668
REMARK 465 LEU B 669
REMARK 465 GLY B 670
REMARK 465 PRO B 671
REMARK 465 GLU B 672
REMARK 465 GLN B 673
REMARK 465 LYS B 674
REMARK 465 LEU B 675
REMARK 465 ILE B 676
REMARK 465 SER B 677
REMARK 465 GLU B 678
REMARK 465 GLU B 679
REMARK 465 ASP B 680
REMARK 465 LEU B 681
REMARK 465 ASN B 682
REMARK 465 SER B 683
REMARK 465 ALA B 684
REMARK 465 VAL B 685
REMARK 465 ASP B 686
REMARK 465 HIS B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 HIS B 690
REMARK 465 HIS B 691
REMARK 465 HIS B 692
REMARK 465 ALA C 41
REMARK 465 PRO C 42
REMARK 465 ALA C 43
REMARK 465 ALA C 44
REMARK 465 ASP C 45
REMARK 465 ALA C 46
REMARK 465 ALA C 47
REMARK 465 GLN C 48
REMARK 465 ALA C 49
REMARK 465 GLN C 667
REMARK 465 LYS C 668
REMARK 465 LEU C 669
REMARK 465 GLY C 670
REMARK 465 PRO C 671
REMARK 465 GLU C 672
REMARK 465 GLN C 673
REMARK 465 LYS C 674
REMARK 465 LEU C 675
REMARK 465 ILE C 676
REMARK 465 SER C 677
REMARK 465 GLU C 678
REMARK 465 GLU C 679
REMARK 465 ASP C 680
REMARK 465 LEU C 681
REMARK 465 ASN C 682
REMARK 465 SER C 683
REMARK 465 ALA C 684
REMARK 465 VAL C 685
REMARK 465 ASP C 686
REMARK 465 HIS C 687
REMARK 465 HIS C 688
REMARK 465 HIS C 689
REMARK 465 HIS C 690
REMARK 465 HIS C 691
REMARK 465 HIS C 692
REMARK 465 ALA D 41
REMARK 465 PRO D 42
REMARK 465 ALA D 43
REMARK 465 ALA D 44
REMARK 465 ASP D 45
REMARK 465 ALA D 46
REMARK 465 ALA D 47
REMARK 465 GLN D 48
REMARK 465 ALA D 49
REMARK 465 GLN D 667
REMARK 465 LYS D 668
REMARK 465 LEU D 669
REMARK 465 GLY D 670
REMARK 465 PRO D 671
REMARK 465 GLU D 672
REMARK 465 GLN D 673
REMARK 465 LYS D 674
REMARK 465 LEU D 675
REMARK 465 ILE D 676
REMARK 465 SER D 677
REMARK 465 GLU D 678
REMARK 465 GLU D 679
REMARK 465 ASP D 680
REMARK 465 LEU D 681
REMARK 465 ASN D 682
REMARK 465 SER D 683
REMARK 465 ALA D 684
REMARK 465 VAL D 685
REMARK 465 ASP D 686
REMARK 465 HIS D 687
REMARK 465 HIS D 688
REMARK 465 HIS D 689
REMARK 465 HIS D 690
REMARK 465 HIS D 691
REMARK 465 HIS D 692
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
REMARK 500 O SER C 482 NH1 ARG C 492 2.11
REMARK 500 OG SER B 205 NE2 HIS B 370 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 67 CG MET A 67 SD 0.059
REMARK 500 MET A 67 SD MET A 67 CE 0.076
REMARK 500 PRO A 495 CB PRO A 495 CG 0.062
REMARK 500 MET A 554 SD MET A 554 CE -0.067
REMARK 500 MET A 561 SD MET A 561 CE -0.065
REMARK 500 MET B 67 CG MET B 67 SD 0.058
REMARK 500 MET B 67 SD MET B 67 CE 0.092
REMARK 500 GLN B 72 CG GLN B 72 CD 0.060
REMARK 500 MET B 258 SD MET B 258 CE -0.057
REMARK 500 MET B 302 SD MET B 302 CE -0.060
REMARK 500 MET B 561 SD MET B 561 CE -0.090
REMARK 500 MET B 570 SD MET B 570 CE -0.080
REMARK 500 MET C 67 SD MET C 67 CE 0.133
REMARK 500 GLN C 72 CG GLN C 72 CD 0.060
REMARK 500 MET C 81 SD MET C 81 CE 0.112
REMARK 500 MET C 570 SD MET C 570 CE -0.073
REMARK 500 MET D 67 SD MET D 67 CE 0.130
REMARK 500 GLN D 72 CG GLN D 72 CD 0.054
REMARK 500 MET D 81 SD MET D 81 CE 0.060
REMARK 500 ARG D 101 CB ARG D 101 CG 0.053
REMARK 500 MET D 236 SD MET D 236 CE -0.060
REMARK 500 MET D 302 SD MET D 302 CE -0.071
REMARK 500 ARG D 432 CG ARG D 432 CD 0.057
REMARK 500 PRO D 495 CB PRO D 495 CG 0.058
REMARK 500 MET D 570 SD MET D 570 CE -0.059
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 121 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ILE A 144 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP A 239 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 GLY A 344 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU A 449 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU A 451 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 VAL B 121 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLY B 344 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 ILE B 419 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 LEU B 451 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASN B 603 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 VAL C 121 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ILE C 144 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 HIS C 242 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 GLY C 344 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASN C 603 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 ILE C 612 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 VAL D 121 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ILE D 144 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLY D 200 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 GLY D 344 N - CA - C ANGL. DEV. = 7.3 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 TYR A 154 -114.88 49.85
REMARK 500 TYR B 154 -107.58 44.77
REMARK 500 TYR C 154 -110.95 50.94
REMARK 500 TYR D 154 -101.39 48.91
REMARK 500 SER D 205 -114.69 62.44
DBREF 2B4K A 41 667 GB 18139885 AAL60195 41 667
DBREF 2B4K B 41 667 GB 18139885 AAL60195 41 667
DBREF 2B4K C 41 667 GB 18139885 AAL60195 41 667
DBREF 2B4K D 41 667 GB 18139885 AAL60195 41 667
SEQADV 2B4K LYS A 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K LEU A 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLY A 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K PRO A 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLU A 672 GB 18139885 MYC TAG
SEQADV 2B4K GLN A 673 GB 18139885 MYC TAG
SEQADV 2B4K LYS A 674 GB 18139885 MYC TAG
SEQADV 2B4K LEU A 675 GB 18139885 MYC TAG
SEQADV 2B4K ILE A 676 GB 18139885 MYC TAG
SEQADV 2B4K SER A 677 GB 18139885 MYC TAG
SEQADV 2B4K GLU A 678 GB 18139885 MYC TAG
SEQADV 2B4K GLU A 679 GB 18139885 MYC TAG
SEQADV 2B4K ASP A 680 GB 18139885 MYC TAG
SEQADV 2B4K LEU A 681 GB 18139885 MYC TAG
SEQADV 2B4K ASN A 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K SER A 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ALA A 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K VAL A 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ASP A 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K HIS A 687 GB 18139885 HIS TAG
SEQADV 2B4K HIS A 688 GB 18139885 HIS TAG
SEQADV 2B4K HIS A 689 GB 18139885 HIS TAG
SEQADV 2B4K HIS A 690 GB 18139885 HIS TAG
SEQADV 2B4K HIS A 691 GB 18139885 HIS TAG
SEQADV 2B4K HIS A 692 GB 18139885 HIS TAG
SEQADV 2B4K LYS B 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K LEU B 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLY B 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K PRO B 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLU B 672 GB 18139885 MYC TAG
SEQADV 2B4K GLN B 673 GB 18139885 MYC TAG
SEQADV 2B4K LYS B 674 GB 18139885 MYC TAG
SEQADV 2B4K LEU B 675 GB 18139885 MYC TAG
SEQADV 2B4K ILE B 676 GB 18139885 MYC TAG
SEQADV 2B4K SER B 677 GB 18139885 MYC TAG
SEQADV 2B4K GLU B 678 GB 18139885 MYC TAG
SEQADV 2B4K GLU B 679 GB 18139885 MYC TAG
SEQADV 2B4K ASP B 680 GB 18139885 MYC TAG
SEQADV 2B4K LEU B 681 GB 18139885 MYC TAG
SEQADV 2B4K ASN B 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K SER B 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ALA B 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K VAL B 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ASP B 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K HIS B 687 GB 18139885 HIS TAG
SEQADV 2B4K HIS B 688 GB 18139885 HIS TAG
SEQADV 2B4K HIS B 689 GB 18139885 HIS TAG
SEQADV 2B4K HIS B 690 GB 18139885 HIS TAG
SEQADV 2B4K HIS B 691 GB 18139885 HIS TAG
SEQADV 2B4K HIS B 692 GB 18139885 HIS TAG
SEQADV 2B4K LYS C 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K LEU C 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLY C 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K PRO C 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLU C 672 GB 18139885 MYC TAG
SEQADV 2B4K GLN C 673 GB 18139885 MYC TAG
SEQADV 2B4K LYS C 674 GB 18139885 MYC TAG
SEQADV 2B4K LEU C 675 GB 18139885 MYC TAG
SEQADV 2B4K ILE C 676 GB 18139885 MYC TAG
SEQADV 2B4K SER C 677 GB 18139885 MYC TAG
SEQADV 2B4K GLU C 678 GB 18139885 MYC TAG
SEQADV 2B4K GLU C 679 GB 18139885 MYC TAG
SEQADV 2B4K ASP C 680 GB 18139885 MYC TAG
SEQADV 2B4K LEU C 681 GB 18139885 MYC TAG
SEQADV 2B4K ASN C 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K SER C 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ALA C 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K VAL C 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ASP C 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K HIS C 687 GB 18139885 HIS TAG
SEQADV 2B4K HIS C 688 GB 18139885 HIS TAG
SEQADV 2B4K HIS C 689 GB 18139885 HIS TAG
SEQADV 2B4K HIS C 690 GB 18139885 HIS TAG
SEQADV 2B4K HIS C 691 GB 18139885 HIS TAG
SEQADV 2B4K HIS C 692 GB 18139885 HIS TAG
SEQADV 2B4K LYS D 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K LEU D 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLY D 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K PRO D 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K GLU D 672 GB 18139885 MYC TAG
SEQADV 2B4K GLN D 673 GB 18139885 MYC TAG
SEQADV 2B4K LYS D 674 GB 18139885 MYC TAG
SEQADV 2B4K LEU D 675 GB 18139885 MYC TAG
SEQADV 2B4K ILE D 676 GB 18139885 MYC TAG
SEQADV 2B4K SER D 677 GB 18139885 MYC TAG
SEQADV 2B4K GLU D 678 GB 18139885 MYC TAG
SEQADV 2B4K GLU D 679 GB 18139885 MYC TAG
SEQADV 2B4K ASP D 680 GB 18139885 MYC TAG
SEQADV 2B4K LEU D 681 GB 18139885 MYC TAG
SEQADV 2B4K ASN D 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K SER D 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ALA D 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K VAL D 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K ASP D 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B4K HIS D 687 GB 18139885 HIS TAG
SEQADV 2B4K HIS D 688 GB 18139885 HIS TAG
SEQADV 2B4K HIS D 689 GB 18139885 HIS TAG
SEQADV 2B4K HIS D 690 GB 18139885 HIS TAG
SEQADV 2B4K HIS D 691 GB 18139885 HIS TAG
SEQADV 2B4K HIS D 692 GB 18139885 HIS TAG
SEQRES 1 A 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 A 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 A 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 A 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 A 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 A 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 A 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 A 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 A 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 A 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 A 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 A 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 A 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 A 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 A 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 A 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 A 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 A 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 A 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 A 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 A 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 A 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 A 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 A 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 A 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 A 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 A 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 A 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 A 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 A 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 A 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 A 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 A 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 A 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 A 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 A 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 A 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 A 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 A 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 A 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 A 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 A 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 A 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 A 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 A 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 A 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 A 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 A 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 A 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 A 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 A 652 HIS HIS
SEQRES 1 B 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 B 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 B 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 B 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 B 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 B 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 B 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 B 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 B 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 B 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 B 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 B 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 B 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 B 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 B 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 B 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 B 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 B 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 B 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 B 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 B 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 B 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 B 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 B 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 B 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 B 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 B 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 B 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 B 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 B 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 B 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 B 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 B 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 B 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 B 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 B 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 B 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 B 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 B 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 B 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 B 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 B 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 B 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 B 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 B 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 B 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 B 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 B 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 B 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 B 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 B 652 HIS HIS
SEQRES 1 C 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 C 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 C 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 C 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 C 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 C 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 C 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 C 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 C 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 C 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 C 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 C 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 C 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 C 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 C 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 C 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 C 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 C 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 C 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 C 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 C 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 C 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 C 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 C 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 C 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 C 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 C 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 C 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 C 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 C 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 C 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 C 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 C 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 C 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 C 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 C 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 C 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 C 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 C 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 C 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 C 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 C 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 C 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 C 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 C 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 C 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 C 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 C 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 C 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 C 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 C 652 HIS HIS
SEQRES 1 D 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 D 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 D 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 D 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 D 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 D 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 D 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 D 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 D 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 D 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 D 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 D 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 D 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 D 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 D 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 D 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 D 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 D 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 D 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 D 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 D 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 D 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 D 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 D 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 D 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 D 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 D 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 D 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 D 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 D 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 D 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 D 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 D 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 D 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 D 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 D 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 D 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 D 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 D 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 D 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 D 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 D 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 D 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 D 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 D 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 D 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 D 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 D 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 D 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 D 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 D 652 HIS HIS
HET PG9 3598 11
HET PG9 3599 11
HET PG9 3600 11
HET GOL 2430 6
HET GOL 2431 6
HET GOL 2432 6
HET GOL 2433 6
HETNAM PG9 D-PHENYLGLYCINE
HETNAM GOL GLYCEROL
FORMUL 5 PG9 3(C8 H9 N1 O2)
FORMUL 8 GOL 4(C3 H8 O3)
FORMUL 12 HOH *5(H2 O1)
HELIX 1 1 PRO A 68 ARG A 73 1 6
HELIX 2 2 ASN A 113 ALA A 118 1 6
HELIX 3 3 THR A 126 LEU A 131 1 6
HELIX 4 4 PRO A 132 GLY A 134 5 3
HELIX 5 5 ASP A 135 GLY A 142 1 8
HELIX 6 6 ASP A 176 VAL A 192 1 17
HELIX 7 7 SER A 205 ASP A 217 1 13
HELIX 8 8 GLY A 249 THR A 259 1 11
HELIX 9 9 ASP A 273 GLY A 282 1 10
HELIX 10 10 SER A 283 GLY A 292 1 10
HELIX 11 11 LEU A 293 GLN A 295 5 3
HELIX 12 12 TYR A 296 ALA A 304 1 9
HELIX 13 13 ASP A 309 GLY A 314 1 6
HELIX 14 14 ALA A 316 ARG A 324 1 9
HELIX 15 15 TRP A 343 ALA A 355 1 13
HELIX 16 16 SER A 371 TYR A 375 5 5
HELIX 17 17 ASP A 388 VAL A 397 1 10
HELIX 18 18 VAL A 397 LYS A 407 1 11
HELIX 19 19 GLN A 489 LYS A 494 1 6
HELIX 20 20 PRO A 495 GLN A 499 5 5
HELIX 21 21 GLN A 501 SER A 506 1 6
HELIX 22 22 ASP A 558 GLY A 562 5 5
HELIX 23 23 ARG A 576 ARG A 578 5 3
HELIX 24 24 ASN A 634 ALA A 638 5 5
HELIX 25 25 GLY A 653 ALA A 657 5 5
HELIX 26 26 PRO B 68 ARG B 73 1 6
HELIX 27 27 ASN B 113 ALA B 118 1 6
HELIX 28 28 THR B 126 LEU B 131 1 6
HELIX 29 29 PRO B 132 GLY B 134 5 3
HELIX 30 30 ASP B 135 GLY B 141 1 7
HELIX 31 31 ASP B 176 ASN B 191 1 16
HELIX 32 32 SER B 205 ASP B 217 1 13
HELIX 33 33 GLY B 249 THR B 259 1 11
HELIX 34 34 ASP B 273 GLY B 282 1 10
HELIX 35 35 SER B 283 GLY B 292 1 10
HELIX 36 36 TYR B 296 HIS B 305 1 10
HELIX 37 37 ASP B 309 GLY B 314 1 6
HELIX 38 38 ALA B 316 ARG B 324 1 9
HELIX 39 39 TRP B 343 ALA B 355 1 13
HELIX 40 40 SER B 371 TYR B 375 5 5
HELIX 41 41 ASP B 388 VAL B 397 1 10
HELIX 42 42 VAL B 397 LYS B 407 1 11
HELIX 43 43 GLN B 489 LYS B 494 1 6
HELIX 44 44 PRO B 495 GLN B 499 5 5
HELIX 45 45 GLN B 501 SER B 506 1 6
HELIX 46 46 ASP B 558 GLY B 562 5 5
HELIX 47 47 ARG B 576 ARG B 578 5 3
HELIX 48 48 ASN B 634 ALA B 638 5 5
HELIX 49 49 LYS B 639 TYR B 643 5 5
HELIX 50 50 GLY B 653 ALA B 657 5 5
HELIX 51 51 MET C 67 GLN C 71 5 5
HELIX 52 52 ASN C 113 ALA C 118 1 6
HELIX 53 53 THR C 126 LEU C 131 1 6
HELIX 54 54 PRO C 132 GLY C 134 5 3
HELIX 55 55 ASP C 135 GLY C 141 1 7
HELIX 56 56 THR C 178 HIS C 190 1 13
HELIX 57 57 SER C 205 ASP C 217 1 13
HELIX 58 58 GLY C 249 THR C 259 1 11
HELIX 59 59 ASP C 273 GLY C 282 1 10
HELIX 60 60 SER C 283 ALA C 291 1 9
HELIX 61 61 GLY C 292 GLN C 295 5 4
HELIX 62 62 TYR C 296 HIS C 305 1 10
HELIX 63 63 ASP C 309 GLY C 314 1 6
HELIX 64 64 ALA C 316 LYS C 325 1 10
HELIX 65 65 TRP C 343 ALA C 355 1 13
HELIX 66 66 SER C 371 TYR C 375 5 5
HELIX 67 67 ASP C 388 VAL C 397 1 10
HELIX 68 68 VAL C 397 LYS C 407 1 11
HELIX 69 69 GLN C 489 LYS C 494 1 6
HELIX 70 70 PRO C 495 GLN C 499 5 5
HELIX 71 71 GLN C 501 SER C 506 1 6
HELIX 72 72 ASP C 558 GLY C 562 5 5
HELIX 73 73 ARG C 576 ARG C 578 5 3
HELIX 74 74 ASN C 634 ALA C 638 5 5
HELIX 75 75 PRO D 68 ARG D 73 1 6
HELIX 76 76 ASN D 113 ALA D 118 1 6
HELIX 77 77 THR D 126 LEU D 131 1 6
HELIX 78 78 PRO D 132 GLY D 134 5 3
HELIX 79 79 ASP D 135 GLY D 141 1 7
HELIX 80 80 ASP D 176 VAL D 192 1 17
HELIX 81 81 TYR D 206 LEU D 215 1 10
HELIX 82 82 GLY D 249 THR D 259 1 11
HELIX 83 83 ASP D 273 GLY D 282 1 10
HELIX 84 84 SER D 283 ALA D 291 1 9
HELIX 85 85 TYR D 296 HIS D 305 1 10
HELIX 86 86 ASP D 309 GLY D 314 1 6
HELIX 87 87 ALA D 316 LYS D 325 1 10
HELIX 88 88 TRP D 343 ALA D 355 1 13
HELIX 89 89 SER D 371 TYR D 375 5 5
HELIX 90 90 ASP D 388 VAL D 397 1 10
HELIX 91 91 VAL D 397 LYS D 407 1 11
HELIX 92 92 ASP D 453 HIS D 455 5 3
HELIX 93 93 GLN D 489 LYS D 494 1 6
HELIX 94 94 PRO D 495 GLN D 499 5 5
HELIX 95 95 GLN D 501 ARG D 507 1 7
HELIX 96 96 ASP D 558 GLY D 562 5 5
HELIX 97 97 ARG D 576 ARG D 578 5 3
HELIX 98 98 ASN D 634 ALA D 638 5 5
HELIX 99 99 LYS D 639 TYR D 643 5 5
HELIX 100 100 GLY D 653 ALA D 657 5 5
SHEET 1 A 6 TYR A 75 PRO A 83 0
SHEET 2 A 6 LYS A 89 PRO A 97 -1 O LEU A 90 N VAL A 82
SHEET 3 A 6 ILE A 144 ASP A 149 -1 O ARG A 145 N VAL A 95
SHEET 4 A 6 ALA A 103 THR A 110 1 N PRO A 104 O ILE A 144
SHEET 5 A 6 SER A 195 SER A 204 1 O GLY A 200 N LEU A 107
SHEET 6 A 6 LEU A 222 GLU A 228 1 O ALA A 226 N MET A 201
SHEET 1 B 2 PHE A 241 HIS A 242 0
SHEET 2 B 2 ALA A 245 PHE A 246 -1 O ALA A 245 N HIS A 242
SHEET 1 C 4 MET A 330 GLY A 335 0
SHEET 2 C 4 ASN A 361 GLY A 366 1 O VAL A 364 N TRP A 332
SHEET 3 C 4 ALA A 418 ASN A 422 1 O TYR A 421 N MET A 365
SHEET 4 C 4 LYS A 427 TYR A 431 -1 O LYS A 427 N ASN A 422
SHEET 1 D 2 THR A 379 LEU A 380 0
SHEET 2 D 2 LEU A 383 GLU A 384 -1 O LEU A 383 N LEU A 380
SHEET 1 E 6 LEU A 457 SER A 458 0
SHEET 2 E 6 THR A 447 LEU A 451 -1 N TYR A 450 O SER A 458
SHEET 3 E 6 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 E 6 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 E 6 ALA A 646 HIS A 652 -1 O SER A 649 N ALA A 535
SHEET 6 E 6 GLY A 466 SER A 472 -1 N GLY A 466 O HIS A 652
SHEET 1 F 5 LEU A 457 SER A 458 0
SHEET 2 F 5 THR A 447 LEU A 451 -1 N TYR A 450 O SER A 458
SHEET 3 F 5 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 F 5 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 F 5 LEU A 593 THR A 598 -1 O TYR A 595 N LEU A 532
SHEET 1 G 4 VAL A 511 GLU A 514 0
SHEET 2 G 4 ARG A 611 GLN A 617 -1 O VAL A 614 N TYR A 513
SHEET 3 G 4 ASP A 542 VAL A 550 -1 N ILE A 548 O MET A 613
SHEET 4 G 4 GLU A 565 ARG A 574 -1 O LEU A 566 N ASP A 549
SHEET 1 H 2 VAL A 522 GLY A 526 0
SHEET 2 H 2 VAL A 602 PHE A 606 -1 O VAL A 602 N GLY A 526
SHEET 1 I 6 TYR B 75 PRO B 83 0
SHEET 2 I 6 LYS B 89 PRO B 97 -1 O ILE B 94 N ARG B 78
SHEET 3 I 6 ILE B 144 ASP B 149 -1 O ARG B 145 N VAL B 95
SHEET 4 I 6 ALA B 103 THR B 110 1 N LEU B 106 O ILE B 144
SHEET 5 I 6 SER B 195 SER B 204 1 O GLY B 200 N ILE B 105
SHEET 6 I 6 LEU B 222 GLU B 228 1 O GLU B 228 N GLY B 203
SHEET 1 J 2 PHE B 241 HIS B 242 0
SHEET 2 J 2 ALA B 245 PHE B 246 -1 O ALA B 245 N HIS B 242
SHEET 1 K 4 MET B 330 GLY B 335 0
SHEET 2 K 4 ASN B 361 GLY B 366 1 O VAL B 364 N TRP B 332
SHEET 3 K 4 ALA B 418 ASN B 422 1 O ILE B 419 N LEU B 363
SHEET 4 K 4 LYS B 427 TYR B 431 -1 O LYS B 427 N ASN B 422
SHEET 1 L 2 THR B 379 LEU B 380 0
SHEET 2 L 2 LEU B 383 GLU B 384 -1 O LEU B 383 N LEU B 380
SHEET 1 M 6 GLY B 456 SER B 458 0
SHEET 2 M 6 THR B 447 ALA B 452 -1 N TYR B 450 O SER B 458
SHEET 3 M 6 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 M 6 VAL B 529 THR B 536 -1 N ASP B 531 O SER B 659
SHEET 5 M 6 ALA B 646 HIS B 652 -1 O SER B 649 N ALA B 535
SHEET 6 M 6 GLY B 466 SER B 472 -1 N ASP B 468 O ILE B 650
SHEET 1 N 5 GLY B 456 SER B 458 0
SHEET 2 N 5 THR B 447 ALA B 452 -1 N TYR B 450 O SER B 458
SHEET 3 N 5 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 N 5 VAL B 529 THR B 536 -1 N ASP B 531 O SER B 659
SHEET 5 N 5 LEU B 593 THR B 598 -1 O TYR B 595 N LEU B 532
SHEET 1 O 4 VAL B 510 GLU B 514 0
SHEET 2 O 4 ARG B 611 GLN B 617 -1 O VAL B 614 N TYR B 513
SHEET 3 O 4 ASP B 542 VAL B 550 -1 N ILE B 548 O MET B 613
SHEET 4 O 4 GLU B 565 ARG B 574 -1 O LEU B 566 N ASP B 549
SHEET 1 P 3 VAL B 602 PHE B 606 0
SHEET 2 P 3 VAL B 522 GLY B 526 -1 N GLY B 526 O VAL B 602
SHEET 3 P 3 VAL B 664 VAL B 665 -1 O VAL B 665 N ARG B 523
SHEET 1 Q 6 TYR C 75 PRO C 83 0
SHEET 2 Q 6 LYS C 89 PRO C 97 -1 O ILE C 94 N ARG C 78
SHEET 3 Q 6 ILE C 144 ASP C 149 -1 O ARG C 145 N VAL C 95
SHEET 4 Q 6 ALA C 103 THR C 110 1 N THR C 110 O GLN C 148
SHEET 5 Q 6 SER C 195 SER C 204 1 O GLY C 200 N LEU C 107
SHEET 6 Q 6 LEU C 222 GLU C 228 1 O GLU C 228 N GLY C 203
SHEET 1 R 2 PHE C 241 HIS C 242 0
SHEET 2 R 2 ALA C 245 PHE C 246 -1 O ALA C 245 N HIS C 242
SHEET 1 S 4 MET C 330 GLY C 335 0
SHEET 2 S 4 ASN C 361 GLY C 366 1 O VAL C 364 N TRP C 332
SHEET 3 S 4 ALA C 418 ASN C 422 1 O TYR C 421 N MET C 365
SHEET 4 S 4 LYS C 427 TYR C 431 -1 O LYS C 427 N ASN C 422
SHEET 1 T 2 THR C 379 LEU C 380 0
SHEET 2 T 2 LEU C 383 GLU C 384 -1 O LEU C 383 N LEU C 380
SHEET 1 U 2 VAL C 437 CYS C 438 0
SHEET 2 U 2 GLY C 444 GLY C 445 1 O GLY C 444 N CYS C 438
SHEET 1 V 6 GLY C 456 SER C 458 0
SHEET 2 V 6 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 V 6 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 V 6 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 V 6 ALA C 646 HIS C 652 -1 O HIS C 651 N PHE C 533
SHEET 6 V 6 GLY C 466 SER C 472 -1 N TYR C 470 O GLN C 648
SHEET 1 W 5 GLY C 456 SER C 458 0
SHEET 2 W 5 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 W 5 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 W 5 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 W 5 THR C 592 THR C 598 -1 O TYR C 595 N LEU C 532
SHEET 1 X 4 VAL C 510 GLU C 514 0
SHEET 2 X 4 ARG C 611 GLN C 617 -1 O ILE C 616 N VAL C 511
SHEET 3 X 4 ASP C 542 VAL C 550 -1 N ILE C 548 O MET C 613
SHEET 4 X 4 GLU C 565 ARG C 574 -1 O SER C 569 N LEU C 547
SHEET 1 Y 3 VAL C 602 PHE C 606 0
SHEET 2 Y 3 VAL C 522 GLY C 526 -1 N GLY C 526 O VAL C 602
SHEET 3 Y 3 VAL C 664 VAL C 665 -1 O VAL C 665 N ARG C 523
SHEET 1 Z 6 TYR D 75 PRO D 83 0
SHEET 2 Z 6 LYS D 89 PRO D 97 -1 O ILE D 96 N ILE D 76
SHEET 3 Z 6 ILE D 144 ASP D 149 -1 O ARG D 145 N VAL D 95
SHEET 4 Z 6 ALA D 103 THR D 110 1 N PRO D 104 O ILE D 144
SHEET 5 Z 6 SER D 195 SER D 205 1 O GLY D 200 N LEU D 107
SHEET 6 Z 6 LEU D 222 PRO D 230 1 O GLU D 228 N GLY D 203
SHEET 1 AA 2 PHE D 241 HIS D 242 0
SHEET 2 AA 2 ALA D 245 PHE D 246 -1 O ALA D 245 N HIS D 242
SHEET 1 AB 4 MET D 330 GLY D 335 0
SHEET 2 AB 4 ASN D 361 GLY D 366 1 O VAL D 364 N TRP D 332
SHEET 3 AB 4 ALA D 418 ASN D 422 1 O TYR D 421 N MET D 365
SHEET 4 AB 4 LYS D 427 TYR D 431 -1 O LYS D 427 N ASN D 422
SHEET 1 AC 2 THR D 379 LEU D 380 0
SHEET 2 AC 2 LEU D 383 GLU D 384 -1 O LEU D 383 N LEU D 380
SHEET 1 AD 2 VAL D 437 CYS D 438 0
SHEET 2 AD 2 GLY D 444 GLY D 445 1 O GLY D 444 N CYS D 438
SHEET 1 AE 6 LEU D 457 SER D 458 0
SHEET 2 AE 6 THR D 447 LEU D 451 -1 N TYR D 450 O SER D 458
SHEET 3 AE 6 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AE 6 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AE 6 ALA D 646 HIS D 652 -1 O SER D 649 N ALA D 535
SHEET 6 AE 6 GLY D 466 SER D 472 -1 N TYR D 470 O GLN D 648
SHEET 1 AF 5 LEU D 457 SER D 458 0
SHEET 2 AF 5 THR D 447 LEU D 451 -1 N TYR D 450 O SER D 458
SHEET 3 AF 5 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AF 5 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AF 5 LEU D 593 THR D 598 -1 O PHE D 597 N ALA D 530
SHEET 1 AG 4 VAL D 511 GLU D 514 0
SHEET 2 AG 4 ARG D 611 GLN D 617 -1 O ILE D 616 N VAL D 511
SHEET 3 AG 4 ASP D 542 VAL D 550 -1 N ILE D 548 O MET D 613
SHEET 4 AG 4 GLU D 565 ARG D 574 -1 O LEU D 566 N ASP D 549
SHEET 1 AH 2 VAL D 522 ARG D 523 0
SHEET 2 AH 2 VAL D 605 PHE D 606 -1 O PHE D 606 N VAL D 522
SSBOND 1 CYS A 438 CYS A 442
SSBOND 2 CYS D 438 CYS D 442
CISPEP 1 TRP A 434 PRO A 435 0 -0.71
CISPEP 2 ARG A 483 PRO A 484 0 -0.26
CISPEP 3 PHE A 621 PRO A 622 0 -2.20
CISPEP 4 TRP B 434 PRO B 435 0 -0.63
CISPEP 5 ARG B 483 PRO B 484 0 -1.14
CISPEP 6 PHE B 621 PRO B 622 0 -2.27
CISPEP 7 TRP C 434 PRO C 435 0 -0.96
CISPEP 8 ARG C 483 PRO C 484 0 -0.44
CISPEP 9 PHE C 621 PRO C 622 0 -1.61
CISPEP 10 TRP D 434 PRO D 435 0 1.20
CISPEP 11 ARG D 483 PRO D 484 0 -1.69
CISPEP 12 PHE D 621 PRO D 622 0 -2.61
CRYST1 340.909 340.909 340.909 90.00 90.00 90.00 I 2 3 96
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 0.002933 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002933 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002933 0.00000
TER 4884 LYS A 666
TER 9768 LYS B 666
TER 14652 LYS C 666
TER 19536 LYS D 666
MASTER 553 0 7 100 130 0 0 619594 4 61 204
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