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HEADER HYDROLASE 01-NOV-17 5YP4
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP IV) WITH LYS-PRO
TITLE 2 FROM PSEUDOXANTHOMONAS MEXICANA WO24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV,DAP IV;
COMPND 5 EC: 3.4.14.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOXANTHOMONAS MEXICANA;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS SP. WO24;
SOURCE 4 ORGANISM_TAXID: 128785;
SOURCE 5 STRAIN: WO24;
SOURCE 6 GENE: DAP4;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS DAP IV, CLAN SC S9, PEPTIDASE, DPP4, DPP8, DPP9, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUIMOTO,S.MORISAWA,I.IIZUKA,
AUTHOR 2 A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,Y.SAKAMOTO,T.NONAKA
REVDAT 1 21-FEB-18 5YP4 0
JRNL AUTH S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUJIMOTO,S.MORISAWA,
JRNL AUTH 2 I.IIZUKA,A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,
JRNL AUTH 3 Y.SAKAMOTO,T.NONAKA
JRNL TITL CRYSTAL STRUCTURES OF A BACTERIAL DIPEPTIDYL PEPTIDASE IV
JRNL TITL 2 REVEAL A NOVEL SUBSTRATE RECOGNITION MECHANISM DISTINCT FROM
JRNL TITL 3 THAT OF MAMMALIAN ORTHOLOGUES.
JRNL REF SCI REP V. 8 2714 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29426867
JRNL DOI 10.1038/S41598-018-21056-Y
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 232846
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12222
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11640
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 641
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22262
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 191
REMARK 3 SOLVENT ATOMS : 2877
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.67000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : -0.70000
REMARK 3 B12 (A**2) : -0.84000
REMARK 3 B13 (A**2) : -0.67000
REMARK 3 B23 (A**2) : 0.74000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.336
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22990 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21075 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31227 ; 1.887 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48683 ; 1.093 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2842 ; 7.125 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1065 ;30.528 ;23.033
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3599 ;14.269 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 198 ;19.188 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3403 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 25812 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4974 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 11404 ; 2.011 ; 2.042
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11404 ; 2.011 ; 2.042
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14231 ; 2.846 ; 3.047
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14232 ; 2.846 ; 3.047
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11586 ; 2.726 ; 2.345
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11586 ; 2.726 ; 2.345
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 16996 ; 4.157 ; 3.388
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 26233 ; 5.888 ;24.818
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 26049 ; 5.843 ;24.676
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005662.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.5.436
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 245086
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 5YP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 20000, 80MM MES PH6.5, 20%
REMARK 280 GLYCEROL, 4MM LYS-PRO, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 ARG A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 PHE A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 PHE A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 ILE A 12
REMARK 465 THR A 13
REMARK 465 VAL A 14
REMARK 465 ALA A 15
REMARK 465 THR A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 HIS A 21
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LEU B 3
REMARK 465 ALA B 4
REMARK 465 LEU B 5
REMARK 465 PHE B 6
REMARK 465 ALA B 7
REMARK 465 LEU B 8
REMARK 465 PHE B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 ILE B 12
REMARK 465 THR B 13
REMARK 465 VAL B 14
REMARK 465 ALA B 15
REMARK 465 THR B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 HIS B 21
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 LEU C 3
REMARK 465 ALA C 4
REMARK 465 LEU C 5
REMARK 465 PHE C 6
REMARK 465 ALA C 7
REMARK 465 LEU C 8
REMARK 465 PHE C 9
REMARK 465 ALA C 10
REMARK 465 LEU C 11
REMARK 465 ILE C 12
REMARK 465 THR C 13
REMARK 465 VAL C 14
REMARK 465 ALA C 15
REMARK 465 THR C 16
REMARK 465 ALA C 17
REMARK 465 LEU C 18
REMARK 465 PRO C 19
REMARK 465 ALA C 20
REMARK 465 HIS C 21
REMARK 465 ASP C 60
REMARK 465 ARG C 61
REMARK 465 GLY C 90
REMARK 465 GLU C 91
REMARK 465 GLU C 92
REMARK 465 VAL C 93
REMARK 465 LEU C 94
REMARK 465 SER C 95
REMARK 465 ASP C 96
REMARK 465 GLU C 97
REMARK 465 GLU C 98
REMARK 465 LYS C 99
REMARK 465 ALA C 100
REMARK 465 ARG C 101
REMARK 465 ARG C 102
REMARK 465 GLU C 103
REMARK 465 ARG C 104
REMARK 465 GLN C 105
REMARK 465 ARG C 106
REMARK 465 ILE C 107
REMARK 465 ALA C 108
REMARK 465 ALA C 109
REMARK 465 SER C 119
REMARK 465 PRO C 120
REMARK 465 ASP C 121
REMARK 465 GLY C 122
REMARK 465 LYS C 123
REMARK 465 ASP C 137
REMARK 465 LEU C 138
REMARK 465 THR C 139
REMARK 465 LYS C 140
REMARK 465 SER C 141
REMARK 465 GLY C 142
REMARK 465 ARG C 143
REMARK 465 ASP C 144
REMARK 465 ASN C 151
REMARK 465 GLY C 152
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 LEU D 3
REMARK 465 ALA D 4
REMARK 465 LEU D 5
REMARK 465 PHE D 6
REMARK 465 ALA D 7
REMARK 465 LEU D 8
REMARK 465 PHE D 9
REMARK 465 ALA D 10
REMARK 465 LEU D 11
REMARK 465 ILE D 12
REMARK 465 THR D 13
REMARK 465 VAL D 14
REMARK 465 ALA D 15
REMARK 465 THR D 16
REMARK 465 ALA D 17
REMARK 465 LEU D 18
REMARK 465 PRO D 19
REMARK 465 ALA D 20
REMARK 465 HIS D 21
REMARK 465 TYR D 241
REMARK 465 GLU D 242
REMARK 465 VAL D 243
REMARK 465 TYR D 244
REMARK 465 PRO D 245
REMARK 465 ASP D 246
REMARK 465 ARG D 247
REMARK 465 THR D 248
REMARK 465 GLU D 249
REMARK 465 VAL D 250
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 CB LYS A 744 O HOH A 1318 1.84
REMARK 500 CB LYS D 744 O HOH D 1357 2.03
REMARK 500 N ALA A 22 O HOH A 901 2.06
REMARK 500 OE2 GLU C 712 NH2 ARG C 741 2.11
REMARK 500 OD1 ASP A 62 O HOH A 902 2.12
REMARK 500 O HOH C 1013 O HOH C 1396 2.17
REMARK 500 OE1 GLU C 208 O HOH C 901 2.18
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 392 CD GLU C 392 OE2 0.068
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 286 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 351 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 484 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 537 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 568 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 568 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LEU A 590 CA - CB - CG ANGL. DEV. = -17.1 DEGREES
REMARK 500 ARG A 606 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 606 NE - CZ - NH2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 652 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 724 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 741 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 49 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 62 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP B 62 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG B 327 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 351 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 423 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 VAL B 584 CG1 - CB - CG2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 LEU B 590 CA - CB - CG ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG B 606 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 606 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 652 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 724 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 724 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 49 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 174 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 174 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 254 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 301 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG C 301 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP C 310 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG C 403 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 403 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 537 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 591 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 591 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 606 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP C 641 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU C 644 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG C 733 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 264 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 423 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP D 461 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 499 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG D 606 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG D 606 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP D 641 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG D 741 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
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 LEU A 36 -62.64 -128.56
REMARK 500 ASP A 144 4.01 -64.75
REMARK 500 ARG A 247 155.34 179.46
REMARK 500 THR A 336 -79.23 -115.12
REMARK 500 THR A 501 -35.94 -139.69
REMARK 500 SER A 543 -140.68 -156.58
REMARK 500 LYS A 580 38.76 -146.03
REMARK 500 THR A 583 -79.12 -119.43
REMARK 500 SER A 613 -113.61 72.01
REMARK 500 ALA A 637 60.15 30.63
REMARK 500 ASP A 655 -178.47 62.22
REMARK 500 ASN A 660 57.90 -144.21
REMARK 500 ASN A 691 -76.89 -121.08
REMARK 500 LYS A 720 -138.35 -102.29
REMARK 500 LYS A 744 78.69 39.21
REMARK 500 LEU B 36 -61.97 -131.87
REMARK 500 SER B 141 94.81 -163.09
REMARK 500 ALA B 258 126.06 -39.90
REMARK 500 THR B 336 -88.97 -115.13
REMARK 500 THR B 501 -31.31 -131.43
REMARK 500 ARG B 542 48.80 -70.93
REMARK 500 SER B 543 -141.40 -149.91
REMARK 500 LYS B 580 39.79 -143.25
REMARK 500 THR B 583 -81.09 -124.16
REMARK 500 SER B 613 -112.06 71.26
REMARK 500 HIS B 626 53.95 -141.52
REMARK 500 ALA B 637 58.18 29.56
REMARK 500 ASP B 655 -176.90 64.93
REMARK 500 ASN B 660 56.35 -146.05
REMARK 500 ASN B 691 -73.76 -127.30
REMARK 500 LYS B 720 -145.96 -103.08
REMARK 500 LYS B 744 83.96 45.20
REMARK 500 ASP C 286 105.28 -52.67
REMARK 500 ASP C 288 68.76 -101.41
REMARK 500 THR C 336 -85.89 -107.74
REMARK 500 THR C 501 -39.73 -138.12
REMARK 500 LYS C 580 32.97 -148.20
REMARK 500 THR C 583 -81.65 -123.10
REMARK 500 SER C 613 -111.64 71.76
REMARK 500 HIS C 626 53.23 -140.23
REMARK 500 ALA C 637 54.19 29.65
REMARK 500 ASP C 655 -178.05 65.71
REMARK 500 ASN C 660 54.98 -153.81
REMARK 500 LEU D 36 -55.59 -129.39
REMARK 500 ASP D 62 89.25 -151.89
REMARK 500 SER D 141 73.53 32.47
REMARK 500 THR D 336 -86.64 -113.28
REMARK 500 THR D 501 -37.46 -130.81
REMARK 500 SER D 543 -131.61 -149.34
REMARK 500 LYS D 580 45.54 -145.62
REMARK 500
REMARK 500 THIS ENTRY HAS 59 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 A1713 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A1714 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A1715 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH A1716 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A1717 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH B1584 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B1585 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH C1507 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH C1508 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH C1509 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH C1510 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH C1511 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH D1656 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH D1657 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH D1658 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH D1659 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH D1660 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D1661 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH D1662 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH D1663 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH D1664 DISTANCE = 7.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS A 801 and PRO A
REMARK 800 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS B 801 and PRO B
REMARK 800 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO B 802 and SER B
REMARK 800 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS C 801 and PRO C
REMARK 800 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LYS D 801 and PRO D
REMARK 800 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO D 802 and SER D
REMARK 800 613
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YP1 RELATED DB: PDB
REMARK 900 5YP1 IS THE SAME PROTEIN APO FROM.
REMARK 900 RELATED ID: 5YP2 RELATED DB: PDB
REMARK 900 5YP2 IS THE SAME PROTEIN COMPLEXED WITH DPP4 INHIBITOR 1C.
REMARK 900 RELATED ID: 5YP3 RELATED DB: PDB
REMARK 900 5YP3 IS THE SAME PROTEIN COMPLEXED WITH ILE-PRO.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE M12I IS MUTAGENESIS ACCORDING TO SEQUENCE DATABASE
REMARK 999 UNIPORTKB Q6F3I7 (DAP4_PSEMX).
DBREF 5YP4 A 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
DBREF 5YP4 B 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
DBREF 5YP4 C 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
DBREF 5YP4 D 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
SEQADV 5YP4 ILE A 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQADV 5YP4 ILE B 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQADV 5YP4 ILE C 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQADV 5YP4 ILE D 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQRES 1 A 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 A 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 A 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 A 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 A 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 A 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 A 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 A 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 A 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 A 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 A 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 A 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 A 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 A 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 A 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 A 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 A 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 A 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 A 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 A 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 A 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 A 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 A 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 A 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 A 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 A 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 A 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 A 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 A 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 A 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 A 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 A 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 A 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 A 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 A 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 A 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 A 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 A 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 A 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 A 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 A 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 A 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 A 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 A 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 A 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 A 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 A 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 A 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 A 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 A 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 A 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 A 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 A 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 A 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 A 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 A 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 A 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 A 745 CYS LEU LYS PRO
SEQRES 1 B 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 B 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 B 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 B 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 B 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 B 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 B 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 B 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 B 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 B 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 B 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 B 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 B 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 B 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 B 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 B 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 B 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 B 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 B 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 B 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 B 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 B 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 B 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 B 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 B 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 B 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 B 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 B 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 B 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 B 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 B 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 B 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 B 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 B 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 B 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 B 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 B 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 B 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 B 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 B 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 B 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 B 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 B 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 B 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 B 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 B 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 B 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 B 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 B 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 B 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 B 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 B 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 B 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 B 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 B 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 B 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 B 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 B 745 CYS LEU LYS PRO
SEQRES 1 C 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 C 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 C 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 C 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 C 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 C 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 C 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 C 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 C 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 C 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 C 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 C 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 C 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 C 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 C 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 C 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 C 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 C 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 C 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 C 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 C 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 C 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 C 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 C 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 C 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 C 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 C 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 C 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 C 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 C 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 C 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 C 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 C 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 C 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 C 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 C 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 C 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 C 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 C 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 C 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 C 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 C 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 C 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 C 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 C 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 C 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 C 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 C 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 C 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 C 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 C 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 C 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 C 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 C 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 C 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 C 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 C 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 C 745 CYS LEU LYS PRO
SEQRES 1 D 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 D 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 D 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 D 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 D 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 D 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 D 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 D 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 D 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 D 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 D 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 D 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 D 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 D 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 D 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 D 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 D 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 D 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 D 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 D 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 D 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 D 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 D 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 D 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 D 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 D 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 D 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 D 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 D 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 D 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 D 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 D 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 D 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 D 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 D 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 D 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 D 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 D 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 D 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 D 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 D 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 D 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 D 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 D 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 D 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 D 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 D 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 D 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 D 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 D 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 D 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 D 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 D 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 D 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 D 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 D 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 D 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 D 745 CYS LEU LYS PRO
HET GOL A 803 6
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET LYS A 801 9
HET PRO A 802 7
HET GOL B 803 6
HET GOL B 804 6
HET GOL B 805 6
HET GOL B 806 6
HET GOL B 807 6
HET GOL B 808 6
HET GOL B 809 6
HET GOL B 810 6
HET GOL B 811 6
HET GOL B 812 6
HET LYS B 801 9
HET PRO B 802 7
HET LYS C 801 9
HET PRO C 802 8
HET GOL C 803 6
HET GOL C 804 6
HET GOL D 803 6
HET GOL D 804 6
HET GOL D 805 6
HET GOL D 806 6
HET GOL D 807 6
HET LYS D 801 9
HET PRO D 802 7
HETNAM GOL GLYCEROL
HETNAM LYS LYSINE
HETNAM PRO PROLINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 21(C3 H8 O3)
FORMUL 9 LYS 4(C6 H15 N2 O2 1+)
FORMUL 10 PRO 4(C5 H9 N O2)
FORMUL 34 HOH *2877(H2 O)
HELIX 1 AA1 THR A 26 GLY A 32 1 7
HELIX 2 AA2 ASP A 83 LEU A 88 1 6
HELIX 3 AA3 SER A 95 GLN A 105 1 11
HELIX 4 AA4 GLU A 203 MET A 210 1 8
HELIX 5 AA5 TYR A 480 ALA A 485 1 6
HELIX 6 AA6 SER A 543 GLN A 554 1 12
HELIX 7 AA7 GLY A 570 GLY A 575 1 6
HELIX 8 AA8 ALA A 576 TYR A 578 5 3
HELIX 9 AA9 THR A 583 SER A 598 1 16
HELIX 10 AB1 SER A 613 HIS A 626 1 14
HELIX 11 AB2 ASP A 641 TYR A 645 5 5
HELIX 12 AB3 ASP A 646 ASP A 655 1 10
HELIX 13 AB4 LEU A 656 ALA A 659 5 4
HELIX 14 AB5 ASN A 660 SER A 668 1 9
HELIX 15 AB6 SER A 668 VAL A 673 1 6
HELIX 16 AB7 ASP A 674 ILE A 676 5 3
HELIX 17 AB8 PHE A 694 GLY A 708 1 15
HELIX 18 AB9 ARG A 724 LYS A 744 1 21
HELIX 19 AC1 THR B 26 GLY B 32 1 7
HELIX 20 AC2 ASP B 83 LEU B 88 1 6
HELIX 21 AC3 SER B 95 GLN B 105 1 11
HELIX 22 AC4 GLY B 142 ASP B 144 5 3
HELIX 23 AC5 GLU B 203 MET B 210 1 8
HELIX 24 AC6 TYR B 480 ALA B 485 1 6
HELIX 25 AC7 SER B 543 GLN B 554 1 12
HELIX 26 AC8 GLY B 570 GLY B 575 1 6
HELIX 27 AC9 ALA B 576 TYR B 578 5 3
HELIX 28 AD1 THR B 583 GLN B 599 1 17
HELIX 29 AD2 SER B 613 HIS B 626 1 14
HELIX 30 AD3 ASP B 641 TYR B 645 5 5
HELIX 31 AD4 ASP B 646 ASP B 655 1 10
HELIX 32 AD5 LEU B 656 ALA B 659 5 4
HELIX 33 AD6 ASN B 660 SER B 668 1 9
HELIX 34 AD7 SER B 668 VAL B 673 1 6
HELIX 35 AD8 ASP B 674 ILE B 676 5 3
HELIX 36 AD9 PHE B 694 GLY B 708 1 15
HELIX 37 AE1 ARG B 724 LYS B 744 1 21
HELIX 38 AE2 THR C 26 GLY C 32 1 7
HELIX 39 AE3 ASP C 83 LEU C 88 1 6
HELIX 40 AE4 GLU C 203 MET C 210 1 8
HELIX 41 AE5 ARG C 542 GLN C 554 1 13
HELIX 42 AE6 GLY C 570 ALA C 576 1 7
HELIX 43 AE7 THR C 583 GLN C 599 1 17
HELIX 44 AE8 SER C 613 HIS C 626 1 14
HELIX 45 AE9 ASP C 641 TYR C 645 5 5
HELIX 46 AF1 ASP C 646 ASP C 655 1 10
HELIX 47 AF2 LEU C 656 ALA C 659 5 4
HELIX 48 AF3 ASN C 660 SER C 668 1 9
HELIX 49 AF4 SER C 668 VAL C 673 1 6
HELIX 50 AF5 ASP C 674 ILE C 676 5 3
HELIX 51 AF6 PHE C 694 GLY C 708 1 15
HELIX 52 AF7 ARG C 724 LYS C 744 1 21
HELIX 53 AF8 THR D 26 GLY D 32 1 7
HELIX 54 AF9 ASP D 83 LEU D 88 1 6
HELIX 55 AG1 SER D 95 GLN D 105 1 11
HELIX 56 AG2 GLU D 203 MET D 210 1 8
HELIX 57 AG3 SER D 543 GLN D 554 1 12
HELIX 58 AG4 GLY D 570 GLY D 575 1 6
HELIX 59 AG5 ALA D 576 TYR D 578 5 3
HELIX 60 AG6 THR D 583 SER D 598 1 16
HELIX 61 AG7 SER D 613 HIS D 626 1 14
HELIX 62 AG8 ASP D 641 TYR D 645 5 5
HELIX 63 AG9 ASP D 646 ASP D 655 1 10
HELIX 64 AH1 LEU D 656 ALA D 659 5 4
HELIX 65 AH2 ASN D 660 SER D 668 1 9
HELIX 66 AH3 SER D 668 VAL D 673 1 6
HELIX 67 AH4 ASP D 674 ILE D 676 5 3
HELIX 68 AH5 PHE D 694 GLY D 708 1 15
HELIX 69 AH6 ARG D 724 LYS D 744 1 21
SHEET 1 AA1 4 LEU A 41 ILE A 46 0
SHEET 2 AA1 4 ARG A 52 GLY A 58 -1 O LEU A 56 N THR A 42
SHEET 3 AA1 4 ARG A 65 ASP A 72 -1 O TRP A 69 N PHE A 55
SHEET 4 AA1 4 GLN A 77 VAL A 82 -1 O GLN A 77 N ASP A 72
SHEET 1 AA2 4 LEU A 41 ILE A 46 0
SHEET 2 AA2 4 ARG A 52 GLY A 58 -1 O LEU A 56 N THR A 42
SHEET 3 AA2 4 ARG A 65 ASP A 72 -1 O TRP A 69 N PHE A 55
SHEET 4 AA2 4 SER A 111 GLY A 112 1 O SER A 111 N LEU A 66
SHEET 1 AA3 4 GLN A 117 TRP A 118 0
SHEET 2 AA3 4 ALA A 124 LEU A 129 -1 O LEU A 126 N GLN A 117
SHEET 3 AA3 4 GLU A 132 ASP A 137 -1 O GLU A 132 N LEU A 129
SHEET 4 AA3 4 VAL A 146 LYS A 148 -1 O ARG A 147 N PHE A 135
SHEET 1 AA4 4 THR A 157 ILE A 161 0
SHEET 2 AA4 4 PHE A 167 ARG A 172 -1 O ILE A 171 N THR A 157
SHEET 3 AA4 4 ASN A 175 ASP A 180 -1 O ILE A 179 N VAL A 168
SHEET 4 AA4 4 LYS A 185 GLN A 188 -1 O VAL A 187 N ALA A 178
SHEET 1 AA5 3 ILE A 197 ASN A 199 0
SHEET 2 AA5 3 ILE A 225 ASP A 231 -1 O ILE A 230 N GLY A 198
SHEET 3 AA5 3 TYR A 216 TRP A 218 -1 N TRP A 217 O ALA A 226
SHEET 1 AA6 4 ILE A 197 ASN A 199 0
SHEET 2 AA6 4 ILE A 225 ASP A 231 -1 O ILE A 230 N GLY A 198
SHEET 3 AA6 4 ARG A 264 ILE A 270 -1 O GLY A 268 N PHE A 227
SHEET 4 AA6 4 ARG A 279 ILE A 281 -1 O ILE A 281 N LEU A 267
SHEET 1 AA7 2 VAL A 237 TYR A 244 0
SHEET 2 AA7 2 ARG A 247 ARG A 254 -1 O VAL A 251 N ARG A 240
SHEET 1 AA8 4 ILE A 289 ASP A 298 0
SHEET 2 AA8 4 ARG A 301 SER A 308 -1 O GLN A 307 N TYR A 290
SHEET 3 AA8 4 LYS A 313 THR A 320 -1 O THR A 319 N LEU A 302
SHEET 4 AA8 4 GLN A 326 THR A 333 -1 O ARG A 327 N GLU A 318
SHEET 1 AA9 4 ARG A 345 PHE A 346 0
SHEET 2 AA9 4 PHE A 352 SER A 356 -1 O LEU A 353 N ARG A 345
SHEET 3 AA9 4 HIS A 363 ALA A 367 -1 O ALA A 367 N PHE A 352
SHEET 4 AA9 4 LEU A 374 ALA A 376 -1 O THR A 375 N VAL A 366
SHEET 1 AB1 4 VAL A 384 ASP A 391 0
SHEET 2 AB1 4 LEU A 396 GLY A 401 -1 O LEU A 396 N ASP A 391
SHEET 3 AB1 4 HIS A 410 PRO A 415 -1 O VAL A 414 N ALA A 397
SHEET 4 AB1 4 ARG A 422 ARG A 423 -1 O ARG A 422 N ALA A 413
SHEET 1 AB2 4 MET A 430 PHE A 435 0
SHEET 2 AB2 4 VAL A 441 SER A 447 -1 O SER A 445 N ALA A 432
SHEET 3 AB2 4 GLN A 454 LYS A 459 -1 O GLN A 454 N TRP A 446
SHEET 4 AB2 4 LYS A 464 THR A 467 -1 O LEU A 465 N LEU A 457
SHEET 1 AB3 8 THR A 490 THR A 496 0
SHEET 2 AB3 8 PRO A 503 ILE A 509 -1 O LEU A 508 N ALA A 491
SHEET 3 AB3 8 VAL A 557 LEU A 561 -1 O VAL A 558 N ILE A 509
SHEET 4 AB3 8 TYR A 520 PHE A 525 1 N PRO A 521 O VAL A 557
SHEET 5 AB3 8 VAL A 602 TRP A 612 1 O GLY A 608 N VAL A 524
SHEET 6 AB3 8 CYS A 632 GLY A 636 1 O GLY A 636 N GLY A 611
SHEET 7 AB3 8 LEU A 681 GLY A 686 1 O ILE A 684 N ALA A 635
SHEET 8 AB3 8 GLU A 712 TYR A 716 1 O GLU A 712 N LEU A 681
SHEET 1 AB4 4 LEU B 41 ILE B 46 0
SHEET 2 AB4 4 ARG B 52 GLY B 58 -1 O LEU B 56 N THR B 42
SHEET 3 AB4 4 ARG B 65 ASP B 72 -1 O TRP B 69 N PHE B 55
SHEET 4 AB4 4 GLN B 77 VAL B 82 -1 O GLN B 77 N ASP B 72
SHEET 1 AB5 4 LEU B 41 ILE B 46 0
SHEET 2 AB5 4 ARG B 52 GLY B 58 -1 O LEU B 56 N THR B 42
SHEET 3 AB5 4 ARG B 65 ASP B 72 -1 O TRP B 69 N PHE B 55
SHEET 4 AB5 4 SER B 111 GLY B 112 1 O SER B 111 N LEU B 66
SHEET 1 AB6 4 GLN B 117 TRP B 118 0
SHEET 2 AB6 4 ALA B 124 LEU B 129 -1 O LEU B 126 N GLN B 117
SHEET 3 AB6 4 GLU B 132 ASP B 137 -1 O TYR B 134 N PHE B 127
SHEET 4 AB6 4 VAL B 146 LYS B 148 -1 O ARG B 147 N PHE B 135
SHEET 1 AB7 4 THR B 157 ILE B 161 0
SHEET 2 AB7 4 PHE B 167 ARG B 172 -1 O ILE B 171 N THR B 157
SHEET 3 AB7 4 ASN B 175 ASP B 180 -1 O ILE B 179 N VAL B 168
SHEET 4 AB7 4 LYS B 185 GLN B 188 -1 O VAL B 187 N ALA B 178
SHEET 1 AB8 3 ILE B 197 ASN B 199 0
SHEET 2 AB8 3 ILE B 225 ASP B 231 -1 O ILE B 230 N GLY B 198
SHEET 3 AB8 3 TYR B 216 TRP B 218 -1 N TRP B 217 O ALA B 226
SHEET 1 AB9 4 ILE B 197 ASN B 199 0
SHEET 2 AB9 4 ILE B 225 ASP B 231 -1 O ILE B 230 N GLY B 198
SHEET 3 AB9 4 ARG B 264 ILE B 270 -1 O GLY B 268 N PHE B 227
SHEET 4 AB9 4 ARG B 279 ILE B 281 -1 O ILE B 281 N LEU B 267
SHEET 1 AC1 2 VAL B 237 VAL B 243 0
SHEET 2 AC1 2 THR B 248 ARG B 254 -1 O VAL B 251 N ARG B 240
SHEET 1 AC2 4 ILE B 289 ASP B 298 0
SHEET 2 AC2 4 ARG B 301 SER B 308 -1 O THR B 303 N ASP B 295
SHEET 3 AC2 4 LYS B 313 THR B 320 -1 O THR B 319 N LEU B 302
SHEET 4 AC2 4 GLN B 326 THR B 333 -1 O LEU B 329 N LEU B 316
SHEET 1 AC3 4 ARG B 345 PHE B 346 0
SHEET 2 AC3 4 PHE B 352 SER B 356 -1 O LEU B 353 N ARG B 345
SHEET 3 AC3 4 HIS B 363 ALA B 367 -1 O ALA B 367 N PHE B 352
SHEET 4 AC3 4 LEU B 374 ALA B 376 -1 O THR B 375 N VAL B 366
SHEET 1 AC4 4 VAL B 384 ASP B 391 0
SHEET 2 AC4 4 LEU B 396 GLY B 401 -1 O LEU B 396 N ASP B 391
SHEET 3 AC4 4 HIS B 410 PRO B 415 -1 O VAL B 414 N ALA B 397
SHEET 4 AC4 4 ARG B 422 ARG B 423 -1 O ARG B 422 N ALA B 413
SHEET 1 AC5 4 MET B 430 PHE B 435 0
SHEET 2 AC5 4 VAL B 441 SER B 448 -1 O VAL B 443 N THR B 434
SHEET 3 AC5 4 THR B 451 LYS B 459 -1 O GLN B 454 N TRP B 446
SHEET 4 AC5 4 LYS B 464 THR B 467 -1 O ALA B 466 N LEU B 457
SHEET 1 AC6 8 THR B 490 THR B 496 0
SHEET 2 AC6 8 PRO B 503 ILE B 509 -1 O LEU B 504 N LEU B 495
SHEET 3 AC6 8 VAL B 557 LEU B 561 -1 O VAL B 558 N ILE B 509
SHEET 4 AC6 8 TYR B 520 PHE B 525 1 N PRO B 521 O VAL B 557
SHEET 5 AC6 8 VAL B 602 TRP B 612 1 O GLY B 608 N VAL B 522
SHEET 6 AC6 8 CYS B 632 GLY B 636 1 O VAL B 634 N VAL B 609
SHEET 7 AC6 8 LEU B 681 GLY B 686 1 O ILE B 684 N ALA B 635
SHEET 8 AC6 8 GLU B 712 TYR B 716 1 O GLU B 712 N LEU B 681
SHEET 1 AC7 4 THR C 42 ILE C 46 0
SHEET 2 AC7 4 ARG C 52 GLY C 58 -1 O THR C 54 N GLN C 45
SHEET 3 AC7 4 ARG C 65 ASP C 72 -1 O TRP C 69 N PHE C 55
SHEET 4 AC7 4 THR C 78 VAL C 82 -1 O LEU C 81 N LEU C 68
SHEET 1 AC8 4 THR C 42 ILE C 46 0
SHEET 2 AC8 4 ARG C 52 GLY C 58 -1 O THR C 54 N GLN C 45
SHEET 3 AC8 4 ARG C 65 ASP C 72 -1 O TRP C 69 N PHE C 55
SHEET 4 AC8 4 SER C 111 GLY C 112 1 O SER C 111 N LEU C 66
SHEET 1 AC9 3 LEU C 125 LEU C 129 0
SHEET 2 AC9 3 GLU C 132 TYR C 136 -1 O TYR C 134 N PHE C 127
SHEET 3 AC9 3 ARG C 147 LYS C 148 -1 O ARG C 147 N PHE C 135
SHEET 1 AD1 4 THR C 157 ILE C 161 0
SHEET 2 AD1 4 PHE C 167 ARG C 172 -1 O ILE C 171 N THR C 157
SHEET 3 AD1 4 ASN C 175 ASP C 180 -1 O ILE C 179 N VAL C 168
SHEET 4 AD1 4 GLU C 186 GLN C 188 -1 O VAL C 187 N ALA C 178
SHEET 1 AD2 3 ILE C 197 ASN C 199 0
SHEET 2 AD2 3 ILE C 225 ASP C 231 -1 O ILE C 230 N GLY C 198
SHEET 3 AD2 3 TYR C 216 TRP C 218 -1 N TRP C 217 O ALA C 226
SHEET 1 AD3 4 ILE C 197 ASN C 199 0
SHEET 2 AD3 4 ILE C 225 ASP C 231 -1 O ILE C 230 N GLY C 198
SHEET 3 AD3 4 ARG C 264 ILE C 270 -1 O ARG C 264 N ASP C 231
SHEET 4 AD3 4 ARG C 279 ILE C 281 -1 O ILE C 281 N LEU C 267
SHEET 1 AD4 2 VAL C 237 VAL C 243 0
SHEET 2 AD4 2 THR C 248 ARG C 254 -1 O GLN C 253 N GLN C 238
SHEET 1 AD5 4 ILE C 289 ASP C 298 0
SHEET 2 AD5 4 ARG C 301 SER C 308 -1 O GLN C 307 N TYR C 290
SHEET 3 AD5 4 LYS C 313 THR C 320 -1 O THR C 319 N LEU C 302
SHEET 4 AD5 4 GLN C 326 THR C 333 -1 O ARG C 327 N GLU C 318
SHEET 1 AD6 4 ARG C 345 PHE C 346 0
SHEET 2 AD6 4 PHE C 352 SER C 356 -1 O LEU C 353 N ARG C 345
SHEET 3 AD6 4 HIS C 363 ALA C 367 -1 O TYR C 365 N TRP C 354
SHEET 4 AD6 4 LEU C 374 ALA C 376 -1 O THR C 375 N VAL C 366
SHEET 1 AD7 4 VAL C 384 ASP C 391 0
SHEET 2 AD7 4 LEU C 396 GLY C 401 -1 O LEU C 396 N ASP C 391
SHEET 3 AD7 4 HIS C 410 PRO C 415 -1 O VAL C 414 N ALA C 397
SHEET 4 AD7 4 ARG C 422 ARG C 423 -1 O ARG C 422 N ALA C 413
SHEET 1 AD8 4 MET C 430 PHE C 435 0
SHEET 2 AD8 4 VAL C 441 SER C 447 -1 O SER C 445 N ALA C 432
SHEET 3 AD8 4 GLN C 454 LYS C 459 -1 O PHE C 458 N PHE C 442
SHEET 4 AD8 4 LYS C 464 LEU C 469 -1 O ALA C 466 N LEU C 457
SHEET 1 AD9 8 THR C 490 THR C 496 0
SHEET 2 AD9 8 PRO C 503 ILE C 509 -1 O LEU C 508 N ALA C 491
SHEET 3 AD9 8 VAL C 557 LEU C 561 -1 O VAL C 558 N ILE C 509
SHEET 4 AD9 8 TYR C 520 PHE C 525 1 N PHE C 525 O PHE C 559
SHEET 5 AD9 8 VAL C 602 TRP C 612 1 O GLY C 608 N VAL C 524
SHEET 6 AD9 8 CYS C 632 GLY C 636 1 O VAL C 634 N VAL C 609
SHEET 7 AD9 8 LEU C 681 GLY C 686 1 O ILE C 684 N ALA C 635
SHEET 8 AD9 8 GLU C 712 TYR C 716 1 O GLU C 712 N LEU C 681
SHEET 1 AE1 4 LEU D 41 ILE D 46 0
SHEET 2 AE1 4 ARG D 52 LYS D 59 -1 O LEU D 56 N THR D 42
SHEET 3 AE1 4 ASP D 62 ASP D 72 -1 O TRP D 69 N PHE D 55
SHEET 4 AE1 4 GLN D 77 VAL D 82 -1 O LEU D 81 N LEU D 68
SHEET 1 AE2 4 LEU D 41 ILE D 46 0
SHEET 2 AE2 4 ARG D 52 LYS D 59 -1 O LEU D 56 N THR D 42
SHEET 3 AE2 4 ASP D 62 ASP D 72 -1 O TRP D 69 N PHE D 55
SHEET 4 AE2 4 SER D 111 GLY D 112 1 O SER D 111 N ASN D 64
SHEET 1 AE3 4 GLN D 117 TRP D 118 0
SHEET 2 AE3 4 ALA D 124 LEU D 129 -1 O LEU D 126 N GLN D 117
SHEET 3 AE3 4 GLU D 132 ASP D 137 -1 O TYR D 134 N PHE D 127
SHEET 4 AE3 4 VAL D 146 LYS D 148 -1 O ARG D 147 N PHE D 135
SHEET 1 AE4 4 THR D 157 ILE D 161 0
SHEET 2 AE4 4 PHE D 167 ARG D 172 -1 O ILE D 171 N THR D 157
SHEET 3 AE4 4 ASN D 175 ASP D 180 -1 O ILE D 179 N VAL D 168
SHEET 4 AE4 4 GLU D 186 GLN D 188 -1 O VAL D 187 N ALA D 178
SHEET 1 AE5 3 ILE D 197 ASN D 199 0
SHEET 2 AE5 3 ILE D 225 ASP D 231 -1 O ILE D 230 N GLY D 198
SHEET 3 AE5 3 TYR D 216 TRP D 218 -1 N TRP D 217 O ALA D 226
SHEET 1 AE6 4 ILE D 197 ASN D 199 0
SHEET 2 AE6 4 ILE D 225 ASP D 231 -1 O ILE D 230 N GLY D 198
SHEET 3 AE6 4 ARG D 264 ILE D 270 -1 O GLY D 268 N PHE D 227
SHEET 4 AE6 4 ARG D 279 ILE D 281 -1 O ILE D 281 N LEU D 267
SHEET 1 AE7 2 VAL D 237 GLN D 238 0
SHEET 2 AE7 2 GLN D 253 ARG D 254 -1 O GLN D 253 N GLN D 238
SHEET 1 AE8 4 ILE D 289 ASP D 298 0
SHEET 2 AE8 4 ARG D 301 SER D 308 -1 O ARG D 301 N ARG D 297
SHEET 3 AE8 4 LYS D 313 THR D 320 -1 O THR D 319 N LEU D 302
SHEET 4 AE8 4 GLN D 326 THR D 333 -1 O LEU D 329 N LEU D 316
SHEET 1 AE9 4 ARG D 345 PHE D 346 0
SHEET 2 AE9 4 PHE D 352 SER D 356 -1 O LEU D 353 N ARG D 345
SHEET 3 AE9 4 HIS D 363 ALA D 367 -1 O TYR D 365 N TRP D 354
SHEET 4 AE9 4 LEU D 374 ALA D 376 -1 O THR D 375 N VAL D 366
SHEET 1 AF1 4 VAL D 384 ASP D 391 0
SHEET 2 AF1 4 LEU D 396 GLY D 401 -1 O LEU D 396 N ASP D 391
SHEET 3 AF1 4 HIS D 410 PRO D 415 -1 O VAL D 414 N ALA D 397
SHEET 4 AF1 4 ARG D 422 ARG D 423 -1 O ARG D 422 N ALA D 413
SHEET 1 AF2 4 MET D 430 PHE D 435 0
SHEET 2 AF2 4 VAL D 441 SER D 447 -1 O VAL D 443 N THR D 434
SHEET 3 AF2 4 GLN D 454 LYS D 459 -1 O GLN D 454 N TRP D 446
SHEET 4 AF2 4 LYS D 464 THR D 467 -1 O LEU D 465 N LEU D 457
SHEET 1 AF3 8 THR D 490 THR D 496 0
SHEET 2 AF3 8 PRO D 503 ILE D 509 -1 O LEU D 508 N ALA D 491
SHEET 3 AF3 8 VAL D 557 LEU D 561 -1 O VAL D 558 N ILE D 509
SHEET 4 AF3 8 TYR D 520 PHE D 525 1 N VAL D 523 O VAL D 557
SHEET 5 AF3 8 VAL D 602 TRP D 612 1 O GLY D 608 N VAL D 524
SHEET 6 AF3 8 CYS D 632 GLY D 636 1 O GLY D 636 N GLY D 611
SHEET 7 AF3 8 LEU D 681 GLY D 686 1 O LEU D 682 N ALA D 635
SHEET 8 AF3 8 GLU D 712 TYR D 716 1 O GLU D 712 N LEU D 681
LINK OG SER A 613 C PRO A 802 1555 1555 1.47
LINK OG SER B 613 C PRO B 802 1555 1555 1.48
LINK OG SER D 613 C PRO D 802 1555 1555 1.47
LINK C LYS A 801 N PRO A 802 1555 1555 1.34
LINK C LYS B 801 N PRO B 802 1555 1555 1.33
LINK C LYS C 801 N PRO C 802 1555 1555 1.33
LINK C LYS D 801 N PRO D 802 1555 1555 1.33
SITE 1 AC1 6 ARG A 106 ILE A 107 ALA A 108 ALA A 109
SITE 2 AC1 6 HOH A 904 HOH A1281
SITE 1 AC2 7 LYS A 43 GLU A 98 ARG A 101 GLN A 105
SITE 2 AC2 7 ASP A 115 HOH A1061 HOH A1243
SITE 1 AC3 8 THR A 333 SER A 334 THR A 335 ARG A 358
SITE 2 AC3 8 HOH A1072 HOH A1214 HOH A1346 THR B 333
SITE 1 AC4 4 THR A 450 ARG A 484 HOH A1320 HOH A1338
SITE 1 AC5 3 THR B 450 ARG B 484 HOH B1292
SITE 1 AC6 10 LYS A 312 THR A 333 SER A 334 THR A 335
SITE 2 AC6 10 HOH A1198 THR B 331 THR B 333 ARG B 358
SITE 3 AC6 10 HOH B1139 HOH B1175
SITE 1 AC7 5 ALA B 498 ARG B 564 VAL B 584 ASP B 587
SITE 2 AC7 5 HOH B1186
SITE 1 AC8 7 GLY B 405 ALA B 406 PRO B 503 HIS B 505
SITE 2 AC8 7 ARG B 569 HOH B 948 HOH B 995
SITE 1 AC9 6 ARG B 106 ILE B 107 ALA B 108 ALA B 109
SITE 2 AC9 6 ARG B 724 HOH B 915
SITE 1 AD1 6 ARG B 293 VAL B 294 ASP B 295 ASN B 342
SITE 2 AD1 6 HOH B1183 HOH B1200
SITE 1 AD2 5 ARG B 106 TYR B 527 LYS B 801 PRO B 802
SITE 2 AD2 5 HOH B 945
SITE 1 AD3 5 ASP B 449 THR B 490 ALA B 491 TYR B 492
SITE 2 AD3 5 ARG B 537
SITE 1 AD4 11 GLU B 97 ARG B 101 VAL B 201 ALA B 202
SITE 2 AD4 11 ASP B 207 HIS B 213 THR B 214 HOH B 916
SITE 3 AD4 11 HOH B1000 HOH B1114 HOH B1180
SITE 1 AD5 8 GLU B 98 ARG B 101 GLN B 105 ASP B 115
SITE 2 AD5 8 HOH B 939 HOH B1057 HOH B1085 HOH B1157
SITE 1 AD6 9 ARG C 542 SER C 543 ASP C 544 TRP C 612
SITE 2 AD6 9 ARG C 731 HOH C 951 HOH C 953 HOH C1164
SITE 3 AD6 9 HOH C1389
SITE 1 AD7 5 THR C 31 GLY C 725 HOH C 925 HOH C1027
SITE 2 AD7 5 HOH C1114
SITE 1 AD8 3 HOH C1080 ARG D 564 ASP D 587
SITE 1 AD9 6 ARG D 106 ILE D 107 ALA D 108 ALA D 109
SITE 2 AD9 6 ARG D 724 HOH D 949
SITE 1 AE1 5 ASP D 121 PHE D 135 GLY D 165 LEU D 181
SITE 2 AE1 5 HOH D1128
SITE 1 AE2 7 THR D 450 VAL D 473 ARG D 484 HOH D 906
SITE 2 AE2 7 HOH D1003 HOH D1223 HOH D1310
SITE 1 AE3 8 LYS D 43 GLU D 98 ARG D 101 GLN D 105
SITE 2 AE3 8 ASP D 115 HOH D 901 HOH D 996 HOH D1165
SITE 1 AE4 12 ARG A 106 GLU A 208 GLU A 209 ASP A 211
SITE 2 AE4 12 TYR A 527 SER A 613 ASN A 614 TYR A 645
SITE 3 AE4 12 TYR A 649 ASN A 691 HOH A1226 HOH A1452
SITE 1 AE5 11 ARG B 106 GLU B 208 GLU B 209 TYR B 527
SITE 2 AE5 11 SER B 613 ASN B 614 TYR B 645 TYR B 649
SITE 3 AE5 11 ASN B 691 GOL B 809 HOH B1341
SITE 1 AE6 14 TYR B 527 TRP B 612 ASN B 614 GLY B 615
SITE 2 AE6 14 GLY B 616 TYR B 617 GLY B 636 ALA B 637
SITE 3 AE6 14 TYR B 645 TYR B 649 VAL B 692 HIS B 721
SITE 4 AE6 14 LYS B 801 GOL B 809
SITE 1 AE7 9 GLU C 209 TYR C 527 SER C 613 ASN C 614
SITE 2 AE7 9 TYR C 645 TYR C 649 ASN C 691 HOH C 901
SITE 3 AE7 9 HOH C1252
SITE 1 AE8 10 ARG D 106 GLU D 208 GLU D 209 TYR D 527
SITE 2 AE8 10 SER D 613 ASN D 614 TYR D 645 TYR D 649
SITE 3 AE8 10 ASN D 691 HOH D1448
SITE 1 AE9 13 TYR D 527 TRP D 612 ASN D 614 GLY D 615
SITE 2 AE9 13 GLY D 616 TYR D 617 GLY D 636 ALA D 637
SITE 3 AE9 13 PRO D 638 TYR D 645 TYR D 649 HIS D 721
SITE 4 AE9 13 LYS D 801
CRYST1 88.656 104.487 112.838 67.42 68.83 65.46 P 1 4
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 0.011280 -0.005149 -0.003068 0.00000
SCALE2 0.000000 0.010521 -0.003020 0.00000
SCALE3 0.000000 0.000000 0.009888 0.00000
TER 5661 PRO A 745
TER 11322 PRO B 745
TER 16702 PRO C 745
TER 22274 PRO D 745
MASTER 709 0 29 69 195 0 62 625330 4 140 232
END |