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HEADER HYDROLASE/COMPLEX 22-JUN-04 1W1I
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR CD26)
TITLE 2 IN COMPLEX WITH ADENOSINE DEAMINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,
COMPND 4 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND 5 CHAIN: A, B, C, D;
COMPND 6 FRAGMENT: EXTRACELLULAR DOMAIN 39 - 766;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ADENOSINE DEAMINASE;
COMPND 11 SYNONYM: ADENOSINE AMINOHYDROLASE;
COMPND 12 CHAIN: E, F, G, H;
COMPND 13 EC: 3.5.4.4
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: SF9 CELLS;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTC;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGAN: KIDNEY;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE;
SOURCE 12 TISSUE: INTESTINAL MUCOSA;
SOURCE 13 OTHER_DETAILS: SIGMA, TYPE VI, FROM CALF INTESTINAL MUCOSA
KEYWDS DIPETIDYL PEPTIDASE IV, DPPIV, CD26, ALPHA/BETA-HYDROLASE
KEYWDS 2 FOLD, BETA-PROPELLER FOLD, PROTEIN-PROTEIN COMPLEX,
KEYWDS 3 ADENOSINE DEAMINASE, ADA, SERINE PROTEASE, AMINOPEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
REVDAT 1 02-SEP-04 1W1I 0
JRNL AUTH W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
JRNL TITL CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV
JRNL TITL 2 (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE DEAMINASE
JRNL TITL 3 REVEALS A HIGHLY AMPHIPHILIC INTERFACE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC 5.1.9999
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) : 3.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.46
REMARK 3 NUMBER OF REFLECTIONS : 98926
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) : 0.22445
REMARK 3 R VALUE (WORKING SET) : 0.22377
REMARK 3 FREE R VALUE : 0.25704
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2048
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) : 3.030
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.108
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6906
REMARK 3 BIN R VALUE (WORKING SET) : 0.367
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.417
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 35087
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 790
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.459
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.45
REMARK 3 B22 (A**2) : -2.35
REMARK 3 B33 (A**2) : -1.47
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 1.75
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.498
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.378
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 41313 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 63508 ; 1.340 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 8614 ; 5.963 ; 7.500
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1772 ;34.827 ;24.108
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5999 ;19.946 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 184 ;19.790 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5519 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 45884 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 17208 ; 0.232 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1927 ; 0.187 ; 0.500
REMARK 3 SYMMETRY VDW REFINED (A): 58 ; 0.275 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED (A): 7 ; 0.282 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED (A): 1927 ; 0.187 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 21822 ; 0.646 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 34915 ; 1.141 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 17155 ; 0.608 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 15310 ; 1.053 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 40 A 70 1
REMARK 3 1 B 40 B 70 1
REMARK 3 1 C 40 C 70 1
REMARK 3 1 D 40 D 70 1
REMARK 3 2 A 74 A 281 1
REMARK 3 2 B 74 B 281 1
REMARK 3 2 C 74 C 281 1
REMARK 3 2 D 74 D 281 1
REMARK 3 3 A 296 A 331 1
REMARK 3 3 B 296 B 331 1
REMARK 3 3 C 296 C 331 1
REMARK 3 3 D 296 D 331 1
REMARK 3 4 A 347 A 764 1
REMARK 3 4 B 347 B 764 1
REMARK 3 4 C 347 C 764 1
REMARK 3 4 D 347 D 764 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 5696 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 5696 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 5696 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 5696 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 5696 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 5696 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 5696 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 5696 ; 0.04 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 6 E 55 1
REMARK 3 1 F 6 F 55 1
REMARK 3 1 G 6 G 55 1
REMARK 3 1 H 6 H 55 1
REMARK 3 2 E 217 E 237 1
REMARK 3 2 F 217 F 237 1
REMARK 3 2 G 217 G 237 1
REMARK 3 2 H 217 H 237 1
REMARK 3 3 E 85 E 108 1
REMARK 3 3 F 85 F 108 1
REMARK 3 3 G 85 G 108 1
REMARK 3 3 H 85 H 108 1
REMARK 3 4 E 144 E 215 1
REMARK 3 4 F 144 F 215 1
REMARK 3 4 G 144 G 215 1
REMARK 3 4 H 144 H 215 1
REMARK 3 5 E 119 E 126 1
REMARK 3 5 F 119 F 126 1
REMARK 3 5 G 119 G 126 1
REMARK 3 5 H 119 H 126 1
REMARK 3 6 E 57 E 72 1
REMARK 3 6 F 57 F 72 1
REMARK 3 6 G 57 G 72 1
REMARK 3 6 H 57 H 72 1
REMARK 3 7 E 241 E 280 1
REMARK 3 7 F 241 F 280 1
REMARK 3 7 G 241 G 280 1
REMARK 3 7 H 241 H 280 1
REMARK 3 8 E 338 E 351 1
REMARK 3 8 F 338 F 351 1
REMARK 3 8 G 338 G 351 1
REMARK 3 8 H 338 H 351 1
REMARK 3 9 E 284 E 335 1
REMARK 3 9 F 284 F 335 1
REMARK 3 9 G 284 G 335 1
REMARK 3 9 H 284 H 335 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 E (A): 2372 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 2372 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 G (A): 2372 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 H (A): 2372 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 2 E (A**2): 2372 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 2372 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 2 G (A**2): 2372 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 2 H (A**2): 2372 ; 0.03 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 :1.20
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
REMARK 3 RIDING POSITIONS. RESIDUES 1-3 OF CHAINS E,F,G,H OF ADA
REMARK 3 ARE DISORDERED
REMARK 4
REMARK 4 1W1I COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 23-JUN-2004.
REMARK 100 THE EBI ID CODE IS EBI-20204.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-2003
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY BEAMLINE BL1
REMARK 200 BEAMLINE : BL1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.914
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (165MM)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100817
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.03
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 200 DATA REDUNDANCY : 2.3
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.4
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.10
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 ENTRIES 1N1M AND 1KRM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 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 79.03250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.25200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.03250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 84.25200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC
REMARK 300
REMARK 300 THE COMPLEX DESCRIBED BY REMARK 350 BELOW IS OF THE
REMARK 300 TYPE A2B2, WHERE CHAINS A AND B ARE IN CONTACT
REMARK 300 WITH EACH OTHER, AND EACH OF THESE CHAINS IS IN TURN
REMARK 300 IN COMPLEX WITH CHAINS F AND E RESPECTIVELY.
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, F, B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 E 1
REMARK 465 ALA E 2
REMARK 465 GLN E 3
REMARK 465 PRO E 356
REMARK 465 ALA E 357
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLN F 3
REMARK 465 PRO F 356
REMARK 465 ALA F 357
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 GLN G 3
REMARK 465 PRO G 356
REMARK 465 ALA G 357
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLN H 3
REMARK 465 PRO H 356
REMARK 465 ALA H 357
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR F 351 N
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 LEU A 246 CA - CB - CG ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU C 246 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU D 300 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 THR E 176 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU E 325 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ALA E 350 CA - C - N ANGL. DEV. = -46.1 DEGREES
REMARK 500 ALA E 350 O - C - N ANGL. DEV. = -52.0 DEGREES
REMARK 500 TYR E 351 N - CA - C ANGL. DEV. = 48.8 DEGREES
REMARK 500 TYR E 351 N - CA - CB ANGL. DEV. = -20.9 DEGREES
REMARK 500 LEU F 325 CA - CB - CG ANGL. DEV. = 13.0 DEGREES
REMARK 500 ASP G 77 CB - CG - OD2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 LEU G 325 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 PHE H 283 N - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500 LEU H 325 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 O TYR E 240 N THR E 242 2.01
REMARK 500 N TYR E 351 O LEU F 347 1.94
REMARK 500 N TYR E 351 O TYR F 348 2.04
REMARK 500 OH TYR F 240 OG SER F 266 2.01
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 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
REMARK 500 GLU E 113 -110.89 9.19
REMARK 500 HIS E 238 -82.49 70.89
REMARK 500 ASP E 295 -84.12 70.19
REMARK 500 HIS F 238 -94.10 63.18
REMARK 500 ASP F 295 -86.03 70.27
REMARK 500 HIS G 238 -102.28 74.03
REMARK 500 ASP G 295 -83.50 69.55
REMARK 500 HIS H 238 -84.52 64.82
REMARK 500 ASP H 295 -84.36 70.94
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU F 337 ASP F 338 149.62
REMARK 500 GLU H 113 PRO H 114 149.40
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM ZN ZN E 501 THE COORDINATION ANGLES ARE:
REMARK 600 1 ASP 295E OD1
REMARK 600 2 HIS 15E NE2 75.6
REMARK 600 3 HIS 17E NE2 90.3 112.6
REMARK 600 4 HIS 214E NE2 162.3 87.4 101.1
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM ZN ZN F 501 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 15F NE2
REMARK 600 2 HIS 17F NE2 105.8
REMARK 600 3 ASP 295F OD1 74.6 89.6
REMARK 600 4 HIS 214F NE2 84.6 97.0 159.2
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM ZN ZN G 501 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 214G NE2
REMARK 600 2 HIS 17G NE2 99.4
REMARK 600 3 ASP 295G OD1 161.8 90.4
REMARK 600 4 HIS 15G NE2 85.6 111.3 76.5
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM ZN ZN H 501 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 15H NE2
REMARK 600 2 HIS 17H NE2 108.1
REMARK 600 3 HIS 214H NE2 85.9 98.3
REMARK 600 4 ASP 295H OD1 75.7 88.3 161.5
REMARK 600 1 2 3
REMARK 600
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN E
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN F
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN G
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN H
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J2E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN
REMARK 900 COMPLEX WITH ANINHIBITOR
REMARK 900 RELATED ID: 1NU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)
REMARK 900 RELATED ID: 1NU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL
REMARK 900 PEPTIDASE IV (DPP-IV)IN COMPLEX WITH
REMARK 900 DIPROTIN A (ILI)
REMARK 900 RELATED ID: 1PFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL
REMARK 900 PEPTIDASE IV /CD26
REMARK 900 RELATED ID: 1KRM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOVINE ADENOSINE
REMARK 900 DEAMINASE COMPLEXEDWITH 6-HYDROXYL-1,6-
REMARK 900 DIHYDROPURINE RIBOSIDE
REMARK 900 RELATED ID: 1NDV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE
REMARK 900 COMPLEXED WITHFR117016
REMARK 900 RELATED ID: 1NDW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE
REMARK 900 COMPLEXED WITHFR221647
REMARK 900 RELATED ID: 1NDY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE
REMARK 900 COMPLEXED WITHFR230513
REMARK 900 RELATED ID: 1NDZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE
REMARK 900 COMPLEXED WITHFR235999
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICTS DESCRIBED WITH ANNOTATION FOR THIS
REMARK 999 REMARK HAS BEEN DESCRIBED IN J. PHARM. BIOMED. ANAL.
REMARK 999 14:1513-1519(1996). PUBMED ID: 8877857.
DBREF 1W1I A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 1W1I B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 1W1I C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 1W1I D 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 1W1I E 1 357 UNP P56658 ADA_BOVIN 0 356
DBREF 1W1I F 1 357 UNP P56658 ADA_BOVIN 0 356
DBREF 1W1I G 1 357 UNP P56658 ADA_BOVIN 0 356
DBREF 1W1I H 1 357 UNP P56658 ADA_BOVIN 0 356
SEQADV 1W1I ASP E 8 UNP P56658 ASN 7 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS E 32 UNP P56658 ARG 31 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG E 33 UNP P56658 LYS 32 CONFLICT SEE REMARK 999
SEQADV 1W1I LEU E 47 UNP P56658 GLN 46 CONFLICT
SEQADV 1W1I THR E 57 UNP P56658 SER 56 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP E 60 UNP P56658 GLU 59 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP E 77 UNP P56658 GLU 76 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE E 79 UNP P56658 VAL 78 CONFLICT SEE REMARK 999
SEQADV 1W1I GLN E 199 UNP P56658 LYS 198 VARIANT
SEQADV 1W1I THR E 246 UNP P56658 ALA 245 VARIANT
SEQADV 1W1I ILE E 261 UNP P56658 VAL 260 CONFLICT SEE REMARK 999
SEQADV 1W1I ALA E 279 UNP P56658 PRO 278 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE E 281 UNP P56658 VAL 280 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS E 313 UNP P56658 ASN 312 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP E 314 UNP P56658 GLU 313 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG E 352 UNP P56658 GLY 351 VARIANT
SEQADV 1W1I ASP F 8 UNP P56658 ASN 7 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS F 32 UNP P56658 ARG 31 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG F 33 UNP P56658 LYS 32 CONFLICT SEE REMARK 999
SEQADV 1W1I LEU F 47 UNP P56658 GLN 46 CONFLICT
SEQADV 1W1I THR F 57 UNP P56658 SER 56 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP F 60 UNP P56658 GLU 59 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP F 77 UNP P56658 GLU 76 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE F 79 UNP P56658 VAL 78 CONFLICT SEE REMARK 999
SEQADV 1W1I GLN F 199 UNP P56658 LYS 198 VARIANT
SEQADV 1W1I THR F 246 UNP P56658 ALA 245 VARIANT
SEQADV 1W1I ILE F 261 UNP P56658 VAL 260 CONFLICT SEE REMARK 999
SEQADV 1W1I ALA F 279 UNP P56658 PRO 278 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE F 281 UNP P56658 VAL 280 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS F 313 UNP P56658 ASN 312 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP F 314 UNP P56658 GLU 313 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG F 352 UNP P56658 GLY 351 VARIANT
SEQADV 1W1I ASP G 8 UNP P56658 ASN 7 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS G 32 UNP P56658 ARG 31 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG G 33 UNP P56658 LYS 32 CONFLICT SEE REMARK 999
SEQADV 1W1I LEU G 47 UNP P56658 GLN 46 CONFLICT
SEQADV 1W1I THR G 57 UNP P56658 SER 56 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP G 60 UNP P56658 GLU 59 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP G 77 UNP P56658 GLU 76 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE G 79 UNP P56658 VAL 78 CONFLICT SEE REMARK 999
SEQADV 1W1I GLN G 199 UNP P56658 LYS 198 VARIANT
SEQADV 1W1I THR G 246 UNP P56658 ALA 245 VARIANT
SEQADV 1W1I ILE G 261 UNP P56658 VAL 260 CONFLICT SEE REMARK 999
SEQADV 1W1I ALA G 279 UNP P56658 PRO 278 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE G 281 UNP P56658 VAL 280 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS G 313 UNP P56658 ASN 312 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP G 314 UNP P56658 GLU 313 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG G 352 UNP P56658 GLY 351 VARIANT
SEQADV 1W1I ASP H 8 UNP P56658 ASN 7 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS H 32 UNP P56658 ARG 31 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG H 33 UNP P56658 LYS 32 CONFLICT SEE REMARK 999
SEQADV 1W1I LEU H 47 UNP P56658 GLN 46 CONFLICT
SEQADV 1W1I THR H 57 UNP P56658 SER 56 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP H 60 UNP P56658 GLU 59 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP H 77 UNP P56658 GLU 76 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE H 79 UNP P56658 VAL 78 CONFLICT SEE REMARK 999
SEQADV 1W1I GLN H 199 UNP P56658 LYS 198 VARIANT
SEQADV 1W1I THR H 246 UNP P56658 ALA 245 VARIANT
SEQADV 1W1I ILE H 261 UNP P56658 VAL 260 CONFLICT SEE REMARK 999
SEQADV 1W1I ALA H 279 UNP P56658 PRO 278 CONFLICT SEE REMARK 999
SEQADV 1W1I ILE H 281 UNP P56658 VAL 280 CONFLICT SEE REMARK 999
SEQADV 1W1I LYS H 313 UNP P56658 ASN 312 CONFLICT SEE REMARK 999
SEQADV 1W1I ASP H 314 UNP P56658 GLU 313 CONFLICT SEE REMARK 999
SEQADV 1W1I ARG H 352 UNP P56658 GLY 351 VARIANT
SEQRES 1 A 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 C 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 C 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 C 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 C 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 C 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 C 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 C 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 C 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 C 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 C 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 C 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 C 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 C 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 C 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 C 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 C 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 C 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 C 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 C 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 C 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 C 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 C 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 C 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 C 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 C 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 C 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 C 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 C 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 C 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 C 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 C 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 D 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 D 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 D 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 D 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 D 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 D 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 D 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 D 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 D 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 D 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 D 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 D 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 D 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 D 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 D 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 D 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 D 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 D 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 D 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 D 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 D 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 D 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 D 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 D 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 D 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 D 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 D 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 D 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 D 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 D 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 D 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 D 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 D 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 D 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 D 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 D 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 D 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 D 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 D 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 D 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 D 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 D 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 D 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 D 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 E 357 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 E 357 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 E 357 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 E 357 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 E 357 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 E 357 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 E 357 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 E 357 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 E 357 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 E 357 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 E 357 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 E 357 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 E 357 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 E 357 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 E 357 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 E 357 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 E 357 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 E 357 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 E 357 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 E 357 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 E 357 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 E 357 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 E 357 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 E 357 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 E 357 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 E 357 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 E 357 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 E 357 ARG MET PRO SER PRO ALA
SEQRES 1 F 357 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 F 357 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 F 357 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 F 357 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 F 357 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 F 357 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 F 357 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 F 357 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 F 357 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 F 357 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 F 357 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 F 357 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 F 357 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 F 357 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 F 357 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 F 357 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 F 357 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 F 357 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 F 357 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 F 357 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 F 357 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 F 357 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 F 357 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 F 357 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 F 357 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 F 357 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 F 357 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 F 357 ARG MET PRO SER PRO ALA
SEQRES 1 G 357 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 G 357 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 G 357 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 G 357 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 G 357 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 G 357 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 G 357 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 G 357 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 G 357 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 G 357 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 G 357 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 G 357 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 G 357 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 G 357 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 G 357 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 G 357 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 G 357 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 G 357 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 G 357 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 G 357 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 G 357 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 G 357 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 G 357 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 G 357 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 G 357 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 G 357 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 G 357 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 G 357 ARG MET PRO SER PRO ALA
SEQRES 1 H 357 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 H 357 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 H 357 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 H 357 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 H 357 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 H 357 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 H 357 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 H 357 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 H 357 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 H 357 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 H 357 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 H 357 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 H 357 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 H 357 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 H 357 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 H 357 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 H 357 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 H 357 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 H 357 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 H 357 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 H 357 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 H 357 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 H 357 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 H 357 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 H 357 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 H 357 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 H 357 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 H 357 ARG MET PRO SER PRO ALA
HET NAG A 800 14
HET NAG A 801 14
HET AFL A 802 10
HET NAG A 810 14
HET NAG A 811 14
HET NAG A 820 14
HET NAG A 821 14
HET NAG A 830 14
HET NAG A 831 14
HET BMA A 832 11
HET MAN A 833 11
HET NAG A 840 14
HET NAG A 850 14
HET NDG A 860 14
HET NDG A 870 14
HET NAG B 800 14
HET AFL B 802 10
HET NAG B 810 14
HET NAG B 820 14
HET NAG B 821 14
HET NAG B 830 14
HET NAG B 831 14
HET BMA B 832 11
HET MAN B 833 11
HET NAG B 840 14
HET NAG B 850 14
HET NAG B 851 14
HET NDG B 860 14
HET NAG B 870 14
HET NAG C 800 14
HET NAG C 801 14
HET AFL C 802 10
HET NAG C 810 14
HET NAG C 811 14
HET NAG C 820 14
HET NAG C 821 14
HET NAG C 830 14
HET NAG C 831 14
HET BMA C 832 11
HET MAN C 833 11
HET NAG C 840 14
HET NAG C 850 14
HET NAG C 851 14
HET NAG C 860 14
HET NAG C 870 14
HET NAG D 800 14
HET AFL D 802 10
HET NAG D 810 14
HET NAG D 820 14
HET NAG D 821 14
HET NAG D 830 14
HET NAG D 831 14
HET BMA D 832 11
HET MAN D 833 11
HET NAG D 840 14
HET NAG D 850 14
HET NAG D 851 14
HET NAG D 860 14
HET NAG D 870 14
HET ZN E 501 1
HET ZN F 501 1
HET ZN G 501 1
HET ZN H 501 1
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM AFL BETA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 9 ZN 4(ZN1 2+)
FORMUL 12 NAG 44(C8 H15 N1 O6)
FORMUL 13 MAN 5(C6 H12 O6)
FORMUL 14 BMA 4(C6 H12 O6)
FORMUL 15 AFL 4(C6 H12 O5)
FORMUL 16 NDG 3(C8 H15 N1 O6)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 ASP A 274 LEU A 276 5 3
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 ASN A 506 1 10
HELIX 8 8 ASN A 562 ASN A 572 1 11
HELIX 9 9 GLY A 587 HIS A 592 1 6
HELIX 10 10 ALA A 593 ASN A 595 5 3
HELIX 11 11 THR A 600 MET A 616 1 17
HELIX 12 12 SER A 630 GLY A 641 1 12
HELIX 13 13 ARG A 658 TYR A 662 5 5
HELIX 14 14 ASP A 663 GLY A 672 1 10
HELIX 15 15 ASN A 679 ASN A 685 1 7
HELIX 16 16 VAL A 688 VAL A 698 5 11
HELIX 17 17 HIS A 712 VAL A 726 1 15
HELIX 18 18 SER A 744 SER A 764 1 21
HELIX 19 19 THR B 44 ASN B 51 1 8
HELIX 20 20 ASP B 200 VAL B 207 1 8
HELIX 21 21 ASP B 274 LEU B 276 5 3
HELIX 22 22 PRO B 290 ILE B 295 1 6
HELIX 23 23 LEU B 340 GLN B 344 5 5
HELIX 24 24 GLU B 421 MET B 425 5 5
HELIX 25 25 SER B 446 ASN B 450 5 5
HELIX 26 26 ASN B 497 ASN B 506 1 10
HELIX 27 27 ASN B 562 ASN B 572 1 11
HELIX 28 28 GLY B 587 HIS B 592 1 6
HELIX 29 29 ALA B 593 ASN B 595 5 3
HELIX 30 30 THR B 600 MET B 616 1 17
HELIX 31 31 SER B 630 GLY B 641 1 12
HELIX 32 32 ARG B 658 TYR B 662 5 5
HELIX 33 33 ASP B 663 GLY B 672 1 10
HELIX 34 34 ASN B 679 ASN B 685 1 7
HELIX 35 35 VAL B 688 VAL B 698 5 11
HELIX 36 36 HIS B 712 VAL B 726 1 15
HELIX 37 37 SER B 744 SER B 764 1 21
HELIX 38 38 THR C 44 LYS C 50 1 7
HELIX 39 39 ASP C 200 VAL C 207 1 8
HELIX 40 40 ASP C 274 LEU C 276 5 3
HELIX 41 41 PRO C 290 ILE C 295 1 6
HELIX 42 42 VAL C 341 GLN C 344 5 4
HELIX 43 43 GLU C 421 MET C 425 5 5
HELIX 44 44 SER C 446 ASN C 450 5 5
HELIX 45 45 ASN C 497 ASN C 506 1 10
HELIX 46 46 ASN C 562 ASN C 572 1 11
HELIX 47 47 GLY C 587 HIS C 592 1 6
HELIX 48 48 ALA C 593 ASN C 595 5 3
HELIX 49 49 THR C 600 MET C 616 1 17
HELIX 50 50 SER C 630 GLY C 641 1 12
HELIX 51 51 ARG C 658 TYR C 662 5 5
HELIX 52 52 ASP C 663 GLY C 672 1 10
HELIX 53 53 ASN C 679 ASN C 685 1 7
HELIX 54 54 VAL C 688 VAL C 698 5 11
HELIX 55 55 HIS C 712 GLY C 727 1 16
HELIX 56 56 SER C 744 SER C 764 1 21
HELIX 57 57 THR D 44 ASN D 51 1 8
HELIX 58 58 ASP D 200 VAL D 207 1 8
HELIX 59 59 ASP D 274 LEU D 276 5 3
HELIX 60 60 PRO D 290 ILE D 295 1 6
HELIX 61 61 VAL D 341 GLN D 344 5 4
HELIX 62 62 GLU D 421 MET D 425 5 5
HELIX 63 63 SER D 446 ASN D 450 5 5
HELIX 64 64 ASN D 497 ASN D 506 1 10
HELIX 65 65 ASN D 562 ASN D 572 1 11
HELIX 66 66 GLY D 587 HIS D 592 1 6
HELIX 67 67 ALA D 593 ASN D 595 5 3
HELIX 68 68 THR D 600 MET D 616 1 17
HELIX 69 69 SER D 630 GLY D 641 1 12
HELIX 70 70 ARG D 658 TYR D 662 5 5
HELIX 71 71 ASP D 663 GLY D 672 1 10
HELIX 72 72 ASN D 679 ASN D 685 1 7
HELIX 73 73 VAL D 688 VAL D 698 5 11
HELIX 74 74 HIS D 712 GLY D 727 1 16
HELIX 75 75 SER D 744 SER D 764 1 21
HELIX 76 76 ASP E 19 ALA E 21 5 3
HELIX 77 77 LYS E 23 GLY E 35 1 13
HELIX 78 78 THR E 42 GLY E 51 1 10
HELIX 79 79 THR E 57 ALA E 63 1 7
HELIX 80 80 LYS E 64 ALA E 73 1 10
HELIX 81 81 CYS E 75 ASP E 93 1 19
HELIX 82 82 PRO E 104 ALA E 108 5 5
HELIX 83 83 ILE E 115 GLN E 119 5 5
HELIX 84 84 THR E 125 GLY E 145 1 21
HELIX 85 85 GLN E 158 TYR E 172 1 15
HELIX 86 86 GLY E 190 LEU E 193 5 4
HELIX 87 87 PHE E 194 GLY E 208 1 15
HELIX 88 88 SER E 220 THR E 230 1 11
HELIX 89 89 TYR E 240 LEU E 243 5 4
HELIX 90 90 ASP E 245 GLU E 255 1 11
HELIX 91 91 CYS E 262 GLY E 270 1 9
HELIX 92 92 HIS E 278 ASP E 286 1 9
HELIX 93 93 THR E 303 ASP E 314 1 12
HELIX 94 94 THR E 318 SER E 333 1 16
HELIX 95 95 PRO E 336 TYR E 351 1 16
HELIX 96 96 ASP F 19 ALA F 21 5 3
HELIX 97 97 LYS F 23 GLY F 35 1 13
HELIX 98 98 THR F 42 GLY F 51 1 10
HELIX 99 99 THR F 57 ALA F 63 1 7
HELIX 100 100 LYS F 64 ALA F 73 1 10
HELIX 101 101 CYS F 75 ASP F 93 1 19
HELIX 102 102 PRO F 104 ALA F 108 5 5
HELIX 103 103 THR F 125 GLY F 145 1 21
HELIX 104 104 GLN F 158 TYR F 172 1 15
HELIX 105 105 GLY F 190 LEU F 193 5 4
HELIX 106 106 PHE F 194 GLY F 208 1 15
HELIX 107 107 SER F 220 THR F 230 1 11
HELIX 108 108 TYR F 240 LEU F 243 5 4
HELIX 109 109 ASP F 245 GLU F 255 1 11
HELIX 110 110 CYS F 262 GLY F 270 1 9
HELIX 111 111 HIS F 278 ASP F 286 1 9
HELIX 112 112 THR F 303 ASP F 314 1 12
HELIX 113 113 THR F 318 SER F 333 1 16
HELIX 114 114 PRO F 336 ALA F 350 1 15
HELIX 115 115 LEU G 18 ALA G 21 5 4
HELIX 116 116 LYS G 23 GLY G 35 1 13
HELIX 117 117 THR G 42 GLY G 51 1 10
HELIX 118 118 THR G 57 ALA G 63 1 7
HELIX 119 119 LYS G 64 ALA G 73 1 10
HELIX 120 120 CYS G 75 ASP G 93 1 19
HELIX 121 121 PRO G 104 ALA G 108 5 5
HELIX 122 122 THR G 125 GLY G 145 1 21
HELIX 123 123 GLN G 158 TYR G 172 1 15
HELIX 124 124 GLY G 190 LEU G 193 5 4
HELIX 125 125 PHE G 194 GLY G 208 1 15
HELIX 126 126 SER G 220 THR G 230 1 11
HELIX 127 127 TYR G 240 LEU G 243 5 4
HELIX 128 128 ASP G 245 GLU G 255 1 11
HELIX 129 129 CYS G 262 GLY G 270 1 9
HELIX 130 130 HIS G 278 ASP G 286 1 9
HELIX 131 131 THR G 303 ASP G 314 1 12
HELIX 132 132 THR G 318 SER G 333 1 16
HELIX 133 133 PRO G 336 ARG G 352 1 17
HELIX 134 134 ASP H 19 ALA H 21 5 3
HELIX 135 135 LYS H 23 GLY H 35 1 13
HELIX 136 136 THR H 42 GLY H 51 1 10
HELIX 137 137 THR H 57 ALA H 63 1 7
HELIX 138 138 LYS H 64 ALA H 73 1 10
HELIX 139 139 CYS H 75 ASP H 93 1 19
HELIX 140 140 PRO H 104 ALA H 108 5 5
HELIX 141 141 ILE H 115 GLN H 119 5 5
HELIX 142 142 THR H 125 GLY H 145 1 21
HELIX 143 143 GLN H 158 TYR H 172 1 15
HELIX 144 144 GLY H 190 LEU H 193 5 4
HELIX 145 145 PHE H 194 GLY H 208 1 15
HELIX 146 146 SER H 220 THR H 230 1 11
HELIX 147 147 TYR H 240 LEU H 243 5 4
HELIX 148 148 ASP H 245 GLU H 255 1 11
HELIX 149 149 CYS H 262 GLY H 270 1 9
HELIX 150 150 VAL H 280 ASN H 285 1 6
HELIX 151 151 THR H 303 ASP H 314 1 12
HELIX 152 152 THR H 318 SER H 333 1 16
HELIX 153 153 PRO H 336 TYR H 351 1 16
SHEET 1 AA 2 LYS A 41 THR A 42 0
SHEET 2 AA 2 VAL A 507 GLN A 508 1 N GLN A 508 O LYS A 41
SHEET 1 AB 4 LEU A 60 TRP A 62 0
SHEET 2 AB 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AB 4 ASN A 75 ASN A 80 -1 O ASN A 75 N GLN A 72
SHEET 4 AB 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AC 4 ILE A 102 ILE A 107 0
SHEET 2 AC 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AC 4 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 4 AC 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AD 4 TRP A 154 TRP A 157 0
SHEET 2 AD 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 AD 4 ASP A 171 LYS A 175 -1 O ASP A 171 N TRP A 168
SHEET 4 AD 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AE 3 ILE A 194 ASN A 196 0
SHEET 2 AE 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AE 3 LEU A 214 TRP A 216 -1 O TRP A 215 N ALA A 224
SHEET 1 AF 4 ILE A 194 ASN A 196 0
SHEET 2 AF 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AF 4 THR A 265 ASN A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AF 4 ILE A 285 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AG 2 LEU A 235 PHE A 240 0
SHEET 2 AG 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AH 4 HIS A 298 TRP A 305 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AH 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AH 4 HIS A 345 MET A 348 -1 O HIS A 345 N MET A 325
SHEET 1 AI 4 HIS A 298 TRP A 305 0
SHEET 2 AI 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 AI 4 TYR A 322 TYR A 330 -1 O TYR A 322 N ARG A 317
SHEET 4 AI 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 AJ 4 HIS A 363 PHE A 364 0
SHEET 2 AJ 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AJ 4 ARG A 382 GLN A 388 -1 O HIS A 383 N ILE A 375
SHEET 4 AJ 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AK 4 VAL A 404 LEU A 410 0
SHEET 2 AK 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 AK 4 ASN A 430 GLN A 435 -1 O ASN A 430 N SER A 419
SHEET 4 AK 4 ASP A 438 CYS A 444 -1 N ASP A 438 O GLN A 435
SHEET 1 AL 4 TYR A 457 PHE A 461 0
SHEET 2 AL 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 AL 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AL 4 LYS A 489 GLU A 495 -1 O LYS A 489 N SER A 484
SHEET 1 AM 8 SER A 511 LEU A 519 0
SHEET 2 AM 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AM 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AM 8 TYR A 540 VAL A 546 1 O PRO A 541 N ILE A 574
SHEET 5 AM 8 VAL A 619 TRP A 629 1 N ASP A 620 O TYR A 540
SHEET 6 AM 8 CYS A 649 VAL A 653 1 O CYS A 649 N ILE A 626
SHEET 7 AM 8 GLU A 699 GLY A 705 1 O GLU A 699 N GLY A 650
SHEET 8 AM 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 BA 2 LYS B 41 THR B 42 0
SHEET 2 BA 2 VAL B 507 GLN B 508 1 N GLN B 508 O LYS B 41
SHEET 1 BB 4 ARG B 61 TRP B 62 0
SHEET 2 BB 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 BB 4 ASN B 75 ASN B 80 -1 O ASN B 75 N GLN B 72
SHEET 4 BB 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 BC 4 ILE B 102 ILE B 107 0
SHEET 2 BC 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 BC 4 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 4 BC 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 BD 4 TRP B 154 TRP B 157 0
SHEET 2 BD 4 LEU B 164 TRP B 168 -1 O ALA B 165 N THR B 156
SHEET 3 BD 4 ASP B 171 LYS B 175 -1 O ASP B 171 N TRP B 168
SHEET 4 BD 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 BE 3 ILE B 194 ASN B 196 0
SHEET 2 BE 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BE 3 LEU B 214 TRP B 216 -1 O TRP B 215 N ALA B 224
SHEET 1 BF 4 ILE B 194 ASN B 196 0
SHEET 2 BF 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 BF 4 THR B 265 ASN B 272 -1 O THR B 265 N ASN B 229
SHEET 4 BF 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 BG 2 LEU B 235 PHE B 240 0
SHEET 2 BG 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 BH 7 HIS B 298 TRP B 305 0
SHEET 2 BH 7 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 BH 7 TYR B 322 TYR B 330 -1 O TYR B 322 N ARG B 317
SHEET 4 BH 7 TRP B 337 ASN B 338 -1 O ASN B 338 N ASP B 329
SHEET 5 BH 7 TYR B 322 TYR B 330 -1 O ASP B 329 N ASN B 338
SHEET 6 BH 7 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 7 BH 7 TYR B 322 TYR B 330 -1 O SER B 323 N GLU B 347
SHEET 1 BI 4 HIS B 363 PHE B 364 0
SHEET 2 BI 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 BI 4 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 4 BI 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 BJ 4 VAL B 404 LEU B 410 0
SHEET 2 BJ 4 TYR B 414 SER B 419 -1 O TYR B 416 N GLU B 408
SHEET 3 BJ 4 ASN B 430 GLN B 435 -1 O ASN B 430 N SER B 419
SHEET 4 BJ 4 ASP B 438 CYS B 444 -1 N ASP B 438 O GLN B 435
SHEET 1 BK 4 TYR B 457 PHE B 461 0
SHEET 2 BK 4 TYR B 467 CYS B 472 -1 O GLN B 469 N SER B 460
SHEET 3 BK 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 BK 4 LYS B 489 GLU B 495 -1 O LYS B 489 N SER B 484
SHEET 1 BL 8 SER B 511 LEU B 519 0
SHEET 2 BL 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 BL 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 BL 8 TYR B 540 ASP B 545 1 O PRO B 541 N ILE B 574
SHEET 5 BL 8 VAL B 619 TRP B 629 1 N ASP B 620 O TYR B 540
SHEET 6 BL 8 CYS B 649 VAL B 653 1 O CYS B 649 N ILE B 626
SHEET 7 BL 8 GLU B 699 GLY B 705 1 O GLU B 699 N GLY B 650
SHEET 8 BL 8 GLN B 731 TYR B 735 1 O GLN B 731 N LEU B 702
SHEET 1 CA 2 LYS C 41 THR C 42 0
SHEET 2 CA 2 VAL C 507 GLN C 508 1 N GLN C 508 O LYS C 41
SHEET 1 CB 4 ARG C 61 TRP C 62 0
SHEET 2 CB 4 GLU C 67 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 CB 4 ILE C 76 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 4 CB 4 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 CC 4 ILE C 102 ILE C 107 0
SHEET 2 CC 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 CC 4 TYR C 128 ASP C 136 -1 O THR C 129 N VAL C 121
SHEET 4 CC 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 CD 4 TRP C 154 TRP C 157 0
SHEET 2 CD 4 LEU C 164 TRP C 168 -1 O ALA C 165 N THR C 156
SHEET 3 CD 4 ASP C 171 LYS C 175 -1 O ASP C 171 N TRP C 168
SHEET 4 CD 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 CE 7 ILE C 194 ASN C 196 0
SHEET 2 CE 7 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 CE 7 LEU C 214 TRP C 216 -1 O TRP C 215 N ALA C 224
SHEET 4 CE 7 PHE C 222 ASN C 229 -1 O ALA C 224 N TRP C 215
SHEET 5 CE 7 SER C 284 GLN C 286
SHEET 6 CE 7 THR C 265 ASN C 272 -1 O VAL C 270 N ILE C 285
SHEET 7 CE 7 PHE C 222 ASN C 229 -1 O LEU C 223 N VAL C 271
SHEET 1 CF 2 LEU C 235 PHE C 240 0
SHEET 2 CF 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 CG 7 HIS C 298 TRP C 305 0
SHEET 2 CG 7 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 CG 7 TYR C 322 TYR C 330 -1 O TYR C 322 N ARG C 317
SHEET 4 CG 7 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 5 CG 7 TYR C 322 TYR C 330 -1 O ASP C 329 N ASN C 338
SHEET 6 CG 7 HIS C 345 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 7 CG 7 TYR C 322 TYR C 330 -1 O SER C 323 N GLU C 347
SHEET 1 CH 4 HIS C 363 PHE C 364 0
SHEET 2 CH 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 CH 4 ARG C 382 GLN C 388 -1 O HIS C 383 N ILE C 375
SHEET 4 CH 4 CYS C 394 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 CI 4 VAL C 404 LEU C 410 0
SHEET 2 CI 4 TYR C 414 SER C 419 -1 O TYR C 416 N GLU C 408
SHEET 3 CI 4 ASN C 430 GLN C 435 -1 O ASN C 430 N SER C 419
SHEET 4 CI 4 ASP C 438 CYS C 444 -1 N ASP C 438 O GLN C 435
SHEET 1 CJ 4 TYR C 457 PHE C 461 0
SHEET 2 CJ 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 CJ 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 CJ 4 LYS C 489 GLU C 495 -1 O LYS C 489 N SER C 484
SHEET 1 CK 8 SER C 511 LEU C 519 0
SHEET 2 CK 8 THR C 522 LEU C 530 -1 O THR C 522 N LEU C 519
SHEET 3 CK 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 CK 8 TYR C 540 VAL C 546 1 O PRO C 541 N ILE C 574
SHEET 5 CK 8 VAL C 619 TRP C 629 1 N ASP C 620 O TYR C 540
SHEET 6 CK 8 CYS C 649 VAL C 653 1 O CYS C 649 N ILE C 626
SHEET 7 CK 8 GLU C 699 GLY C 705 1 O GLU C 699 N GLY C 650
SHEET 8 CK 8 GLN C 731 TYR C 735 1 O GLN C 731 N LEU C 702
SHEET 1 DA 4 ARG D 61 TRP D 62 0
SHEET 2 DA 4 GLU D 67 GLN D 72 -1 O LEU D 69 N ARG D 61
SHEET 3 DA 4 ASN D 75 ASN D 80 -1 O ASN D 75 N GLN D 72
SHEET 4 DA 4 SER D 86 LEU D 90 -1 O SER D 87 N VAL D 78
SHEET 1 DB 4 ILE D 102 ILE D 107 0
SHEET 2 DB 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 DB 4 TYR D 128 ASP D 136 -1 O THR D 129 N VAL D 121
SHEET 4 DB 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 DC 4 TRP D 154 TRP D 157 0
SHEET 2 DC 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 DC 4 ASP D 171 LYS D 175 -1 O ASP D 171 N TRP D 168
SHEET 4 DC 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 DD 7 ILE D 194 ASN D 196 0
SHEET 2 DD 7 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 DD 7 LEU D 214 TRP D 216 -1 O TRP D 215 N ALA D 224
SHEET 4 DD 7 PHE D 222 ASN D 229 -1 O ALA D 224 N TRP D 215
SHEET 5 DD 7 ILE D 285 GLN D 286
SHEET 6 DD 7 THR D 265 ASN D 272 -1 O VAL D 270 N ILE D 285
SHEET 7 DD 7 PHE D 222 ASN D 229 -1 O LEU D 223 N VAL D 271
SHEET 1 DE 2 LEU D 235 PHE D 240 0
SHEET 2 DE 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 DF 7 HIS D 298 TRP D 305 0
SHEET 2 DF 7 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 DF 7 TYR D 322 TYR D 330 -1 O TYR D 322 N ARG D 317
SHEET 4 DF 7 TRP D 337 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 5 DF 7 TYR D 322 TYR D 330 -1 O ASP D 329 N ASN D 338
SHEET 6 DF 7 GLU D 347 MET D 348 -1 O GLU D 347 N SER D 323
SHEET 7 DF 7 TYR D 322 TYR D 330 -1 O SER D 323 N GLU D 347
SHEET 1 DG 4 HIS D 363 PHE D 364 0
SHEET 2 DG 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 DG 4 ARG D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 DG 4 THR D 395 PHE D 396 -1 O THR D 395 N TYR D 386
SHEET 1 DH 4 VAL D 404 LEU D 410 0
SHEET 2 DH 4 TYR D 414 SER D 419 -1 O TYR D 416 N GLU D 408
SHEET 3 DH 4 ASN D 430 GLN D 435 -1 O ASN D 430 N SER D 419
SHEET 4 DH 4 ASP D 438 CYS D 444 -1 N ASP D 438 O GLN D 435
SHEET 1 DI 4 TYR D 457 PHE D 461 0
SHEET 2 DI 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 DI 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 DI 4 LYS D 489 GLU D 495 -1 O LYS D 489 N SER D 484
SHEET 1 DJ 8 SER D 511 LEU D 519 0
SHEET 2 DJ 8 THR D 522 LEU D 530 -1 O THR D 522 N LEU D 519
SHEET 3 DJ 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 DJ 8 TYR D 540 VAL D 546 1 O PRO D 541 N ILE D 574
SHEET 5 DJ 8 VAL D 619 TRP D 629 1 N ASP D 620 O TYR D 540
SHEET 6 DJ 8 CYS D 649 VAL D 653 1 O CYS D 649 N ILE D 626
SHEET 7 DJ 8 GLU D 699 GLY D 705 1 O GLU D 699 N GLY D 650
SHEET 8 DJ 8 GLN D 731 TYR D 735 1 O GLN D 731 N LEU D 702
SHEET 1 EA 8 LYS E 11 HIS E 17 0
SHEET 2 EA 8 VAL E 95 TYR E 102 1 N VAL E 96 O LYS E 11
SHEET 3 EA 8 LYS E 147 MET E 155 1 O LYS E 147 N VAL E 98
SHEET 4 EA 8 VAL E 177 ALA E 183 1 N VAL E 178 O SER E 150
SHEET 5 EA 8 HIS E 210 ALA E 215 1 O HIS E 210 N ILE E 180
SHEET 6 EA 8 ARG E 235 HIS E 238 1 O ARG E 235 N VAL E 213
SHEET 7 EA 8 HIS E 258 ILE E 261 1 O HIS E 258 N LEU E 236
SHEET 8 EA 8 TYR E 290 LEU E 292 1 O SER E 291 N ILE E 261
SHEET 1 FA 8 LYS F 11 HIS F 17 0
SHEET 2 FA 8 VAL F 95 TYR F 102 1 N VAL F 96 O LYS F 11
SHEET 3 FA 8 LYS F 147 MET F 155 1 O LYS F 147 N VAL F 98
SHEET 4 FA 8 VAL F 177 ALA F 183 1 N VAL F 178 O SER F 150
SHEET 5 FA 8 HIS F 210 ALA F 215 1 O HIS F 210 N ILE F 180
SHEET 6 FA 8 ARG F 235 HIS F 238 1 O ARG F 235 N VAL F 213
SHEET 7 FA 8 HIS F 258 ILE F 261 1 O HIS F 258 N LEU F 236
SHEET 8 FA 8 TYR F 290 LEU F 292 1 O SER F 291 N ILE F 261
SHEET 1 GA 8 LYS G 11 GLU G 13 0
SHEET 2 GA 8 VAL G 95 TYR G 102 1 N VAL G 96 O LYS G 11
SHEET 3 GA 8 LYS G 147 MET G 155 1 O LYS G 147 N VAL G 98
SHEET 4 GA 8 VAL G 177 ALA G 183 1 N VAL G 178 O SER G 150
SHEET 5 GA 8 HIS G 210 ALA G 215 1 O HIS G 210 N ILE G 180
SHEET 6 GA 8 ARG G 235 HIS G 238 1 O ARG G 235 N VAL G 213
SHEET 7 GA 8 HIS G 258 ILE G 261 1 O HIS G 258 N LEU G 236
SHEET 8 GA 8 TYR G 290 LEU G 292 1 O SER G 291 N ILE G 261
SHEET 1 HA 8 LYS H 11 HIS H 17 0
SHEET 2 HA 8 VAL H 95 TYR H 102 1 N VAL H 96 O LYS H 11
SHEET 3 HA 8 LYS H 147 MET H 155 1 O LYS H 147 N VAL H 98
SHEET 4 HA 8 VAL H 177 ALA H 183 1 N VAL H 178 O SER H 150
SHEET 5 HA 8 HIS H 210 ALA H 215 1 O HIS H 210 N ILE H 180
SHEET 6 HA 8 ARG H 235 HIS H 238 1 O ARG H 235 N VAL H 213
SHEET 7 HA 8 HIS H 258 ILE H 261 1 O HIS H 258 N LEU H 236
SHEET 8 HA 8 ASN H 289 LEU H 292 1 O ASN H 289 N PHE H 259
SSBOND 1 CYS A 328 CYS A 339 1555 1555
SSBOND 2 CYS A 385 CYS A 394 1555 1555
SSBOND 3 CYS A 444 CYS A 447 1555 1555
SSBOND 4 CYS A 454 CYS A 472 1555 1555
SSBOND 5 CYS A 649 CYS A 762 1555 1555
SSBOND 6 CYS B 328 CYS B 339 1555 1555
SSBOND 7 CYS B 385 CYS B 394 1555 1555
SSBOND 8 CYS B 444 CYS B 447 1555 1555
SSBOND 9 CYS B 454 CYS B 472 1555 1555
SSBOND 10 CYS B 649 CYS B 762 1555 1555
SSBOND 11 CYS C 328 CYS C 339 1555 1555
SSBOND 12 CYS C 385 CYS C 394 1555 1555
SSBOND 13 CYS C 444 CYS C 447 1555 1555
SSBOND 14 CYS C 454 CYS C 472 1555 1555
SSBOND 15 CYS C 649 CYS C 762 1555 1555
SSBOND 16 CYS D 328 CYS D 339 1555 1555
SSBOND 17 CYS D 385 CYS D 394 1555 1555
SSBOND 18 CYS D 444 CYS D 447 1555 1555
SSBOND 19 CYS D 454 CYS D 472 1555 1555
SSBOND 20 CYS D 649 CYS D 762 1555 1555
LINK ND2 ASN A 85 C1 NAG A 800 1555 1555
LINK ND2 ASN A 92 C1 NDG A 870 1555 1555
LINK ND2 ASN A 150 C1 NAG A 810 1555 1555
LINK ND2 ASN A 219 C1 NAG A 820 1555 1555
LINK ND2 ASN A 229 C1 NAG A 830 1555 1555
LINK ND2 ASN A 281 C1 NAG A 840 1555 1555
LINK ND2 ASN A 321 C1 NAG A 850 1555 1555
LINK ND2 ASN A 520 C1 NDG A 860 1555 1555
LINK O6 NAG A 800 C1 AFL A 802 1555 1555
LINK O4 NAG A 800 C1 NAG A 801 1555 1555
LINK O4 NAG A 810 C1 NAG A 811 1555 1555
LINK O4 NAG A 820 C1 NAG A 821 1555 1555
LINK O4 NAG A 830 C1 NAG A 831 1555 1555
LINK O4 NAG A 831 C1 BMA A 832 1555 1555
LINK O3 BMA A 832 C1 MAN A 833 1555 1555
LINK ND2 ASN B 85 C1 NAG B 800 1555 1555
LINK ND2 ASN B 92 C1 NAG B 870 1555 1555
LINK ND2 ASN B 150 C1 NAG B 810 1555 1555
LINK ND2 ASN B 219 C1 NAG B 820 1555 1555
LINK ND2 ASN B 229 C1 NAG B 830 1555 1555
LINK ND2 ASN B 281 C1 NAG B 840 1555 1555
LINK ND2 ASN B 321 C1 NAG B 850 1555 1555
LINK ND2 ASN B 520 C1 NDG B 860 1555 1555
LINK O6 NAG B 800 C1 AFL B 802 1555 1555
LINK O4 NAG B 820 C1 NAG B 821 1555 1555
LINK O4 NAG B 830 C1 NAG B 831 1555 1555
LINK O4 NAG B 831 C1 BMA B 832 1555 1555
LINK O3 BMA B 832 C1 MAN B 833 1555 1555
LINK O4 NAG B 850 C1 NAG B 851 1555 1555
LINK ND2 ASN C 85 C1 NAG C 800 1555 1555
LINK ND2 ASN C 92 C1 NAG C 870 1555 1555
LINK ND2 ASN C 150 C1 NAG C 810 1555 1555
LINK ND2 ASN C 219 C1 NAG C 820 1555 1555
LINK ND2 ASN C 229 C1 NAG C 830 1555 1555
LINK ND2 ASN C 281 C1 NAG C 840 1555 1555
LINK ND2 ASN C 321 C1 NAG C 850 1555 1555
LINK ND2 ASN C 520 C1 NAG C 860 1555 1555
LINK O4 NAG C 800 C1 NAG C 801 1555 1555
LINK O6 NAG C 800 C1 AFL C 802 1555 1555
LINK O4 NAG C 810 C1 NAG C 811 1555 1555
LINK O4 NAG C 820 C1 NAG C 821 1555 1555
LINK O4 NAG C 830 C1 NAG C 831 1555 1555
LINK O4 NAG C 831 C1 BMA C 832 1555 1555
LINK O3 BMA C 832 C1 MAN C 833 1555 1555
LINK O4 NAG C 850 C1 NAG C 851 1555 1555
LINK ND2 ASN D 85 C1 NAG D 800 1555 1555
LINK ND2 ASN D 92 C1 NAG D 870 1555 1555
LINK ND2 ASN D 150 C1 NAG D 810 1555 1555
LINK ND2 ASN D 219 C1 NAG D 820 1555 1555
LINK ND2 ASN D 229 C1 NAG D 830 1555 1555
LINK ND2 ASN D 281 C1 NAG D 840 1555 1555
LINK ND2 ASN D 321 C1 NAG D 850 1555 1555
LINK ND2 ASN D 520 C1 NAG D 860 1555 1555
LINK O6 NAG D 800 C1 AFL D 802 1555 1555
LINK O4 NAG D 820 C1 NAG D 821 1555 1555
LINK O4 NAG D 830 C1 NAG D 831 1555 1555
LINK O4 NAG D 831 C1 BMA D 832 1555 1555
LINK O3 BMA D 832 C1 MAN D 833 1555 1555
LINK O4 NAG D 850 C1 NAG D 851 1555 1555
LINK ZN ZN E 501 NE2 HIS E 214 1555 1555
LINK ZN ZN E 501 NE2 HIS E 17 1555 1555
LINK ZN ZN E 501 NE2 HIS E 15 1555 1555
LINK ZN ZN E 501 OD1 ASP E 295 1555 1555
LINK ZN ZN F 501 NE2 HIS F 15 1555 1555
LINK ZN ZN F 501 NE2 HIS F 214 1555 1555
LINK ZN ZN F 501 OD1 ASP F 295 1555 1555
LINK ZN ZN F 501 NE2 HIS F 17 1555 1555
LINK ZN ZN G 501 NE2 HIS G 15 1555 1555
LINK ZN ZN G 501 OD1 ASP G 295 1555 1555
LINK ZN ZN G 501 NE2 HIS G 17 1555 1555
LINK ZN ZN G 501 NE2 HIS G 214 1555 1555
LINK ZN ZN H 501 OD1 ASP H 295 1555 1555
LINK ZN ZN H 501 NE2 HIS H 214 1555 1555
LINK ZN ZN H 501 NE2 HIS H 17 1555 1555
LINK ZN ZN H 501 NE2 HIS H 15 1555 1555
CISPEP 1 GLY A 474 PRO A 475 0 -0.04
CISPEP 2 GLY B 474 PRO B 475 0 0.13
CISPEP 3 GLY C 474 PRO C 475 0 -0.87
CISPEP 4 GLY D 474 PRO D 475 0 0.40
CISPEP 5 GLU E 121 GLY E 122 0 4.78
CISPEP 6 GLU F 121 GLY F 122 0 4.97
CISPEP 7 GLU G 121 GLY G 122 0 6.05
CISPEP 8 GLU H 121 GLY H 122 0 5.80
SITE 1 AC1 3 ASN A 85 SER A 86 SER A 87
SITE 1 AC4 2 ARG A 147 ASN A 150
SITE 1 AC5 1 ARG A 147
SITE 1 AC6 3 ASN A 219 THR A 221 GLU A 309
SITE 1 AC7 2 TYR A 330 GLU A 332
SITE 1 AC8 4 ILE A 194 ASN A 229 THR A 231 GLU A 232
SITE 1 AC9 3 ARG F 33 ARG F 34 GLY F 35
SITE 1 BC1 2 ARG F 34 GLY F 35
SITE 1 BC2 2 GLY F 35 ILE F 36
SITE 1 BC3 2 TRP A 187 ASN A 281
SITE 1 BC4 4 ILE A 319 ASN A 321 SER A 349 ARG A 596
SITE 1 BC6 2 ASN A 520 ARG A 581
SITE 1 BC7 3 GLU A 73 ASN A 75 ASN A 92
SITE 1 BC8 2 ASN B 85 SER B 87
SITE 1 BC9 3 TYR B 83 SER C 412 ASP C 413
SITE 1 CC1 2 ILE B 148 ASN B 150
SITE 1 CC2 4 ASN B 219 THR B 221 GLN B 308 GLU B 309
SITE 1 CC3 2 THR B 221 GLU B 332
SITE 1 CC4 4 ASN B 229 THR B 231 GLU B 232 ARG E 33
SITE 1 CC5 4 THR B 231 ARG E 33 ARG E 34 GLY E 35
SITE 1 CC6 1 GLY E 35
SITE 1 CC7 2 GLY E 35 ILE E 36
SITE 1 CC8 3 ASN A 450 TRP B 187 ASN B 281
SITE 1 CC9 1 ASN B 321
SITE 1 DC2 2 ASN B 520 ARG B 581
SITE 1 DC3 5 GLU B 73 ASN B 74 ASN B 75 ASN B 92
SITE 2 DC3 5 ARG F 352
SITE 1 DC4 4 GLU C 67 ASN C 85 SER C 86 SER C 87
SITE 1 DC6 1 TYR C 83
SITE 1 DC7 3 ARG C 147 ILE C 148 ASN C 150
SITE 1 DC8 1 ARG C 147
SITE 1 DC9 4 ASN C 219 THR C 221 GLN C 308 GLU C 309
SITE 1 FC1 2 GLU C 309 GLU C 332
SITE 1 FC2 5 ILE C 194 ASN C 229 THR C 231 GLU C 232
SITE 2 FC2 5 ARG G 33
SITE 1 FC3 3 ARG G 33 ARG G 34 GLY G 35
SITE 1 FC4 1 GLY G 35
SITE 1 FC5 1 ILE G 36
SITE 1 FC7 1 ASN C 321
SITE 1 FC9 2 ASN C 520 ARG C 581
SITE 1 GC1 3 GLU C 73 ASN C 75 ASN C 92
SITE 1 GC2 3 ASN D 85 SER D 86 SER D 87
SITE 1 GC3 1 GLU B 521
SITE 1 GC4 2 ARG D 147 ASN D 150
SITE 1 GC5 4 ASN D 219 THR D 221 GLN D 308 GLU D 309
SITE 1 GC6 2 GLU D 309 TYR D 330
SITE 1 GC7 3 ASN D 229 THR D 231 GLU D 232
SITE 1 GC8 3 ARG H 33 ARG H 34 GLY H 35
SITE 1 GC9 1 GLY H 35
SITE 1 HC2 3 ASN C 450 TRP D 187 ASN D 281
SITE 1 HC3 3 ASN D 321 SER D 349 ARG D 596
SITE 1 HC4 1 GLU D 677
SITE 1 HC5 2 ASN D 520 ARG D 581
SITE 1 HC6 3 GLU D 73 ASN D 75 ASN D 92
SITE 1 HC7 4 HIS E 15 HIS E 17 HIS E 214 ASP E 295
SITE 1 HC8 4 HIS F 15 HIS F 17 HIS F 214 ASP F 295
SITE 1 HC9 4 HIS G 15 HIS G 17 HIS G 214 ASP G 295
SITE 1 IC1 5 HIS H 15 HIS H 17 HIS H 214 HIS H 238
SITE 2 IC1 5 ASP H 295
CRYST1 158.065 168.504 236.842 90.00 100.54 90.00 C 1 2 1 16
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 0.006327 0.000000 0.001177 0.00000
SCALE2 0.000000 0.005935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004295 0.00000
TER 5964 PRO A 766
TER 11928 PRO B 766
TER 17892 PRO C 766
TER 23856 PRO D 766
TER 26666 SER E 355
TER 29475 SER F 355
TER 32285 SER G 355
TER 35095 SER H 355
MASTER 660 0 63 153 231 0 59 635877 8 879 336
END |