HEADER HYDROLASE 03-JAN-05 2BGN
TITLE HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE TRP2-TAT(1-9) BOUND
TITLE 2 TO THE ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
CAVEAT 2BGN TYR F 351 HAS WRONG CHIRALITY AT ATOM CA NAG A 840 HAS WRONG
CAVEAT 2 2BGN CHIRALITY AT ATOM C5 NAG B 860 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 2BGN C1 NAG D 860 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 39-766;
COMPND 5 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103, ADENOSINE
COMPND 6 DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ADENOSINE DEAMINASE;
COMPND 11 CHAIN: E, F, G, H;
COMPND 12 SYNONYM: ADENOSINE AMINOHYDROLASE;
COMPND 13 EC: 3.5.4.4;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: TAT PROTEIN;
COMPND 16 CHAIN: W, X, Y, Z;
COMPND 17 FRAGMENT: HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE, RESIDUES
COMPND 18 1-9;
COMPND 19 SYNONYM: TRANSACTIVATING REGULATORY PROTEIN;
COMPND 20 ENGINEERED: YES;
COMPND 21 MUTATION: YES;
COMPND 22 OTHER_DETAILS: ASP2TRP VARIANT OF HIV-1 TAT PROTEIN DERIVED N-
COMPND 23 TERMINAL NONAPEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: KIDNEY;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9 CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: BOVINE;
SOURCE 14 ORGANISM_TAXID: 9913;
SOURCE 15 ORGAN: INTESTINAL MUCOSA;
SOURCE 16 OTHER_DETAILS: SIGMA, TYPE VI, FROM CALF INTESTINAL MUCOSA;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 20 ORGANISM_TAXID: 11676
KEYWDS HYDROLASE, HYDROLASE-COMPLEX, DIPETIDYL PEPTIDASE IV, DPPIV, CD26,
KEYWDS 2 ALPHA/BETA-HYDROLASE FOLD, BETA-PROPELLER FOLD, PROTEIN-PROTEIN
KEYWDS 3 COMPLEX, ADENOSINE DEAMINASE, ADA, SERINE PROTEASE, AMINOPEPTIDASE,
KEYWDS 4 HIV-1 TAT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
REVDAT 5 13-DEC-23 2BGN 1 HETSYN
REVDAT 4 29-JUL-20 2BGN 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 24-FEB-09 2BGN 1 VERSN
REVDAT 2 14-APR-05 2BGN 1 JRNL
REVDAT 1 27-JAN-05 2BGN 0
JRNL AUTH W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN
JRNL TITL CRYSTAL STRUCTURES OF HIV-1 TAT-DERIVED NONAPEPTIDES
JRNL TITL 2 TAT-(1-9) AND TRP2-TAT-(1-9) BOUND TO THE ACTIVE SITE OF
JRNL TITL 3 DIPEPTIDYL-PEPTIDASE IV (CD26)
JRNL REF J.BIOL.CHEM. V. 280 14911 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15695814
JRNL DOI 10.1074/JBC.M413400200
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 94691
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1925
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) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6358
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 35292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 804
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) : 64.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.38000
REMARK 3 B22 (A**2) : -1.90000
REMARK 3 B33 (A**2) : -2.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.40000
REMARK 3 B23 (A**2) : 0.00000
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): 0.502
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.346
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.415
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 41545 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 32136 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 63863 ; 1.518 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): 78891 ; 0.948 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 8652 ; 6.176 ; 7.500
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1780 ;35.566 ;24.112
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6022 ;20.616 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 184 ;18.105 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5544 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 70962 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11766 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7198 ; 0.216 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 31675 ; 0.209 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 20330 ; 0.096 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1179 ; 0.181 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 13 ; 0.178 ; 0.500
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): 24 ; 0.302 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 107 ; 0.251 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.403 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 22111 ; 0.556 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8756 ; 0.327 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 35120 ; 1.013 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 17274 ; 1.102 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15399 ; 1.898 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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): 10693 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 10693 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 10693 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 10693 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 10693 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 10693 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 10693 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 10693 ; 0.02 ; 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 : 10
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 277 1
REMARK 3 7 F 241 F 277 1
REMARK 3 7 G 241 G 277 1
REMARK 3 7 H 241 H 277 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 293 1
REMARK 3 9 F 284 F 293 1
REMARK 3 9 G 284 G 293 1
REMARK 3 9 H 284 H 293 1
REMARK 3 10 E 297 E 335 4
REMARK 3 10 F 297 F 335 4
REMARK 3 10 G 297 G 335 4
REMARK 3 10 H 297 H 335 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 E (A): 3859 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 3859 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 G (A): 3859 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 H (A): 3859 ; 0.01 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 E (A): 610 ; 0.23 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 F (A): 610 ; 0.26 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 G (A): 610 ; 0.26 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 H (A): 610 ; 0.23 ; 0.50
REMARK 3 TIGHT THERMAL 2 E (A**2): 3859 ; 0.03 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 3859 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 2 G (A**2): 3859 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 2 H (A**2): 3859 ; 0.02 ; 0.50
REMARK 3 MEDIUM THERMAL 2 E (A**2): 610 ; 0.27 ; 2.00
REMARK 3 MEDIUM THERMAL 2 F (A**2): 610 ; 0.12 ; 2.00
REMARK 3 MEDIUM THERMAL 2 G (A**2): 610 ; 0.12 ; 2.00
REMARK 3 MEDIUM THERMAL 2 H (A**2): 610 ; 0.13 ; 2.00
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2BGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1290022253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97782
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1W1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 79.47250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.13650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.47250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 85.13650
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 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 300 REMARK: THE COMPLEX DESCRIBED BY REMARK 350 BELOW
REMARK 300 IS OF THETYPE A2B2, WHERE CHAINS A AND B ARE
REMARK 300 IN CONTACT WITHEACH OTHER, AND EACH OF THESE
REMARK 300 CHAINS IS IN TURN INCOMPLEX WITH CHAINS F AND
REMARK 300 E RESPECTIVELY.
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, W, X, I, J, K, L,
REMARK 350 AND CHAINS: M, N, O, P, Q
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H, Y, Z, R, S, T, U,
REMARK 350 AND CHAINS: V, a, b, c, d
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION ASP 2 TRP, CHAINS W, X, Y AND Z
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 SER E 358
REMARK 465 ALA E 359
REMARK 465 GLU E 360
REMARK 465 GLN E 361
REMARK 465 CYS E 362
REMARK 465 LEU E 363
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 SER F 358
REMARK 465 ALA F 359
REMARK 465 GLU F 360
REMARK 465 GLN F 361
REMARK 465 CYS F 362
REMARK 465 LEU F 363
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 SER G 358
REMARK 465 ALA G 359
REMARK 465 GLU G 360
REMARK 465 GLN G 361
REMARK 465 CYS G 362
REMARK 465 LEU G 363
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 465 SER H 358
REMARK 465 ALA H 359
REMARK 465 GLU H 360
REMARK 465 GLN H 361
REMARK 465 CYS H 362
REMARK 465 LEU H 363
REMARK 465 ASN W 7
REMARK 465 ILE W 8
REMARK 465 GLU W 9
REMARK 465 ASN X 7
REMARK 465 ILE X 8
REMARK 465 GLU X 9
REMARK 465 ASN Y 7
REMARK 465 ILE Y 8
REMARK 465 GLU Y 9
REMARK 465 ASN Z 7
REMARK 465 ILE Z 8
REMARK 465 GLU Z 9
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 O4 NAG V 1 O5 NAG V 2 1.99
REMARK 500 O4 NAG d 1 O5 NAG d 2 2.04
REMARK 500 ND2 ASN A 321 O5 NAG M 1 2.08
REMARK 500 ND2 ASN D 321 C2 NAG d 1 2.08
REMARK 500 O4 NAG M 1 O5 NAG M 2 2.13
REMARK 500 O6 NAG a 1 C2 FUL a 2 2.14
REMARK 500 ND2 ASN B 92 C2 NAG B 870 2.14
REMARK 500 CG ASN B 520 C1 NAG B 860 2.16
REMARK 500 ND2 ASN A 150 C2 NAG J 1 2.18
REMARK 500 OH TYR A 248 O TYR B 256 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 423 OE2 GLU E 121 4546 1.77
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 ALA F 350 C TYR F 351 N 0.187
REMARK 500 TYR F 351 N TYR F 351 CA -0.430
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 496 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 535 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 588 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 620 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 678 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 PRO B 290 C - N - CD ANGL. DEV. = -19.5 DEGREES
REMARK 500 ARG B 318 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 496 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 535 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP B 620 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 678 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP C 297 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP C 496 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 535 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP C 620 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 678 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP D 496 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP D 535 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP D 620 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 678 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP E 8 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP E 19 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP E 60 CB - CG - OD2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP E 77 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP E 127 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 143 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP E 181 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP E 185 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 245 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 295 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP E 296 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP E 305 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP E 307 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP E 314 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP F 8 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP F 19 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP F 60 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP F 77 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP F 127 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP F 143 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP F 181 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP F 245 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP F 296 CB - CG - OD2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP F 307 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU F 325 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ALA F 350 CA - C - N ANGL. DEV. = 38.8 DEGREES
REMARK 500 ALA F 350 O - C - N ANGL. DEV. = -40.8 DEGREES
REMARK 500 TYR F 351 C - N - CA ANGL. DEV. = 28.0 DEGREES
REMARK 500 TYR F 351 N - CA - CB ANGL. DEV. = 30.3 DEGREES
REMARK 500 PRO G 5 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 69 ANGLE DEVIATIONS.
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 ARG A 40 -129.30 -93.77
REMARK 500 GLU A 73 45.81 33.65
REMARK 500 ASN A 74 21.58 82.41
REMARK 500 GLU A 97 70.23 -101.01
REMARK 500 SER A 106 116.27 -177.32
REMARK 500 GLN A 123 -101.57 -112.40
REMARK 500 TRP A 124 -155.77 -95.97
REMARK 500 LYS A 139 34.20 -81.71
REMARK 500 ARG A 140 54.19 22.22
REMARK 500 ILE A 193 -59.13 -132.25
REMARK 500 ASP A 200 -165.39 -78.42
REMARK 500 SER A 242 -163.59 67.68
REMARK 500 ALA A 261 -168.56 -79.28
REMARK 500 PRO A 264 177.94 -59.40
REMARK 500 SER A 275 37.87 -95.30
REMARK 500 ILE A 295 1.97 -58.31
REMARK 500 GLN A 320 35.11 -80.72
REMARK 500 ASP A 413 21.41 -144.34
REMARK 500 LYS A 423 22.85 47.76
REMARK 500 ASN A 450 67.56 179.79
REMARK 500 LEU A 491 -79.73 -81.49
REMARK 500 ASN A 497 28.26 48.84
REMARK 500 LYS A 536 13.21 -69.47
REMARK 500 TYR A 547 -68.68 -123.83
REMARK 500 ARG A 597 41.07 -155.70
REMARK 500 THR A 600 -76.18 -123.39
REMARK 500 ASP A 620 96.14 -67.87
REMARK 500 SER A 630 -123.46 64.21
REMARK 500 ASP A 678 -113.64 -115.79
REMARK 500 ASN A 710 -71.52 -97.51
REMARK 500 GLN A 714 -48.23 -29.47
REMARK 500 MET A 733 113.85 -162.61
REMARK 500 ASP A 739 -155.91 -109.04
REMARK 500 ILE A 742 48.57 35.07
REMARK 500 ARG B 40 -129.30 -91.30
REMARK 500 GLU B 97 70.43 -100.89
REMARK 500 SER B 106 116.89 -177.16
REMARK 500 GLN B 123 -102.08 -111.69
REMARK 500 TRP B 124 -155.18 -96.07
REMARK 500 LYS B 139 34.75 -82.52
REMARK 500 ARG B 140 54.78 21.87
REMARK 500 ILE B 193 -60.41 -131.77
REMARK 500 ASP B 200 -165.62 -78.41
REMARK 500 SER B 242 -164.78 69.03
REMARK 500 PRO B 264 177.27 -58.36
REMARK 500 SER B 275 36.96 -94.68
REMARK 500 THR B 288 -164.26 -56.67
REMARK 500 GLN B 320 32.57 -79.48
REMARK 500 ASP B 413 20.42 -143.92
REMARK 500 LYS B 423 23.11 47.21
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 E 113 PRO E 114 146.21
REMARK 500 GLU H 113 PRO H 114 143.57
REMARK 500 ASP X 5 PRO X 6 145.74
REMARK 500 PRO Y 3 VAL Y 4 143.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA F 350 -11.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 15 NE2
REMARK 620 2 HIS E 17 NE2 115.9
REMARK 620 3 HIS E 214 NE2 97.4 99.8
REMARK 620 4 ASP E 295 OD1 68.0 99.8 159.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 15 NE2
REMARK 620 2 HIS F 17 NE2 111.5
REMARK 620 3 HIS F 214 NE2 93.9 93.6
REMARK 620 4 ASP F 295 OD1 80.8 106.3 160.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 15 NE2
REMARK 620 2 HIS G 17 NE2 115.3
REMARK 620 3 HIS G 214 NE2 93.4 94.2
REMARK 620 4 ASP G 295 OD1 99.9 88.7 163.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 15 NE2
REMARK 620 2 HIS H 17 NE2 116.4
REMARK 620 3 HIS H 214 NE2 96.2 95.7
REMARK 620 4 ASP H 295 OD1 68.8 112.2 151.9
REMARK 620 N 1 2 3
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J2E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV
REMARK 900 RELATED ID: 1N1M RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH ANINHIBITOR
REMARK 900 RELATED ID: 1NU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP-IV)
REMARK 900 RELATED ID: 1NU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP-IV)IN
REMARK 900 COMPLEX WITH DIPROTIN A (ILI)
REMARK 900 RELATED ID: 1PFQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV /CD26
REMARK 900 RELATED ID: 1R9M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV AT 2.1ANG.
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1RWQ RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH 5-AMINOMETHYL-6-(2,4-
REMARK 900 DICHLORO-PHENYL )-2-(3,5-DIMETHOXY-PHENYL)-PYRIMIDIN-4- YLAMINE
REMARK 900 RELATED ID: 1TK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL PEPTIDASE IV/CD26
REMARK 900 RELATED ID: 1TKR RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 INHIBITED WITHDIISOPROPYL
REMARK 900 FLUOROPHOSPHATE
REMARK 900 RELATED ID: 1U8E RELATED DB: PDB
REMARK 900 HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 MUTANT Y547F
REMARK 900 RELATED ID: 1W1I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR CD26) IN
REMARK 900 COMPLEX WITH ADENOSINE DEAMINASE
REMARK 900 RELATED ID: 2BGR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HIV-1 TAT DERIVED NONAPEPTIDES TAT(1-9) BOUND
REMARK 900 TO THE ACTIVE SITE OF DIPEPTIDYL PEPTIDASE IV (CD26)
REMARK 900 RELATED ID: 1KRM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOVINE ADENOSINE DEAMINASE COMPLEXED WITH 6-
REMARK 900 HYDROXYL-1,6- DIHYDROPURINE RIBOSIDE
REMARK 900 RELATED ID: 1NDV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH FR117016
REMARK 900 RELATED ID: 1NDW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH FR221647
REMARK 900 RELATED ID: 1NDY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH FR230513
REMARK 900 RELATED ID: 1NDZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH FR235999
REMARK 900 RELATED ID: 1O5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH APOTENT
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1QXL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH FR235380
REMARK 900 RELATED ID: 1UML RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH APOTENT
REMARK 900 INHIBITOR FR233624
REMARK 900 RELATED ID: 1V78 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF ADENOSINE DEAMINASE COMPLEXED WITH POTENT
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 1V79 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF ADENOSINE DEAMINASE COMPLEXED WITH POTENT
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 1V7A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF ADENOSINE DEAMINASE COMPLEXED WITH POTENT
REMARK 900 INHIBITORS
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 2BGN A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2BGN B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2BGN C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2BGN D 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2BGN E 1 1 PDB 2BGN 2BGN 1 1
DBREF 2BGN E 2 363 UNP P56658 ADA_BOVIN 1 362
DBREF 2BGN F 1 1 PDB 2BGN 2BGN 1 1
DBREF 2BGN F 2 363 UNP P56658 ADA_BOVIN 1 362
DBREF 2BGN G 1 1 PDB 2BGN 2BGN 1 1
DBREF 2BGN G 2 363 UNP P56658 ADA_BOVIN 1 362
DBREF 2BGN H 1 1 PDB 2BGN 2BGN 1 1
DBREF 2BGN H 2 363 UNP P56658 ADA_BOVIN 1 362
DBREF 2BGN W 1 9 UNP P12506 TAT_HV1Z2 1 9
DBREF 2BGN X 1 9 UNP P12506 TAT_HV1Z2 1 9
DBREF 2BGN Y 1 9 UNP P12506 TAT_HV1Z2 1 9
DBREF 2BGN Z 1 9 UNP P12506 TAT_HV1Z2 1 9
SEQADV 2BGN ASP E 8 UNP P56658 ASN 7 CONFLICT
SEQADV 2BGN LYS E 32 UNP P56658 ARG 31 CONFLICT
SEQADV 2BGN ARG E 33 UNP P56658 LYS 32 CONFLICT
SEQADV 2BGN LEU E 47 UNP P56658 GLN 46 CONFLICT
SEQADV 2BGN THR E 57 UNP P56658 SER 56 CONFLICT
SEQADV 2BGN ASP E 60 UNP P56658 GLU 59 CONFLICT
SEQADV 2BGN ASP E 77 UNP P56658 GLU 76 CONFLICT
SEQADV 2BGN ILE E 79 UNP P56658 VAL 78 CONFLICT
SEQADV 2BGN GLN E 199 UNP P56658 LYS 198 VARIANT
SEQADV 2BGN THR E 246 UNP P56658 ALA 245 VARIANT
SEQADV 2BGN ILE E 261 UNP P56658 VAL 260 CONFLICT
SEQADV 2BGN ALA E 279 UNP P56658 PRO 278 CONFLICT
SEQADV 2BGN ILE E 281 UNP P56658 VAL 280 CONFLICT
SEQADV 2BGN LYS E 313 UNP P56658 ASN 312 CONFLICT
SEQADV 2BGN ASP E 314 UNP P56658 GLU 313 CONFLICT
SEQADV 2BGN ARG E 352 UNP P56658 GLY 351 VARIANT
SEQADV 2BGN ASP F 8 UNP P56658 ASN 7 CONFLICT
SEQADV 2BGN LYS F 32 UNP P56658 ARG 31 CONFLICT
SEQADV 2BGN ARG F 33 UNP P56658 LYS 32 CONFLICT
SEQADV 2BGN LEU F 47 UNP P56658 GLN 46 CONFLICT
SEQADV 2BGN THR F 57 UNP P56658 SER 56 CONFLICT
SEQADV 2BGN ASP F 60 UNP P56658 GLU 59 CONFLICT
SEQADV 2BGN ASP F 77 UNP P56658 GLU 76 CONFLICT
SEQADV 2BGN ILE F 79 UNP P56658 VAL 78 CONFLICT
SEQADV 2BGN GLN F 199 UNP P56658 LYS 198 VARIANT
SEQADV 2BGN THR F 246 UNP P56658 ALA 245 VARIANT
SEQADV 2BGN ILE F 261 UNP P56658 VAL 260 CONFLICT
SEQADV 2BGN ALA F 279 UNP P56658 PRO 278 CONFLICT
SEQADV 2BGN ILE F 281 UNP P56658 VAL 280 CONFLICT
SEQADV 2BGN LYS F 313 UNP P56658 ASN 312 CONFLICT
SEQADV 2BGN ASP F 314 UNP P56658 GLU 313 CONFLICT
SEQADV 2BGN ARG F 352 UNP P56658 GLY 351 VARIANT
SEQADV 2BGN ASP G 8 UNP P56658 ASN 7 CONFLICT
SEQADV 2BGN LYS G 32 UNP P56658 ARG 31 CONFLICT
SEQADV 2BGN ARG G 33 UNP P56658 LYS 32 CONFLICT
SEQADV 2BGN LEU G 47 UNP P56658 GLN 46 CONFLICT
SEQADV 2BGN THR G 57 UNP P56658 SER 56 CONFLICT
SEQADV 2BGN ASP G 60 UNP P56658 GLU 59 CONFLICT
SEQADV 2BGN ASP G 77 UNP P56658 GLU 76 CONFLICT
SEQADV 2BGN ILE G 79 UNP P56658 VAL 78 CONFLICT
SEQADV 2BGN GLN G 199 UNP P56658 LYS 198 VARIANT
SEQADV 2BGN THR G 246 UNP P56658 ALA 245 VARIANT
SEQADV 2BGN ILE G 261 UNP P56658 VAL 260 CONFLICT
SEQADV 2BGN ALA G 279 UNP P56658 PRO 278 CONFLICT
SEQADV 2BGN ILE G 281 UNP P56658 VAL 280 CONFLICT
SEQADV 2BGN LYS G 313 UNP P56658 ASN 312 CONFLICT
SEQADV 2BGN ASP G 314 UNP P56658 GLU 313 CONFLICT
SEQADV 2BGN ARG G 352 UNP P56658 GLY 351 VARIANT
SEQADV 2BGN ASP H 8 UNP P56658 ASN 7 CONFLICT
SEQADV 2BGN LYS H 32 UNP P56658 ARG 31 CONFLICT
SEQADV 2BGN ARG H 33 UNP P56658 LYS 32 CONFLICT
SEQADV 2BGN LEU H 47 UNP P56658 GLN 46 CONFLICT
SEQADV 2BGN THR H 57 UNP P56658 SER 56 CONFLICT
SEQADV 2BGN ASP H 60 UNP P56658 GLU 59 CONFLICT
SEQADV 2BGN ASP H 77 UNP P56658 GLU 76 CONFLICT
SEQADV 2BGN ILE H 79 UNP P56658 VAL 78 CONFLICT
SEQADV 2BGN GLN H 199 UNP P56658 LYS 198 VARIANT
SEQADV 2BGN THR H 246 UNP P56658 ALA 245 VARIANT
SEQADV 2BGN ILE H 261 UNP P56658 VAL 260 CONFLICT
SEQADV 2BGN ALA H 279 UNP P56658 PRO 278 CONFLICT
SEQADV 2BGN ILE H 281 UNP P56658 VAL 280 CONFLICT
SEQADV 2BGN LYS H 313 UNP P56658 ASN 312 CONFLICT
SEQADV 2BGN ASP H 314 UNP P56658 GLU 313 CONFLICT
SEQADV 2BGN ARG H 352 UNP P56658 GLY 351 VARIANT
SEQADV 2BGN TRP W 2 UNP P12506 ASP 2 ENGINEERED MUTATION
SEQADV 2BGN TRP X 2 UNP P12506 ASP 2 ENGINEERED MUTATION
SEQADV 2BGN TRP Y 2 UNP P12506 ASP 2 ENGINEERED MUTATION
SEQADV 2BGN TRP Z 2 UNP P12506 ASP 2 ENGINEERED MUTATION
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 363 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 E 363 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 E 363 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 E 363 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 E 363 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 E 363 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 E 363 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 E 363 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 E 363 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 E 363 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 E 363 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 E 363 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 E 363 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 E 363 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 E 363 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 E 363 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 E 363 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 E 363 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 E 363 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 E 363 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 E 363 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 E 363 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 E 363 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 E 363 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 E 363 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 E 363 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 E 363 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 E 363 ARG MET PRO SER PRO ALA SER ALA GLU GLN CYS LEU
SEQRES 1 F 363 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 F 363 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 F 363 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 F 363 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 F 363 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 F 363 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 F 363 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 F 363 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 F 363 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 F 363 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 F 363 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 F 363 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 F 363 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 F 363 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 F 363 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 F 363 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 F 363 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 F 363 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 F 363 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 F 363 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 F 363 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 F 363 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 F 363 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 F 363 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 F 363 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 F 363 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 F 363 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 F 363 ARG MET PRO SER PRO ALA SER ALA GLU GLN CYS LEU
SEQRES 1 G 363 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 G 363 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 G 363 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 G 363 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 G 363 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 G 363 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 G 363 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 G 363 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 G 363 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 G 363 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 G 363 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 G 363 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 G 363 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 G 363 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 G 363 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 G 363 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 G 363 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 G 363 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 G 363 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 G 363 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 G 363 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 G 363 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 G 363 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 G 363 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 G 363 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 G 363 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 G 363 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 G 363 ARG MET PRO SER PRO ALA SER ALA GLU GLN CYS LEU
SEQRES 1 H 363 MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU
SEQRES 2 H 363 LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR
SEQRES 3 H 363 ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO
SEQRES 4 H 363 ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET
SEQRES 5 H 363 ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE
SEQRES 6 H 363 ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA
SEQRES 7 H 363 ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA
SEQRES 8 H 363 LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO
SEQRES 9 H 363 HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP
SEQRES 10 H 363 ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL
SEQRES 11 H 363 SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP
SEQRES 12 H 363 PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG
SEQRES 13 H 363 HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS
SEQRES 14 H 363 LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU
SEQRES 15 H 363 ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO
SEQRES 16 H 363 GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY
SEQRES 17 H 363 VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA
SEQRES 18 H 363 ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU
SEQRES 19 H 363 ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR
SEQRES 20 H 363 LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU
SEQRES 21 H 363 ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS
SEQRES 22 H 363 PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP
SEQRES 23 H 363 GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE
SEQRES 24 H 363 PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS
SEQRES 25 H 363 LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU
SEQRES 26 H 363 ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP
SEQRES 27 H 363 GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR
SEQRES 28 H 363 ARG MET PRO SER PRO ALA SER ALA GLU GLN CYS LEU
SEQRES 1 W 9 MET TRP PRO VAL ASP PRO ASN ILE GLU
SEQRES 1 X 9 MET TRP PRO VAL ASP PRO ASN ILE GLU
SEQRES 1 Y 9 MET TRP PRO VAL ASP PRO ASN ILE GLU
SEQRES 1 Z 9 MET TRP PRO VAL ASP PRO ASN ILE GLU
MODRES 2BGN ASN A 85 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 92 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 150 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 219 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 229 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 281 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 321 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN A 520 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 85 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 92 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 150 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 219 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 229 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 281 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 321 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN B 520 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 85 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 92 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 150 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 219 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 229 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 281 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 321 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN C 520 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 85 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 92 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 150 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 219 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 229 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 281 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 321 ASN GLYCOSYLATION SITE
MODRES 2BGN ASN D 520 ASN GLYCOSYLATION SITE
HET NAG I 1 14
HET NAG I 2 14
HET FUL I 3 10
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET MAN L 4 11
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET FUL N 2 10
HET NAG O 1 14
HET NAG O 2 14
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET MAN P 4 11
HET NAG Q 1 14
HET NAG Q 2 14
HET NAG R 1 14
HET NAG R 2 14
HET FUL R 3 10
HET NAG S 1 14
HET NAG S 2 14
HET NAG T 1 14
HET NAG T 2 14
HET NAG U 1 14
HET NAG U 2 14
HET BMA U 3 11
HET MAN U 4 11
HET NAG V 1 14
HET NAG V 2 14
HET NAG a 1 14
HET FUL a 2 10
HET NAG b 1 14
HET NAG b 2 14
HET NAG c 1 14
HET NAG c 2 14
HET BMA c 3 11
HET MAN c 4 11
HET NAG d 1 14
HET NAG d 2 14
HET NAG A 840 14
HET NAG A 860 14
HET NAG A 870 14
HET NAG B 810 14
HET NAG B 840 14
HET NAG B 860 14
HET NAG B 870 14
HET NAG C 840 14
HET NAG C 860 14
HET NAG C 870 14
HET NAG D 810 14
HET NAG D 840 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 NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 13 NAG 48(C8 H15 N O6)
FORMUL 13 FUL 4(C6 H12 O5)
FORMUL 16 BMA 4(C6 H12 O6)
FORMUL 16 MAN 4(C6 H12 O6)
FORMUL 45 ZN 4(ZN 2+)
HELIX 1 1 THR A 44 LYS A 50 1 7
HELIX 2 2 ASP A 200 VAL A 207 1 8
HELIX 3 3 PRO A 290 ILE A 295 1 6
HELIX 4 4 VAL A 341 GLN A 344 5 4
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 ASN A 506 1 10
HELIX 7 7 ASN A 562 THR A 570 1 9
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 LYS A 615 1 16
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 HIS A 712 VAL A 726 1 15
HELIX 17 17 SER A 744 PHE A 763 1 20
HELIX 18 18 THR B 44 LYS B 50 1 7
HELIX 19 19 ASP B 200 VAL B 207 1 8
HELIX 20 20 PRO B 290 ILE B 295 1 6
HELIX 21 21 GLU B 421 MET B 425 5 5
HELIX 22 22 ASN B 497 ASN B 506 1 10
HELIX 23 23 ASN B 562 THR B 570 1 9
HELIX 24 24 GLY B 587 HIS B 592 1 6
HELIX 25 25 ALA B 593 ASN B 595 5 3
HELIX 26 26 THR B 600 LYS B 615 1 16
HELIX 27 27 SER B 630 GLY B 641 1 12
HELIX 28 28 ARG B 658 TYR B 662 5 5
HELIX 29 29 ASP B 663 GLY B 672 1 10
HELIX 30 30 ASN B 679 SER B 686 1 8
HELIX 31 31 VAL B 688 VAL B 698 5 11
HELIX 32 32 HIS B 712 VAL B 726 1 15
HELIX 33 33 SER B 744 PHE B 763 1 20
HELIX 34 34 THR C 44 LYS C 50 1 7
HELIX 35 35 ASP C 200 VAL C 207 1 8
HELIX 36 36 PRO C 290 ILE C 295 1 6
HELIX 37 37 VAL C 341 GLN C 344 5 4
HELIX 38 38 GLU C 421 MET C 425 5 5
HELIX 39 39 ASN C 497 ASN C 506 1 10
HELIX 40 40 ASN C 562 THR C 570 1 9
HELIX 41 41 GLY C 587 HIS C 592 1 6
HELIX 42 42 ALA C 593 ASN C 595 5 3
HELIX 43 43 THR C 600 LYS C 615 1 16
HELIX 44 44 SER C 630 GLY C 641 1 12
HELIX 45 45 ARG C 658 TYR C 662 5 5
HELIX 46 46 ASP C 663 GLY C 672 1 10
HELIX 47 47 ASN C 679 SER C 686 1 8
HELIX 48 48 VAL C 688 VAL C 698 5 11
HELIX 49 49 HIS C 712 VAL C 726 1 15
HELIX 50 50 SER C 744 PHE C 763 1 20
HELIX 51 51 THR D 44 LYS D 50 1 7
HELIX 52 52 ASP D 200 VAL D 207 1 8
HELIX 53 53 PRO D 290 ILE D 295 1 6
HELIX 54 54 VAL D 341 GLN D 344 5 4
HELIX 55 55 GLU D 421 MET D 425 5 5
HELIX 56 56 ASN D 497 ASN D 506 1 10
HELIX 57 57 ASN D 562 THR D 570 1 9
HELIX 58 58 GLY D 587 HIS D 592 1 6
HELIX 59 59 ALA D 593 ASN D 595 5 3
HELIX 60 60 THR D 600 LYS D 615 1 16
HELIX 61 61 SER D 630 GLY D 641 1 12
HELIX 62 62 ARG D 658 TYR D 662 5 5
HELIX 63 63 ASP D 663 GLY D 672 1 10
HELIX 64 64 ASN D 679 SER D 686 1 8
HELIX 65 65 VAL D 688 VAL D 698 5 11
HELIX 66 66 HIS D 712 VAL D 726 1 15
HELIX 67 67 SER D 744 PHE D 763 1 20
HELIX 68 68 LYS E 23 GLY E 35 1 13
HELIX 69 69 THR E 42 GLY E 51 1 10
HELIX 70 70 THR E 57 ALA E 63 1 7
HELIX 71 71 ALA E 63 ALA E 73 1 11
HELIX 72 72 CYS E 75 ASP E 93 1 19
HELIX 73 73 SER E 103 ALA E 108 5 6
HELIX 74 74 THR E 125 GLY E 145 1 21
HELIX 75 75 TRP E 161 TYR E 172 1 12
HELIX 76 76 GLY E 190 LEU E 193 5 4
HELIX 77 77 PHE E 194 GLY E 208 1 15
HELIX 78 78 SER E 220 ASP E 229 1 10
HELIX 79 79 TYR E 240 LEU E 243 5 4
HELIX 80 80 ASP E 245 ASN E 256 1 12
HELIX 81 81 CYS E 262 GLY E 270 1 9
HELIX 82 82 HIS E 278 ASP E 286 1 9
HELIX 83 83 THR E 303 GLY E 316 1 14
HELIX 84 84 THR E 318 SER E 333 1 16
HELIX 85 85 PRO E 336 TYR E 351 1 16
HELIX 86 86 LYS F 23 GLY F 35 1 13
HELIX 87 87 THR F 42 GLY F 51 1 10
HELIX 88 88 THR F 57 ALA F 63 1 7
HELIX 89 89 ALA F 63 ALA F 73 1 11
HELIX 90 90 ARG F 76 ASP F 93 1 18
HELIX 91 91 SER F 103 ALA F 108 5 6
HELIX 92 92 ILE F 115 GLN F 119 5 5
HELIX 93 93 THR F 125 GLY F 145 1 21
HELIX 94 94 TRP F 161 TYR F 172 1 12
HELIX 95 95 ARG F 173 GLN F 175 5 3
HELIX 96 96 GLY F 190 LEU F 193 5 4
HELIX 97 97 PHE F 194 GLY F 208 1 15
HELIX 98 98 SER F 220 ASP F 229 1 10
HELIX 99 99 ASP F 245 ASN F 256 1 12
HELIX 100 100 CYS F 262 GLY F 270 1 9
HELIX 101 101 HIS F 278 ASP F 286 1 9
HELIX 102 102 ASP F 296 LYS F 301 1 6
HELIX 103 103 ASP F 307 GLY F 316 1 10
HELIX 104 104 THR F 318 SER F 333 1 16
HELIX 105 105 GLU F 337 TYR F 351 1 15
HELIX 106 106 LYS G 23 GLY G 35 1 13
HELIX 107 107 THR G 42 GLY G 51 1 10
HELIX 108 108 THR G 57 ALA G 63 1 7
HELIX 109 109 ALA G 63 ALA G 73 1 11
HELIX 110 110 CYS G 75 ASP G 93 1 19
HELIX 111 111 SER G 103 ALA G 108 5 6
HELIX 112 112 ILE G 115 GLN G 119 5 5
HELIX 113 113 THR G 125 GLY G 145 1 21
HELIX 114 114 TRP G 161 TYR G 172 1 12
HELIX 115 115 GLY G 190 LEU G 193 5 4
HELIX 116 116 PHE G 194 GLY G 208 1 15
HELIX 117 117 SER G 220 THR G 230 1 11
HELIX 118 118 TYR G 240 LEU G 243 5 4
HELIX 119 119 ASP G 245 ASN G 256 1 12
HELIX 120 120 CYS G 262 GLY G 270 1 9
HELIX 121 121 HIS G 278 ASP G 286 1 9
HELIX 122 122 ASP G 296 LYS G 301 1 6
HELIX 123 123 THR G 303 GLY G 316 1 14
HELIX 124 124 THR G 318 SER G 333 1 16
HELIX 125 125 PRO G 336 ARG G 352 1 17
HELIX 126 126 LYS H 23 GLY H 35 1 13
HELIX 127 127 THR H 42 GLY H 51 1 10
HELIX 128 128 THR H 57 ALA H 63 1 7
HELIX 129 129 ALA H 63 ALA H 73 1 11
HELIX 130 130 CYS H 75 ASP H 93 1 19
HELIX 131 131 SER H 103 ALA H 108 5 6
HELIX 132 132 ILE H 115 GLN H 119 5 5
HELIX 133 133 THR H 125 PHE H 144 1 20
HELIX 134 134 TRP H 161 TYR H 172 1 12
HELIX 135 135 GLY H 190 LEU H 193 5 4
HELIX 136 136 PHE H 194 GLY H 208 1 15
HELIX 137 137 SER H 220 ASP H 229 1 10
HELIX 138 138 TYR H 240 LEU H 243 5 4
HELIX 139 139 ASP H 245 GLU H 255 1 11
HELIX 140 140 CYS H 262 GLY H 270 1 9
HELIX 141 141 VAL H 280 ASN H 285 1 6
HELIX 142 142 LEU H 304 GLY H 316 1 13
HELIX 143 143 THR H 318 SER H 332 1 15
HELIX 144 144 PRO H 336 ARG H 352 1 17
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 3 PHE A 113 LYS A 122 0
SHEET 2 AC 3 TYR A 128 ASP A 136 -1 O THR A 129 N VAL A 121
SHEET 3 AC 3 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 SER A 284 ILE A 287 -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 THR A 307 0
SHEET 2 AH 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
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 THR A 307 0
SHEET 2 AI 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
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 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
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 LEU B 60 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 3 PHE B 113 LYS B 122 0
SHEET 2 BC 3 TYR B 128 ASP B 136 -1 O THR B 129 N VAL B 121
SHEET 3 BC 3 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 GLN B 286 -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 THR B 307 0
SHEET 2 BH 7 ARG B 310 ARG B 317 -1 O ARG B 310 N ALA B 306
SHEET 3 BH 7 TYR B 322 ASP B 331 -1 O TYR B 322 N ARG B 317
SHEET 4 BH 7 ARG B 336 ASN B 338 -1 O ARG B 336 N ASP B 331
SHEET 5 BH 7 TYR B 322 ASP B 331 -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 ASP B 331 -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 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
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 VAL B 546 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 LEU C 60 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 3 PHE C 113 LYS C 122 0
SHEET 2 CC 3 TYR C 128 ASP C 136 -1 O THR C 129 N VAL C 121
SHEET 3 CC 3 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 ILE C 285 GLN C 286 0
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 THR C 307 0
SHEET 2 CG 7 ARG C 310 ARG C 317 -1 O ARG C 310 N ALA C 306
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 THR C 395 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 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
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 2 LYS D 41 THR D 42 0
SHEET 2 DA 2 VAL D 507 GLN D 508 1 N GLN D 508 O LYS D 41
SHEET 1 DB 4 LEU D 60 TRP D 62 0
SHEET 2 DB 4 GLU D 67 GLN D 72 -1 O LEU D 69 N ARG D 61
SHEET 3 DB 4 ASN D 75 ASN D 80 -1 O ASN D 75 N GLN D 72
SHEET 4 DB 4 SER D 86 LEU D 90 -1 O SER D 87 N VAL D 78
SHEET 1 DC 3 PHE D 113 LYS D 122 0
SHEET 2 DC 3 TYR D 128 ASP D 136 -1 O THR D 129 N VAL D 121
SHEET 3 DC 3 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 DD 4 TRP D 154 TRP D 157 0
SHEET 2 DD 4 LEU D 164 TRP D 168 -1 O ALA D 165 N THR D 156
SHEET 3 DD 4 ASP D 171 LYS D 175 -1 O ASP D 171 N TRP D 168
SHEET 4 DD 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 DE 7 ILE D 194 ASN D 196 0
SHEET 2 DE 7 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 DE 7 LEU D 214 TRP D 216 -1 O TRP D 215 N ALA D 224
SHEET 4 DE 7 PHE D 222 ASN D 229 -1 O ALA D 224 N TRP D 215
SHEET 5 DE 7 ILE D 285 GLN D 286 0
SHEET 6 DE 7 THR D 265 ASN D 272 -1 O VAL D 270 N ILE D 285
SHEET 7 DE 7 PHE D 222 ASN D 229 -1 O LEU D 223 N VAL D 271
SHEET 1 DF 2 LEU D 235 PHE D 240 0
SHEET 2 DF 2 LYS D 250 PRO D 255 -1 O LYS D 250 N PHE D 240
SHEET 1 DG 7 HIS D 298 THR D 307 0
SHEET 2 DG 7 ARG D 310 ARG D 317 -1 O ARG D 310 N ALA D 306
SHEET 3 DG 7 TYR D 322 ASP D 331 -1 O TYR D 322 N ARG D 317
SHEET 4 DG 7 ARG D 336 CYS D 339 -1 O ARG D 336 N ASP D 331
SHEET 5 DG 7 TYR D 322 ASP D 331 -1 O ASP D 329 N ASN D 338
SHEET 6 DG 7 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 7 DG 7 TYR D 322 ASP D 331 -1 O SER D 323 N GLU D 347
SHEET 1 DH 4 HIS D 363 PHE D 364 0
SHEET 2 DH 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 DH 4 ARG D 382 GLN D 388 -1 O HIS D 383 N ILE D 375
SHEET 4 DH 4 LYS D 391 PHE D 396 -1 O LYS D 391 N GLN D 388
SHEET 1 DI 4 VAL D 404 LEU D 410 0
SHEET 2 DI 4 TYR D 414 SER D 419 -1 O TYR D 416 N GLU D 408
SHEET 3 DI 4 ASN D 430 GLN D 435 -1 O ASN D 430 N SER D 419
SHEET 4 DI 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 DJ 4 TYR D 457 PHE D 461 0
SHEET 2 DJ 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 DJ 4 LEU D 479 SER D 484 -1 O LEU D 479 N CYS D 472
SHEET 4 DJ 4 LYS D 489 GLU D 495 -1 O LYS D 489 N SER D 484
SHEET 1 DK 8 SER D 511 LEU D 519 0
SHEET 2 DK 8 THR D 522 LEU D 530 -1 O THR D 522 N LEU D 519
SHEET 3 DK 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 DK 8 TYR D 540 VAL D 546 1 O PRO D 541 N ILE D 574
SHEET 5 DK 8 VAL D 619 TRP D 629 1 N ASP D 620 O TYR D 540
SHEET 6 DK 8 CYS D 649 VAL D 653 1 O CYS D 649 N ILE D 626
SHEET 7 DK 8 GLU D 699 GLY D 705 1 O GLU D 699 N GLY D 650
SHEET 8 DK 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 GLU F 13 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 HIS F 214 1 O HIS F 210 N ILE F 180
SHEET 6 FA 8 ARG F 235 GLY F 237 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 GLU H 13 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 TYR H 290 LEU H 292 1 O SER H 291 N ILE H 261
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.06
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.05
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.05
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.05
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.05
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.04
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.05
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.05
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.05
SSBOND 11 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 12 CYS C 385 CYS C 394 1555 1555 2.06
SSBOND 13 CYS C 444 CYS C 447 1555 1555 2.06
SSBOND 14 CYS C 454 CYS C 472 1555 1555 2.06
SSBOND 15 CYS C 649 CYS C 762 1555 1555 2.05
SSBOND 16 CYS D 328 CYS D 339 1555 1555 2.04
SSBOND 17 CYS D 385 CYS D 394 1555 1555 2.06
SSBOND 18 CYS D 444 CYS D 447 1555 1555 2.05
SSBOND 19 CYS D 454 CYS D 472 1555 1555 2.05
SSBOND 20 CYS D 649 CYS D 762 1555 1555 2.05
LINK ND2 ASN A 85 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN A 92 C1 NAG A 870 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG A 840 1555 1555 1.46
LINK ND2 ASN A 321 C1 NAG M 1 1555 1555 1.45
LINK ND2 ASN A 520 C1 NAG A 860 1555 1555 1.45
LINK ND2 ASN B 85 C1 NAG N 1 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG B 870 1555 1555 1.45
LINK ND2 ASN B 150 C1 NAG B 810 1555 1555 1.45
LINK ND2 ASN B 219 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG P 1 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG B 840 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG Q 1 1555 1555 1.44
LINK ND2 ASN B 520 C1 NAG B 860 1555 1555 1.44
LINK ND2 ASN C 85 C1 NAG R 1 1555 1555 1.45
LINK ND2 ASN C 92 C1 NAG C 870 1555 1555 1.44
LINK ND2 ASN C 150 C1 NAG S 1 1555 1555 1.44
LINK ND2 ASN C 219 C1 NAG T 1 1555 1555 1.45
LINK ND2 ASN C 229 C1 NAG U 1 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG C 840 1555 1555 1.46
LINK ND2 ASN C 321 C1 NAG V 1 1555 1555 1.48
LINK ND2 ASN C 321 O5 NAG V 1 1555 1555 1.85
LINK ND2 ASN C 520 C1 NAG C 860 1555 1555 1.44
LINK ND2 ASN D 85 C1 NAG a 1 1555 1555 1.44
LINK ND2 ASN D 92 C1 NAG D 870 1555 1555 1.45
LINK ND2 ASN D 150 C1 NAG D 810 1555 1555 1.45
LINK ND2 ASN D 219 C1 NAG b 1 1555 1555 1.44
LINK ND2 ASN D 229 C1 NAG c 1 1555 1555 1.44
LINK ND2 ASN D 281 C1 NAG D 840 1555 1555 1.46
LINK ND2 ASN D 321 C1 NAG d 1 1555 1555 1.44
LINK ND2 ASN D 520 C1 NAG D 860 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O6 NAG I 1 C1 FUL I 3 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44
LINK O3 BMA L 3 C1 MAN L 4 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.43
LINK O6 NAG N 1 C1 FUL N 2 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.43
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44
LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44
LINK O6 NAG R 1 C1 FUL R 3 1555 1555 1.44
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45
LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.43
LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44
LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44
LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.46
LINK O6 NAG a 1 C1 FUL a 2 1555 1555 1.40
LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.45
LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44
LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.44
LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.45
LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.42
LINK NE2 HIS E 15 ZN ZN E 501 1555 1555 2.08
LINK NE2 HIS E 17 ZN ZN E 501 1555 1555 2.07
LINK NE2 HIS E 214 ZN ZN E 501 1555 1555 2.01
LINK OD1 ASP E 295 ZN ZN E 501 1555 1555 2.19
LINK NE2 HIS F 15 ZN ZN F 501 1555 1555 2.09
LINK NE2 HIS F 17 ZN ZN F 501 1555 1555 2.13
LINK NE2 HIS F 214 ZN ZN F 501 1555 1555 2.07
LINK OD1 ASP F 295 ZN ZN F 501 1555 1555 2.21
LINK NE2 HIS G 15 ZN ZN G 501 1555 1555 2.09
LINK NE2 HIS G 17 ZN ZN G 501 1555 1555 2.09
LINK NE2 HIS G 214 ZN ZN G 501 1555 1555 2.09
LINK OD1 ASP G 295 ZN ZN G 501 1555 1555 2.23
LINK NE2 HIS H 15 ZN ZN H 501 1555 1555 2.05
LINK NE2 HIS H 17 ZN ZN H 501 1555 1555 2.09
LINK NE2 HIS H 214 ZN ZN H 501 1555 1555 2.06
LINK OD1 ASP H 295 ZN ZN H 501 1555 1555 2.21
CISPEP 1 GLY A 474 PRO A 475 0 10.40
CISPEP 2 GLY B 474 PRO B 475 0 8.90
CISPEP 3 GLY C 474 PRO C 475 0 10.16
CISPEP 4 GLY D 474 PRO D 475 0 11.52
CISPEP 5 GLU E 121 GLY E 122 0 9.30
CISPEP 6 GLU F 121 GLY F 122 0 12.01
CISPEP 7 ALA F 350 TYR F 351 0 -28.54
CISPEP 8 GLU G 121 GLY G 122 0 9.61
CISPEP 9 GLU H 121 GLY H 122 0 10.19
CRYST1 158.945 170.273 239.200 90.00 100.93 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 0.006291 0.000000 0.001215 0.00000
SCALE2 0.000000 0.005873 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004258 0.00000
MTRIX1 1 -0.780000 -0.593000 -0.203000 56.66322 1
MTRIX2 1 -0.586000 0.577000 0.568000 -47.59455 1
MTRIX3 1 -0.220000 0.562000 -0.797000 192.04016 1
MTRIX1 2 -0.997000 -0.032000 0.072000 -4.96595 1
MTRIX2 2 0.031000 -0.999000 -0.018000 14.84250 1
MTRIX3 2 0.072000 -0.016000 0.997000 -116.32928 1
MTRIX1 3 0.744000 0.620000 -0.251000 76.30225 1
MTRIX2 3 0.648000 -0.575000 0.500000 -98.93713 1
MTRIX3 3 0.165000 -0.534000 -0.829000 295.61942 1
MTRIX1 4 -0.772000 0.577000 -0.264000 -70.63954 1
MTRIX2 4 0.610000 0.558000 -0.563000 17.53247 1
MTRIX3 4 -0.178000 -0.596000 -0.783000 286.85556 1
MTRIX1 5 -0.757000 -0.597000 0.264000 -37.52310 1
MTRIX2 5 0.634000 -0.575000 0.517000 88.54301 1
MTRIX3 5 -0.157000 0.559000 0.814000 80.94585 1
MTRIX1 6 0.989000 0.073000 -0.125000 -28.64116 1
MTRIX2 6 0.066000 -0.996000 -0.059000 22.80677 1
MTRIX3 6 -0.129000 0.050000 -0.990000 350.30649 1
(ATOM LINES ARE NOT SHOWN.)
END
