HEADER PROTEIN BINDING 16-JUN-12 4FMB
TITLE VIRA-RAB1 COMPLEX STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE PROTEASE-LIKE VIRA;
COMPND 3 CHAIN: A, C, E;
COMPND 4 SYNONYM: EFFECTOR PROTEIN VIRA;
COMPND 5 EC: 3.4.22.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RAS-RELATED PROTEIN RAB-1A;
COMPND 9 CHAIN: B, D, F;
COMPND 10 SYNONYM: YPT1-RELATED PROTEIN;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 STRAIN: 301;
SOURCE 5 GENE: CP0181, PWR501_0191, VIRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RAB1, RAB1A;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA-BETA FOLD, RAB1-GAP COMPLEX, RAB1, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR F.SHAO,Y.ZHU
REVDAT 2 03-OCT-12 4FMB 1 JRNL
REVDAT 1 05-SEP-12 4FMB 0
JRNL AUTH N.DONG,Y.ZHU,Q.LU,L.HU,Y.ZHENG,F.SHAO
JRNL TITL STRUCTURALLY DISTINCT BACTERIAL TBC-LIKE GAPS LINK ARF
JRNL TITL 2 GTPASE TO RAB1 INACTIVATION TO COUNTERACT HOST DEFENSES.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 150 1029 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22939626
JRNL DOI 10.1016/J.CELL.2012.06.050
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 37746
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1886
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2594
REMARK 3 BIN R VALUE (WORKING SET) : 0.4134
REMARK 3 BIN FREE R VALUE : 0.3884
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12327
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 9
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.36800
REMARK 3 B22 (A**2) : 24.74700
REMARK 3 B33 (A**2) : -8.37900
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 32.26300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.603 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.284 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.426 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.825 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 55.06
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : GDP.PAR
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40511
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M AMMONIUM SULFATE AND 0.1 M TRIS-
REMARK 280 HCL (PH 7.6), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 93.05900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.65550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 93.05900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 63.65550
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, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 126990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -246.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 PRO A 328
REMARK 465 LYS A 329
REMARK 465 ASN A 330
REMARK 465 ASP A 331
REMARK 465 THR A 332
REMARK 465 ALA A 333
REMARK 465 ILE A 334
REMARK 465 SER A 335
REMARK 465 ALA A 336
REMARK 465 SER A 337
REMARK 465 LYS C 329
REMARK 465 ASN C 330
REMARK 465 ASP C 331
REMARK 465 THR C 332
REMARK 465 ALA C 333
REMARK 465 ILE C 334
REMARK 465 SER C 335
REMARK 465 ALA C 336
REMARK 465 SER C 337
REMARK 465 GLY C 338
REMARK 465 GLY C 339
REMARK 465 LYS E 329
REMARK 465 ASN E 330
REMARK 465 ASP E 331
REMARK 465 THR E 332
REMARK 465 ALA E 333
REMARK 465 ILE E 334
REMARK 465 SER E 335
REMARK 465 ALA E 336
REMARK 465 SER E 337
REMARK 465 GLY E 338
REMARK 465 GLY E 339
REMARK 465 PRO F 6
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 VAL A 400 CG1 CG2
REMARK 470 VAL C 400 CG1 CG2
REMARK 470 VAL E 400 CG1 CG2
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 ARG A 312 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 312 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 82 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 82 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG C 312 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG C 312 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG D 82 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG D 82 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 70 155.22 -44.98
REMARK 500 PRO A 126 64.56 -68.23
REMARK 500 LYS A 133 139.95 -177.07
REMARK 500 VAL A 141 140.17 -173.17
REMARK 500 PHE A 145 40.92 -106.28
REMARK 500 ASP A 170 33.81 -91.43
REMARK 500 ALA A 192 36.16 -92.15
REMARK 500 MET A 233 174.88 -55.24
REMARK 500 PHE A 254 52.30 -103.62
REMARK 500 ALA A 277 -16.69 -47.41
REMARK 500 MET A 308 77.64 -160.38
REMARK 500 LEU A 349 67.66 -114.89
REMARK 500 PRO A 375 83.66 -68.52
REMARK 500 PRO A 398 -165.12 -72.79
REMARK 500 ILE B 41 -168.00 -75.58
REMARK 500 TYR B 112 -47.95 -137.23
REMARK 500 VAL B 133 -2.52 -143.13
REMARK 500 ASN B 160 18.89 55.70
REMARK 500 ARG B 175 -70.85 -129.77
REMARK 500 SER C 70 155.37 -44.42
REMARK 500 ASP C 105 -33.03 -130.13
REMARK 500 PRO C 126 64.46 -69.50
REMARK 500 LYS C 133 141.51 -177.02
REMARK 500 VAL C 141 141.18 -173.77
REMARK 500 PHE C 145 40.14 -104.65
REMARK 500 ASP C 170 32.78 -91.16
REMARK 500 ALA C 192 36.93 -91.16
REMARK 500 MET C 233 175.51 -56.06
REMARK 500 CYS C 253 -79.17 -57.52
REMARK 500 PHE C 254 51.39 -90.34
REMARK 500 ALA C 277 -17.02 -48.10
REMARK 500 MET C 308 76.26 -159.79
REMARK 500 LEU C 349 68.61 -115.22
REMARK 500 PRO C 375 84.26 -68.98
REMARK 500 ILE C 384 65.88 -119.81
REMARK 500 PRO C 398 -164.58 -72.56
REMARK 500 ILE D 41 -168.41 -78.47
REMARK 500 TYR D 112 -48.38 -137.66
REMARK 500 VAL D 133 -2.26 -142.37
REMARK 500 GLU D 141 -70.46 -64.85
REMARK 500 ASN D 160 19.06 54.83
REMARK 500 ARG D 175 -70.33 -130.22
REMARK 500 SER E 70 155.30 -44.21
REMARK 500 ASP E 105 -32.65 -130.02
REMARK 500 PRO E 126 63.77 -68.15
REMARK 500 LYS E 133 142.81 -175.48
REMARK 500 VAL E 141 140.96 -173.43
REMARK 500 PHE E 145 40.89 -104.48
REMARK 500 ASP E 170 33.96 -91.54
REMARK 500 PHE E 179 19.43 52.92
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
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 MG B 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 303 O
REMARK 620 2 HOH B 302 O 178.6
REMARK 620 3 SER B 25 OG 90.9 87.7
REMARK 620 4 GDP B 202 O3B 92.4 87.8 84.8
REMARK 620 5 THR B 43 OG1 92.6 87.3 99.2 173.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 302 O
REMARK 620 2 HOH D 301 O 176.0
REMARK 620 3 SER D 25 OG 89.7 94.3
REMARK 620 4 THR D 43 OG1 91.1 88.2 98.3
REMARK 620 5 GDP D 202 O3B 90.0 90.8 79.5 177.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 302 O
REMARK 620 2 HOH F 301 O 179.6
REMARK 620 3 SER F 25 OG 89.7 90.2
REMARK 620 4 THR F 43 OG1 87.1 92.4 98.5
REMARK 620 5 GDP F 202 O3B 97.2 83.2 82.9 175.4
REMARK 620 6 GDP F 202 O1B 75.2 105.2 127.8 129.3 51.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 B 201 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP B 202 O1B
REMARK 620 2 AF3 B 201 F1 89.3
REMARK 620 3 AF3 B 201 F2 90.2 116.9
REMARK 620 4 AF3 B 201 F3 93.4 119.9 123.2
REMARK 620 5 HOH B 301 O 173.5 92.3 94.7 80.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 F 201 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP F 202 O1B
REMARK 620 2 AF3 F 201 F1 94.7
REMARK 620 3 AF3 F 201 F2 90.3 118.6
REMARK 620 4 AF3 F 201 F3 86.3 122.5 118.9
REMARK 620 5 HOH E 501 O 173.7 88.5 93.0 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 D 201 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP D 202 O1B
REMARK 620 2 AF3 D 201 F1 96.2
REMARK 620 3 AF3 D 201 F2 87.2 114.3
REMARK 620 4 AF3 D 201 F3 92.9 126.0 119.3
REMARK 620 5 HOH C 501 O 173.2 90.3 92.3 81.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FMA RELATED DB: PDB
REMARK 900 RELATED ID: 4FMC RELATED DB: PDB
REMARK 900 RELATED ID: 4FMD RELATED DB: PDB
REMARK 900 RELATED ID: 4FME RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES WERE CONFIRMED BY GENE SEQUENCING
DBREF 4FMB A 45 400 UNP Q7BU69 VIRA_SHIFL 45 400
DBREF 4FMB B 6 176 UNP P62820 RAB1A_HUMAN 6 176
DBREF 4FMB C 45 400 UNP Q7BU69 VIRA_SHIFL 45 400
DBREF 4FMB D 6 176 UNP P62820 RAB1A_HUMAN 6 176
DBREF 4FMB E 45 400 UNP Q7BU69 VIRA_SHIFL 45 400
DBREF 4FMB F 6 176 UNP P62820 RAB1A_HUMAN 6 176
SEQADV 4FMB GLY A 40 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB PRO A 41 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB LEU A 42 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB GLY A 43 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB SER A 44 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB ALA B 10 UNP P62820 TYR 10 SEE REMARK 999
SEQADV 4FMB GLY C 40 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB PRO C 41 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB LEU C 42 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB GLY C 43 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB SER C 44 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB ALA D 10 UNP P62820 TYR 10 SEE REMARK 999
SEQADV 4FMB GLY E 40 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB PRO E 41 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB LEU E 42 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB GLY E 43 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB SER E 44 UNP Q7BU69 EXPRESSION TAG
SEQADV 4FMB ALA F 10 UNP P62820 TYR 10 SEE REMARK 999
SEQRES 1 A 361 GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU
SEQRES 2 A 361 ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE
SEQRES 3 A 361 SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE
SEQRES 4 A 361 ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS
SEQRES 5 A 361 LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY
SEQRES 6 A 361 ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR
SEQRES 7 A 361 ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN
SEQRES 8 A 361 LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY
SEQRES 9 A 361 ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU
SEQRES 10 A 361 THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP
SEQRES 11 A 361 ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL
SEQRES 12 A 361 TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER
SEQRES 13 A 361 ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO
SEQRES 14 A 361 LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE
SEQRES 15 A 361 ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU
SEQRES 16 A 361 SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE
SEQRES 17 A 361 PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU
SEQRES 18 A 361 PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA
SEQRES 19 A 361 LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER
SEQRES 20 A 361 SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU
SEQRES 21 A 361 ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG
SEQRES 22 A 361 VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA
SEQRES 23 A 361 VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY
SEQRES 24 A 361 GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER
SEQRES 25 A 361 HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU
SEQRES 26 A 361 THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER
SEQRES 27 A 361 GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN
SEQRES 28 A 361 VAL SER PHE ALA ILE ILE SER PRO ASP VAL
SEQRES 1 B 171 PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY
SEQRES 2 B 171 ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE
SEQRES 3 B 171 ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE
SEQRES 4 B 171 GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY
SEQRES 5 B 171 LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN
SEQRES 6 B 171 GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY
SEQRES 7 B 171 ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN
SEQRES 8 B 171 GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE
SEQRES 9 B 171 ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL
SEQRES 10 B 171 GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP
SEQRES 11 B 171 TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE
SEQRES 12 B 171 PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL
SEQRES 13 B 171 GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS
SEQRES 14 B 171 ARG MET
SEQRES 1 C 361 GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU
SEQRES 2 C 361 ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE
SEQRES 3 C 361 SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE
SEQRES 4 C 361 ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS
SEQRES 5 C 361 LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY
SEQRES 6 C 361 ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR
SEQRES 7 C 361 ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN
SEQRES 8 C 361 LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY
SEQRES 9 C 361 ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU
SEQRES 10 C 361 THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP
SEQRES 11 C 361 ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL
SEQRES 12 C 361 TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER
SEQRES 13 C 361 ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO
SEQRES 14 C 361 LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE
SEQRES 15 C 361 ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU
SEQRES 16 C 361 SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE
SEQRES 17 C 361 PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU
SEQRES 18 C 361 PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA
SEQRES 19 C 361 LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER
SEQRES 20 C 361 SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU
SEQRES 21 C 361 ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG
SEQRES 22 C 361 VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA
SEQRES 23 C 361 VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY
SEQRES 24 C 361 GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER
SEQRES 25 C 361 HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU
SEQRES 26 C 361 THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER
SEQRES 27 C 361 GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN
SEQRES 28 C 361 VAL SER PHE ALA ILE ILE SER PRO ASP VAL
SEQRES 1 D 171 PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY
SEQRES 2 D 171 ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE
SEQRES 3 D 171 ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE
SEQRES 4 D 171 GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY
SEQRES 5 D 171 LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN
SEQRES 6 D 171 GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY
SEQRES 7 D 171 ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN
SEQRES 8 D 171 GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE
SEQRES 9 D 171 ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL
SEQRES 10 D 171 GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP
SEQRES 11 D 171 TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE
SEQRES 12 D 171 PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL
SEQRES 13 D 171 GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS
SEQRES 14 D 171 ARG MET
SEQRES 1 E 361 GLY PRO LEU GLY SER ILE TYR SER PRO HIS GLU THR LEU
SEQRES 2 E 361 ALA GLU LYS HIS SER GLU LYS LYS LEU MET ASP SER PHE
SEQRES 3 E 361 SER PRO SER LEU SER GLN ASP LYS MET ASP GLY GLU PHE
SEQRES 4 E 361 ALA HIS ALA ASN ILE ASP GLY ILE SER ILE ARG LEU CYS
SEQRES 5 E 361 LEU ASN LYS GLY ILE CYS SER VAL PHE TYR LEU ASP GLY
SEQRES 6 E 361 ASP LYS ILE GLN SER THR GLN LEU SER SER LYS GLU TYR
SEQRES 7 E 361 ASN ASN LEU LEU SER SER LEU PRO PRO LYS GLN PHE ASN
SEQRES 8 E 361 LEU GLY LYS VAL HIS THR ILE THR ALA PRO VAL SER GLY
SEQRES 9 E 361 ASN PHE LYS THR HIS LYS PRO ALA PRO GLU VAL ILE GLU
SEQRES 10 E 361 THR ALA ILE ASN CYS CYS THR SER ILE ILE PRO ASN ASP
SEQRES 11 E 361 ASP TYR PHE HIS VAL LYS ASP THR ASP PHE ASN SER VAL
SEQRES 12 E 361 TRP HIS ASP ILE TYR ARG ASP ILE ARG ALA SER ASP SER
SEQRES 13 E 361 ASN SER THR LYS ILE TYR PHE ASN ASN ILE GLU ILE PRO
SEQRES 14 E 361 LEU LYS LEU ILE ALA ASP LEU ILE ASN GLU LEU GLY ILE
SEQRES 15 E 361 ASN GLU PHE ILE ASP SER LYS LYS GLU LEU GLN MET LEU
SEQRES 16 E 361 SER TYR ASN GLN VAL ASN LYS ILE ILE ASN SER ASN PHE
SEQRES 17 E 361 PRO GLN GLN ASP LEU CYS PHE GLN THR GLU LYS LEU LEU
SEQRES 18 E 361 PHE THR SER LEU PHE GLN ASP PRO ALA PHE ILE SER ALA
SEQRES 19 E 361 LEU THR SER ALA PHE TRP GLN SER LEU HIS ILE THR SER
SEQRES 20 E 361 SER SER VAL GLU HIS ILE TYR ALA GLN ILE MET SER GLU
SEQRES 21 E 361 ASN ILE GLU ASN ARG LEU ASN PHE MET PRO GLU GLN ARG
SEQRES 22 E 361 VAL ILE ASN ASN CYS GLY HIS ILE ILE LYS ILE ASN ALA
SEQRES 23 E 361 VAL VAL PRO LYS ASN ASP THR ALA ILE SER ALA SER GLY
SEQRES 24 E 361 GLY ARG ALA TYR GLU VAL SER SER SER ILE LEU PRO SER
SEQRES 25 E 361 HIS ILE THR CYS ASN GLY VAL GLY ILE ASN LYS ILE GLU
SEQRES 26 E 361 THR SER TYR LEU VAL HIS ALA GLY THR LEU PRO SER SER
SEQRES 27 E 361 GLU GLY LEU ARG ASN ALA ILE PRO PRO GLU SER ARG GLN
SEQRES 28 E 361 VAL SER PHE ALA ILE ILE SER PRO ASP VAL
SEQRES 1 F 171 PRO GLU TYR ASP ALA LEU PHE LYS LEU LEU LEU ILE GLY
SEQRES 2 F 171 ASP SER GLY VAL GLY LYS SER CYS LEU LEU LEU ARG PHE
SEQRES 3 F 171 ALA ASP ASP THR TYR THR GLU SER TYR ILE SER THR ILE
SEQRES 4 F 171 GLY VAL ASP PHE LYS ILE ARG THR ILE GLU LEU ASP GLY
SEQRES 5 F 171 LYS THR ILE LYS LEU GLN ILE TRP ASP THR ALA GLY GLN
SEQRES 6 F 171 GLU ARG PHE ARG THR ILE THR SER SER TYR TYR ARG GLY
SEQRES 7 F 171 ALA HIS GLY ILE ILE VAL VAL TYR ASP VAL THR ASP GLN
SEQRES 8 F 171 GLU SER PHE ASN ASN VAL LYS GLN TRP LEU GLN GLU ILE
SEQRES 9 F 171 ASP ARG TYR ALA SER GLU ASN VAL ASN LYS LEU LEU VAL
SEQRES 10 F 171 GLY ASN LYS CYS ASP LEU THR THR LYS LYS VAL VAL ASP
SEQRES 11 F 171 TYR THR THR ALA LYS GLU PHE ALA ASP SER LEU GLY ILE
SEQRES 12 F 171 PRO PHE LEU GLU THR SER ALA LYS ASN ALA THR ASN VAL
SEQRES 13 F 171 GLU GLN SER PHE MET THR MET ALA ALA GLU ILE LYS LYS
SEQRES 14 F 171 ARG MET
HET AF3 B 201 4
HET GDP B 202 28
HET MG B 203 1
HET AF3 D 201 4
HET GDP D 202 28
HET MG D 203 1
HET AF3 F 201 4
HET GDP F 202 28
HET MG F 203 1
HETNAM AF3 ALUMINUM FLUORIDE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 7 AF3 3(AL F3)
FORMUL 8 GDP 3(C10 H15 N5 O11 P2)
FORMUL 9 MG 3(MG 2+)
FORMUL 16 HOH *9(H2 O)
HELIX 1 1 SER A 47 HIS A 56 1 10
HELIX 2 2 SER A 57 SER A 64 1 8
HELIX 3 3 SER A 113 SER A 123 1 11
HELIX 4 4 ALA A 151 CYS A 161 1 11
HELIX 5 5 SER A 181 ALA A 192 1 12
HELIX 6 6 SER A 193 ASN A 196 5 4
HELIX 7 7 PRO A 208 LEU A 219 1 12
HELIX 8 8 SER A 235 PHE A 247 1 13
HELIX 9 9 PHE A 254 PHE A 265 1 12
HELIX 10 10 ASP A 267 ALA A 277 1 11
HELIX 11 11 SER A 286 MET A 308 1 23
HELIX 12 12 SER A 376 ILE A 384 1 9
HELIX 13 13 PRO A 385 ARG A 389 5 5
HELIX 14 14 GLY B 23 ASP B 33 1 11
HELIX 15 15 GLN B 70 ARG B 72 5 3
HELIX 16 16 PHE B 73 SER B 79 1 7
HELIX 17 17 ASP B 95 ASN B 101 1 7
HELIX 18 18 ASN B 101 ALA B 113 1 13
HELIX 19 19 ASP B 135 SER B 145 1 11
HELIX 20 20 ASN B 160 LYS B 174 1 15
HELIX 21 21 SER C 47 HIS C 56 1 10
HELIX 22 22 SER C 57 SER C 64 1 8
HELIX 23 23 SER C 113 SER C 123 1 11
HELIX 24 24 ALA C 151 CYS C 161 1 11
HELIX 25 25 SER C 181 ALA C 192 1 12
HELIX 26 26 SER C 193 ASN C 196 5 4
HELIX 27 27 PRO C 208 LEU C 219 1 12
HELIX 28 28 SER C 235 PHE C 247 1 13
HELIX 29 29 PHE C 254 PHE C 265 1 12
HELIX 30 30 ASP C 267 ALA C 277 1 11
HELIX 31 31 SER C 286 MET C 308 1 23
HELIX 32 32 SER C 376 ILE C 384 1 9
HELIX 33 33 PRO C 385 ARG C 389 5 5
HELIX 34 34 GLY D 23 ASP D 33 1 11
HELIX 35 35 GLN D 70 ARG D 72 5 3
HELIX 36 36 PHE D 73 SER D 79 1 7
HELIX 37 37 ASP D 95 ASN D 101 1 7
HELIX 38 38 ASN D 101 ALA D 113 1 13
HELIX 39 39 ASP D 135 SER D 145 1 11
HELIX 40 40 ASN D 160 LYS D 174 1 15
HELIX 41 41 SER E 47 HIS E 56 1 10
HELIX 42 42 SER E 57 SER E 64 1 8
HELIX 43 43 SER E 113 SER E 123 1 11
HELIX 44 44 ALA E 151 CYS E 161 1 11
HELIX 45 45 SER E 181 ALA E 192 1 12
HELIX 46 46 SER E 193 ASN E 196 5 4
HELIX 47 47 PRO E 208 LEU E 219 1 12
HELIX 48 48 SER E 235 PHE E 247 1 13
HELIX 49 49 PHE E 254 PHE E 265 1 12
HELIX 50 50 ASP E 267 ALA E 277 1 11
HELIX 51 51 SER E 286 MET E 308 1 23
HELIX 52 52 SER E 376 ILE E 384 1 9
HELIX 53 53 PRO E 385 ARG E 389 5 5
HELIX 54 54 GLY F 23 ASP F 33 1 11
HELIX 55 55 GLN F 70 ARG F 72 5 3
HELIX 56 56 PHE F 73 SER F 79 1 7
HELIX 57 57 ASP F 95 ASN F 101 1 7
HELIX 58 58 ASN F 101 ALA F 113 1 13
HELIX 59 59 ASP F 135 SER F 145 1 11
HELIX 60 60 ASN F 160 LYS F 174 1 15
SHEET 1 A 5 SER A 66 PRO A 67 0
SHEET 2 A 5 GLU A 77 ILE A 83 -1 O HIS A 80 N SER A 66
SHEET 3 A 5 ILE A 86 ASN A 93 -1 O LEU A 90 N ALA A 79
SHEET 4 A 5 ILE A 96 ASP A 103 -1 O PHE A 100 N ARG A 89
SHEET 5 A 5 LYS A 106 GLN A 111 -1 O THR A 110 N VAL A 99
SHEET 1 B 4 GLN A 128 PHE A 129 0
SHEET 2 B 4 THR A 163 ILE A 165 1 O THR A 163 N PHE A 129
SHEET 3 B 4 GLN A 390 ASP A 399 -1 O PHE A 393 N SER A 164
SHEET 4 B 4 THR A 136 SER A 142 1 N ALA A 139 O SER A 397
SHEET 1 C 7 GLN A 128 PHE A 129 0
SHEET 2 C 7 THR A 163 ILE A 165 1 O THR A 163 N PHE A 129
SHEET 3 C 7 GLN A 390 ASP A 399 -1 O PHE A 393 N SER A 164
SHEET 4 C 7 VAL A 358 VAL A 369 -1 N ILE A 360 O ILE A 396
SHEET 5 C 7 TYR A 342 ILE A 353 -1 N TYR A 342 O VAL A 369
SHEET 6 C 7 ASN A 316 ALA A 325 -1 N ASN A 324 O GLU A 343
SHEET 7 C 7 LYS A 199 PHE A 202 1 N TYR A 201 O ILE A 323
SHEET 1 D 6 ASP B 47 ILE B 53 0
SHEET 2 D 6 ILE B 60 ASP B 66 -1 O ASP B 66 N ASP B 47
SHEET 3 D 6 ALA B 10 ILE B 17 1 N ALA B 10 O LYS B 61
SHEET 4 D 6 GLY B 86 ASP B 92 1 O ILE B 88 N LEU B 15
SHEET 5 D 6 ASN B 118 ASN B 124 1 O ASN B 124 N TYR B 91
SHEET 6 D 6 PHE B 150 THR B 153 1 O LEU B 151 N GLY B 123
SHEET 1 E 5 PHE C 65 PRO C 67 0
SHEET 2 E 5 GLU C 77 ILE C 83 -1 O HIS C 80 N SER C 66
SHEET 3 E 5 ILE C 86 ASN C 93 -1 O LEU C 90 N PHE C 78
SHEET 4 E 5 ILE C 96 ASP C 103 -1 O PHE C 100 N ARG C 89
SHEET 5 E 5 LYS C 106 GLN C 111 -1 O THR C 110 N VAL C 99
SHEET 1 F 4 GLN C 128 PHE C 129 0
SHEET 2 F 4 THR C 163 ILE C 165 1 O THR C 163 N PHE C 129
SHEET 3 F 4 GLN C 390 ASP C 399 -1 O PHE C 393 N SER C 164
SHEET 4 F 4 THR C 136 SER C 142 1 N ALA C 139 O SER C 397
SHEET 1 G 7 GLN C 128 PHE C 129 0
SHEET 2 G 7 THR C 163 ILE C 165 1 O THR C 163 N PHE C 129
SHEET 3 G 7 GLN C 390 ASP C 399 -1 O PHE C 393 N SER C 164
SHEET 4 G 7 VAL C 358 VAL C 369 -1 N ILE C 360 O ILE C 396
SHEET 5 G 7 TYR C 342 ILE C 353 -1 N HIS C 352 O GLY C 359
SHEET 6 G 7 ASN C 316 ALA C 325 -1 N ASN C 324 O GLU C 343
SHEET 7 G 7 LYS C 199 PHE C 202 1 N TYR C 201 O ILE C 323
SHEET 1 H 6 ASP D 47 ILE D 53 0
SHEET 2 H 6 ILE D 60 ASP D 66 -1 O ASP D 66 N ASP D 47
SHEET 3 H 6 ALA D 10 ILE D 17 1 N ALA D 10 O LYS D 61
SHEET 4 H 6 GLY D 86 ASP D 92 1 O VAL D 90 N ILE D 17
SHEET 5 H 6 ASN D 118 ASN D 124 1 O ASN D 124 N TYR D 91
SHEET 6 H 6 PHE D 150 THR D 153 1 O LEU D 151 N GLY D 123
SHEET 1 I 5 PHE E 65 PRO E 67 0
SHEET 2 I 5 GLU E 77 ILE E 83 -1 O HIS E 80 N SER E 66
SHEET 3 I 5 ILE E 86 ASN E 93 -1 O LEU E 90 N PHE E 78
SHEET 4 I 5 ILE E 96 ASP E 103 -1 O PHE E 100 N ARG E 89
SHEET 5 I 5 LYS E 106 GLN E 111 -1 O THR E 110 N VAL E 99
SHEET 1 J 4 GLN E 128 PHE E 129 0
SHEET 2 J 4 THR E 163 ILE E 165 1 O THR E 163 N PHE E 129
SHEET 3 J 4 GLN E 390 ASP E 399 -1 O PHE E 393 N SER E 164
SHEET 4 J 4 THR E 136 SER E 142 1 N ALA E 139 O SER E 397
SHEET 1 K 7 GLN E 128 PHE E 129 0
SHEET 2 K 7 THR E 163 ILE E 165 1 O THR E 163 N PHE E 129
SHEET 3 K 7 GLN E 390 ASP E 399 -1 O PHE E 393 N SER E 164
SHEET 4 K 7 VAL E 358 VAL E 369 -1 N ILE E 360 O ILE E 396
SHEET 5 K 7 TYR E 342 ILE E 353 -1 N TYR E 342 O VAL E 369
SHEET 6 K 7 ASN E 316 ALA E 325 -1 N ASN E 324 O GLU E 343
SHEET 7 K 7 LYS E 199 PHE E 202 1 N TYR E 201 O ILE E 323
SHEET 1 L 6 ASP F 47 ILE F 53 0
SHEET 2 L 6 ILE F 60 ASP F 66 -1 O ASP F 66 N ASP F 47
SHEET 3 L 6 ALA F 10 ILE F 17 1 N ALA F 10 O LYS F 61
SHEET 4 L 6 GLY F 86 ASP F 92 1 O VAL F 90 N ILE F 17
SHEET 5 L 6 ASN F 118 ASN F 124 1 O ASN F 124 N TYR F 91
SHEET 6 L 6 PHE F 150 THR F 153 1 O LEU F 151 N GLY F 123
SSBOND 1 CYS A 253 CYS E 355 1555 1555 2.02
SSBOND 2 CYS A 355 CYS C 253 1555 1555 2.00
SSBOND 3 CYS C 355 CYS E 253 1555 1555 2.05
LINK MG MG B 203 O HOH B 303 1555 1555 1.75
LINK MG MG D 203 O HOH D 302 1555 1555 1.92
LINK MG MG F 203 O HOH F 302 1555 1555 1.99
LINK MG MG D 203 O HOH D 301 1555 1555 2.01
LINK MG MG F 203 O HOH F 301 1555 1555 2.02
LINK MG MG B 203 O HOH B 302 1555 1555 2.10
LINK OG SER B 25 MG MG B 203 1555 1555 2.18
LINK OG SER D 25 MG MG D 203 1555 1555 2.22
LINK OG SER F 25 MG MG F 203 1555 1555 2.24
LINK O3B GDP B 202 MG MG B 203 1555 1555 2.27
LINK OG1 THR F 43 MG MG F 203 1555 1555 2.42
LINK OG1 THR D 43 MG MG D 203 1555 1555 2.44
LINK OG1 THR B 43 MG MG B 203 1555 1555 2.46
LINK O3B GDP D 202 MG MG D 203 1555 1555 2.52
LINK O3B GDP F 202 MG MG F 203 1555 1555 2.84
LINK O1B GDP F 202 MG MG F 203 1555 1555 2.98
LINK AL AF3 B 201 O1B GDP B 202 1555 1555 1.93
LINK AL AF3 F 201 O1B GDP F 202 1555 1555 1.95
LINK AL AF3 D 201 O1B GDP D 202 1555 1555 1.96
LINK AL AF3 F 201 O HOH E 501 1555 1555 2.07
LINK AL AF3 B 201 O HOH B 301 1555 1555 2.08
LINK AL AF3 D 201 O HOH C 501 1555 1555 2.08
CISPEP 1 GLY A 40 PRO A 41 0 -0.21
CISPEP 2 GLY C 40 PRO C 41 0 -0.04
CISPEP 3 GLY E 40 PRO E 41 0 -0.07
SITE 1 AC1 13 ARG A 188 GLN A 280 SER B 20 GLY B 21
SITE 2 AC1 13 LYS B 24 SER B 42 THR B 43 THR B 67
SITE 3 AC1 13 GLY B 69 GDP B 202 MG B 203 HOH B 301
SITE 4 AC1 13 HOH B 303
SITE 1 AC2 21 ARG A 188 ARG A 191 ASP B 19 GLY B 21
SITE 2 AC2 21 VAL B 22 GLY B 23 LYS B 24 SER B 25
SITE 3 AC2 21 CYS B 26 TYR B 36 ASN B 124 LYS B 125
SITE 4 AC2 21 ASP B 127 LEU B 128 SER B 154 ALA B 155
SITE 5 AC2 21 LYS B 156 AF3 B 201 MG B 203 HOH B 302
SITE 6 AC2 21 HOH B 303
SITE 1 AC3 6 SER B 25 THR B 43 AF3 B 201 GDP B 202
SITE 2 AC3 6 HOH B 302 HOH B 303
SITE 1 AC4 13 ARG C 188 GLN C 280 HOH C 501 SER D 20
SITE 2 AC4 13 GLY D 21 LYS D 24 SER D 42 THR D 43
SITE 3 AC4 13 THR D 67 GLY D 69 GDP D 202 MG D 203
SITE 4 AC4 13 HOH D 302
SITE 1 AC5 20 ARG C 188 ARG C 191 ASP D 19 GLY D 21
SITE 2 AC5 20 VAL D 22 GLY D 23 LYS D 24 SER D 25
SITE 3 AC5 20 CYS D 26 TYR D 36 ASN D 124 LYS D 125
SITE 4 AC5 20 ASP D 127 LEU D 128 SER D 154 ALA D 155
SITE 5 AC5 20 LYS D 156 AF3 D 201 MG D 203 HOH D 302
SITE 1 AC6 6 SER D 25 THR D 43 AF3 D 201 GDP D 202
SITE 2 AC6 6 HOH D 301 HOH D 302
SITE 1 AC7 11 ARG E 188 GLN E 280 HOH E 501 SER F 20
SITE 2 AC7 11 GLY F 21 LYS F 24 THR F 43 THR F 67
SITE 3 AC7 11 GLY F 69 GDP F 202 MG F 203
SITE 1 AC8 20 ARG E 188 ARG E 191 ASP F 19 GLY F 21
SITE 2 AC8 20 VAL F 22 GLY F 23 LYS F 24 SER F 25
SITE 3 AC8 20 CYS F 26 TYR F 36 ASN F 124 LYS F 125
SITE 4 AC8 20 ASP F 127 LEU F 128 SER F 154 ALA F 155
SITE 5 AC8 20 LYS F 156 AF3 F 201 MG F 203 HOH F 302
SITE 1 AC9 6 SER F 25 THR F 43 AF3 F 201 GDP F 202
SITE 2 AC9 6 HOH F 301 HOH F 302
CRYST1 186.118 127.311 107.325 90.00 94.45 90.00 C 1 2 1 12
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 0.005373 0.000000 0.000418 0.00000
SCALE2 0.000000 0.007855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END