HEADER GTP BINDING PROTEIN 21-DEC-07 3BRW
TITLE STRUCTURE OF THE RAP-RAPGAP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAP1 GTPASE-ACTIVATING PROTEIN 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RAP1GAP, UNP RESIDUES 75-415;
COMPND 5 SYNONYM: RAP1GAP1, RAP1GAP;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RAS-RELATED PROTEIN RAP-1B;
COMPND 10 CHAIN: D;
COMPND 11 FRAGMENT: UNP RESIDUES 1-167;
COMPND 12 SYNONYM: GTP-BINDING PROTEIN SMG P21B;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RAP1GAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RAP1B;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTAC
KEYWDS GAP, G PROTEINS, GTPASE, RAP, GTPASE ACTIVATION, GTP-BINDING, GTP
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCRIMA,C.THOMAS,D.DEACONESCU,A.WITTINGHOFER
REVDAT 5 01-NOV-23 3BRW 1 REMARK
REVDAT 4 10-NOV-21 3BRW 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3BRW 1 VERSN
REVDAT 2 22-APR-08 3BRW 1 JRNL
REVDAT 1 11-MAR-08 3BRW 0
JRNL AUTH A.SCRIMA,C.THOMAS,D.DEACONESCU,A.WITTINGHOFER
JRNL TITL THE RAP-RAPGAP COMPLEX: GTP HYDROLYSIS WITHOUT CATALYTIC
JRNL TITL 2 GLUTAMINE AND ARGININE RESIDUES
JRNL REF EMBO J. V. 27 1145 2008
JRNL REFN ISSN 0261-4189
JRNL PMID 18309292
JRNL DOI 10.1038/EMBOJ.2008.30
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 35759
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1878
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2637
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9422
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.21000
REMARK 3 B22 (A**2) : 4.21000
REMARK 3 B33 (A**2) : -6.31000
REMARK 3 B12 (A**2) : 2.10000
REMARK 3 B13 (A**2) : 0.00000
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): 0.500
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.419
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.796
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9678 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13094 ; 1.128 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1167 ; 6.007 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 482 ;37.009 ;24.232
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1655 ;19.627 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;16.589 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1432 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7398 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4102 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6475 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 222 ; 0.150 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.043 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 46 ; 0.181 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.083 ; 0.200
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): 5961 ; 0.439 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9442 ; 0.798 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4107 ; 0.485 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3652 ; 0.840 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS; MOLECULES B AND D, REPRESENTING THE RAP1GAP-RAP1B
REMARK 3 COMPLEX, ARE WELL DEFINED WITH AVERAGE B-FACTORS OF 82 AND 76.
REMARK 3 RAP1GAP MOLECULES A AND C ARE PARTIALLY HIGHLY FLEXIBLE AND ILL
REMARK 3 DEFINED RESULTING IN B-FACTORS OF 100 AND 120, RESPECTIVELY.
REMARK 4
REMARK 4 3BRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37639
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 182.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1SRQ FOR RAP1GAP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-11% PEG 2000 MME, 100MM MES PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.07233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 72.14467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 72.14467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.07233
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 75
REMARK 465 GLY A 412
REMARK 465 GLY A 413
REMARK 465 ASP A 414
REMARK 465 GLU A 415
REMARK 465 PRO B 75
REMARK 465 THR B 76
REMARK 465 THR B 77
REMARK 465 GLU B 415
REMARK 465 PRO C 75
REMARK 465 THR C 76
REMARK 465 THR C 77
REMARK 465 GLY C 326
REMARK 465 PRO C 327
REMARK 465 ASP C 328
REMARK 465 GLY C 329
REMARK 465 ASP C 414
REMARK 465 GLU C 415
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 THR A 76 OG1 CG2
REMARK 470 LEU A 411 CG CD1 CD2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LYS C 78 CG CD CE NZ
REMARK 470 LEU C 411 CG CD1 CD2
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 BE BEF D 170 O3B GDP D 171 1.84
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 PRO C 151 C - N - CD ANGL. DEV. = -14.3 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 LYS A 78 143.69 71.81
REMARK 500 GLU A 82 44.16 -79.10
REMARK 500 LYS A 134 7.06 -54.34
REMARK 500 CYS A 135 -49.66 -153.19
REMARK 500 SER A 145 -144.63 -82.19
REMARK 500 CYS A 146 43.28 -86.47
REMARK 500 LEU A 147 1.98 -57.88
REMARK 500 THR A 148 -47.02 51.67
REMARK 500 LEU A 202 -88.17 42.29
REMARK 500 THR A 205 -45.30 -140.96
REMARK 500 GLU A 215 123.88 64.59
REMARK 500 ASP A 235 60.75 -151.54
REMARK 500 VAL A 245 -60.90 -91.87
REMARK 500 PHE A 259 -84.57 -88.59
REMARK 500 ARG A 260 -127.93 -88.33
REMARK 500 ASN A 301 53.60 -91.59
REMARK 500 ASP A 340 28.62 -61.04
REMARK 500 ARG A 356 -177.08 -65.20
REMARK 500 SER A 407 25.46 -73.78
REMARK 500 MET A 409 -27.49 -145.31
REMARK 500 VAL B 79 -22.52 -140.13
REMARK 500 LYS B 80 135.37 70.11
REMARK 500 GLU B 82 49.82 -107.59
REMARK 500 ASP B 123 32.34 -157.69
REMARK 500 LYS B 134 0.38 -66.73
REMARK 500 CYS B 135 -37.80 -144.02
REMARK 500 ARG B 136 -147.64 -109.96
REMARK 500 THR B 137 106.99 179.30
REMARK 500 CYS B 146 9.70 56.66
REMARK 500 THR B 148 -36.24 65.18
REMARK 500 GLU B 149 89.59 -62.55
REMARK 500 LEU B 202 -107.32 37.01
REMARK 500 ASP B 235 14.22 50.15
REMARK 500 PHE B 239 109.58 -58.98
REMARK 500 ARG B 260 -115.78 49.04
REMARK 500 PRO B 273 136.77 -34.17
REMARK 500 GLN B 281 72.98 44.16
REMARK 500 GLU B 300 -134.77 -86.25
REMARK 500 ASN B 301 59.75 -164.65
REMARK 500 PRO B 306 -39.99 -35.94
REMARK 500 PRO B 327 29.90 -75.45
REMARK 500 SER B 407 6.74 -59.67
REMARK 500 VAL C 79 114.47 171.58
REMARK 500 GLU C 98 106.15 -56.03
REMARK 500 LEU C 127 105.71 -162.70
REMARK 500 LEU C 130 93.71 -163.23
REMARK 500 CYS C 135 -66.67 -91.58
REMARK 500 ARG C 136 -166.22 -117.82
REMARK 500 SER C 145 -111.72 -84.93
REMARK 500 LEU C 147 21.84 -76.11
REMARK 500
REMARK 500 THIS ENTRY HAS 81 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 THR C 148 GLU C 149 -64.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF D 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 171
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SRQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RAP1GAP CATALYTIC DOMAIN
DBREF 3BRW A 75 415 UNP P47736 RPGP1_HUMAN 75 415
DBREF 3BRW B 75 415 UNP P47736 RPGP1_HUMAN 75 415
DBREF 3BRW C 75 415 UNP P47736 RPGP1_HUMAN 75 415
DBREF 3BRW D 1 167 UNP P61224 RAP1B_HUMAN 1 167
SEQADV 3BRW ALA A 204 UNP P47736 GLN 204 ENGINEERED MUTATION
SEQADV 3BRW ALA B 204 UNP P47736 GLN 204 ENGINEERED MUTATION
SEQADV 3BRW ALA C 204 UNP P47736 GLN 204 ENGINEERED MUTATION
SEQRES 1 A 341 PRO THR THR LYS VAL LYS LEU GLU CYS ASN PRO THR ALA
SEQRES 2 A 341 ARG ILE TYR ARG LYS HIS PHE LEU GLY LYS GLU HIS PHE
SEQRES 3 A 341 ASN TYR TYR SER LEU ASP THR ALA LEU GLY HIS LEU VAL
SEQRES 4 A 341 PHE SER LEU LYS TYR ASP VAL ILE GLY ASP GLN GLU HIS
SEQRES 5 A 341 LEU ARG LEU LEU LEU ARG THR LYS CYS ARG THR TYR HIS
SEQRES 6 A 341 ASP VAL ILE PRO ILE SER CYS LEU THR GLU PHE PRO ASN
SEQRES 7 A 341 VAL VAL GLN MET ALA LYS LEU VAL CYS GLU ASP VAL ASN
SEQRES 8 A 341 VAL ASP ARG PHE TYR PRO VAL LEU TYR PRO LYS ALA SER
SEQRES 9 A 341 ARG LEU ILE VAL THR PHE ASP GLU HIS VAL ILE SER ASN
SEQRES 10 A 341 ASN PHE LYS PHE GLY VAL ILE TYR GLN LYS LEU GLY ALA
SEQRES 11 A 341 THR SER GLU GLU GLU LEU PHE SER THR ASN GLU GLU SER
SEQRES 12 A 341 PRO ALA PHE VAL GLU PHE LEU GLU PHE LEU GLY GLN LYS
SEQRES 13 A 341 VAL LYS LEU GLN ASP PHE LYS GLY PHE ARG GLY GLY LEU
SEQRES 14 A 341 ASP VAL THR HIS GLY GLN THR GLY THR GLU SER VAL TYR
SEQRES 15 A 341 CYS ASN PHE ARG ASN LYS GLU ILE MET PHE HIS VAL SER
SEQRES 16 A 341 THR LYS LEU PRO TYR THR GLU GLY ASP ALA GLN GLN LEU
SEQRES 17 A 341 GLN ARG LYS ARG HIS ILE GLY ASN ASP ILE VAL ALA VAL
SEQRES 18 A 341 VAL PHE GLN ASP GLU ASN THR PRO PHE VAL PRO ASP MET
SEQRES 19 A 341 ILE ALA SER ASN PHE LEU HIS ALA TYR VAL VAL VAL GLN
SEQRES 20 A 341 ALA GLU GLY GLY GLY PRO ASP GLY PRO LEU TYR LYS VAL
SEQRES 21 A 341 SER VAL THR ALA ARG ASP ASP VAL PRO PHE PHE GLY PRO
SEQRES 22 A 341 PRO LEU PRO ASP PRO ALA VAL PHE ARG LYS GLY PRO GLU
SEQRES 23 A 341 PHE GLN GLU PHE LEU LEU THR LYS LEU ILE ASN ALA GLU
SEQRES 24 A 341 TYR ALA CYS TYR LYS ALA GLU LYS PHE ALA LYS LEU GLU
SEQRES 25 A 341 GLU ARG THR ARG ALA ALA LEU LEU GLU THR LEU TYR GLU
SEQRES 26 A 341 GLU LEU HIS ILE HIS SER GLN SER MET MET GLY LEU GLY
SEQRES 27 A 341 GLY ASP GLU
SEQRES 1 B 341 PRO THR THR LYS VAL LYS LEU GLU CYS ASN PRO THR ALA
SEQRES 2 B 341 ARG ILE TYR ARG LYS HIS PHE LEU GLY LYS GLU HIS PHE
SEQRES 3 B 341 ASN TYR TYR SER LEU ASP THR ALA LEU GLY HIS LEU VAL
SEQRES 4 B 341 PHE SER LEU LYS TYR ASP VAL ILE GLY ASP GLN GLU HIS
SEQRES 5 B 341 LEU ARG LEU LEU LEU ARG THR LYS CYS ARG THR TYR HIS
SEQRES 6 B 341 ASP VAL ILE PRO ILE SER CYS LEU THR GLU PHE PRO ASN
SEQRES 7 B 341 VAL VAL GLN MET ALA LYS LEU VAL CYS GLU ASP VAL ASN
SEQRES 8 B 341 VAL ASP ARG PHE TYR PRO VAL LEU TYR PRO LYS ALA SER
SEQRES 9 B 341 ARG LEU ILE VAL THR PHE ASP GLU HIS VAL ILE SER ASN
SEQRES 10 B 341 ASN PHE LYS PHE GLY VAL ILE TYR GLN LYS LEU GLY ALA
SEQRES 11 B 341 THR SER GLU GLU GLU LEU PHE SER THR ASN GLU GLU SER
SEQRES 12 B 341 PRO ALA PHE VAL GLU PHE LEU GLU PHE LEU GLY GLN LYS
SEQRES 13 B 341 VAL LYS LEU GLN ASP PHE LYS GLY PHE ARG GLY GLY LEU
SEQRES 14 B 341 ASP VAL THR HIS GLY GLN THR GLY THR GLU SER VAL TYR
SEQRES 15 B 341 CYS ASN PHE ARG ASN LYS GLU ILE MET PHE HIS VAL SER
SEQRES 16 B 341 THR LYS LEU PRO TYR THR GLU GLY ASP ALA GLN GLN LEU
SEQRES 17 B 341 GLN ARG LYS ARG HIS ILE GLY ASN ASP ILE VAL ALA VAL
SEQRES 18 B 341 VAL PHE GLN ASP GLU ASN THR PRO PHE VAL PRO ASP MET
SEQRES 19 B 341 ILE ALA SER ASN PHE LEU HIS ALA TYR VAL VAL VAL GLN
SEQRES 20 B 341 ALA GLU GLY GLY GLY PRO ASP GLY PRO LEU TYR LYS VAL
SEQRES 21 B 341 SER VAL THR ALA ARG ASP ASP VAL PRO PHE PHE GLY PRO
SEQRES 22 B 341 PRO LEU PRO ASP PRO ALA VAL PHE ARG LYS GLY PRO GLU
SEQRES 23 B 341 PHE GLN GLU PHE LEU LEU THR LYS LEU ILE ASN ALA GLU
SEQRES 24 B 341 TYR ALA CYS TYR LYS ALA GLU LYS PHE ALA LYS LEU GLU
SEQRES 25 B 341 GLU ARG THR ARG ALA ALA LEU LEU GLU THR LEU TYR GLU
SEQRES 26 B 341 GLU LEU HIS ILE HIS SER GLN SER MET MET GLY LEU GLY
SEQRES 27 B 341 GLY ASP GLU
SEQRES 1 C 341 PRO THR THR LYS VAL LYS LEU GLU CYS ASN PRO THR ALA
SEQRES 2 C 341 ARG ILE TYR ARG LYS HIS PHE LEU GLY LYS GLU HIS PHE
SEQRES 3 C 341 ASN TYR TYR SER LEU ASP THR ALA LEU GLY HIS LEU VAL
SEQRES 4 C 341 PHE SER LEU LYS TYR ASP VAL ILE GLY ASP GLN GLU HIS
SEQRES 5 C 341 LEU ARG LEU LEU LEU ARG THR LYS CYS ARG THR TYR HIS
SEQRES 6 C 341 ASP VAL ILE PRO ILE SER CYS LEU THR GLU PHE PRO ASN
SEQRES 7 C 341 VAL VAL GLN MET ALA LYS LEU VAL CYS GLU ASP VAL ASN
SEQRES 8 C 341 VAL ASP ARG PHE TYR PRO VAL LEU TYR PRO LYS ALA SER
SEQRES 9 C 341 ARG LEU ILE VAL THR PHE ASP GLU HIS VAL ILE SER ASN
SEQRES 10 C 341 ASN PHE LYS PHE GLY VAL ILE TYR GLN LYS LEU GLY ALA
SEQRES 11 C 341 THR SER GLU GLU GLU LEU PHE SER THR ASN GLU GLU SER
SEQRES 12 C 341 PRO ALA PHE VAL GLU PHE LEU GLU PHE LEU GLY GLN LYS
SEQRES 13 C 341 VAL LYS LEU GLN ASP PHE LYS GLY PHE ARG GLY GLY LEU
SEQRES 14 C 341 ASP VAL THR HIS GLY GLN THR GLY THR GLU SER VAL TYR
SEQRES 15 C 341 CYS ASN PHE ARG ASN LYS GLU ILE MET PHE HIS VAL SER
SEQRES 16 C 341 THR LYS LEU PRO TYR THR GLU GLY ASP ALA GLN GLN LEU
SEQRES 17 C 341 GLN ARG LYS ARG HIS ILE GLY ASN ASP ILE VAL ALA VAL
SEQRES 18 C 341 VAL PHE GLN ASP GLU ASN THR PRO PHE VAL PRO ASP MET
SEQRES 19 C 341 ILE ALA SER ASN PHE LEU HIS ALA TYR VAL VAL VAL GLN
SEQRES 20 C 341 ALA GLU GLY GLY GLY PRO ASP GLY PRO LEU TYR LYS VAL
SEQRES 21 C 341 SER VAL THR ALA ARG ASP ASP VAL PRO PHE PHE GLY PRO
SEQRES 22 C 341 PRO LEU PRO ASP PRO ALA VAL PHE ARG LYS GLY PRO GLU
SEQRES 23 C 341 PHE GLN GLU PHE LEU LEU THR LYS LEU ILE ASN ALA GLU
SEQRES 24 C 341 TYR ALA CYS TYR LYS ALA GLU LYS PHE ALA LYS LEU GLU
SEQRES 25 C 341 GLU ARG THR ARG ALA ALA LEU LEU GLU THR LEU TYR GLU
SEQRES 26 C 341 GLU LEU HIS ILE HIS SER GLN SER MET MET GLY LEU GLY
SEQRES 27 C 341 GLY ASP GLU
SEQRES 1 D 167 MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY
SEQRES 2 D 167 VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY
SEQRES 3 D 167 ILE PHE VAL GLU LYS TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 D 167 TYR ARG LYS GLN VAL GLU VAL ASP ALA GLN GLN CYS MET
SEQRES 5 D 167 LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR
SEQRES 6 D 167 ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE
SEQRES 7 D 167 ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN
SEQRES 8 D 167 ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS
SEQRES 9 D 167 ASP THR ASP ASP VAL PRO MET ILE LEU VAL GLY ASN LYS
SEQRES 10 D 167 CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN
SEQRES 11 D 167 GLY GLN ASN LEU ALA ARG GLN TRP ASN ASN CYS ALA PHE
SEQRES 12 D 167 LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU
SEQRES 13 D 167 ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG
HET MG D 172 1
HET BEF D 170 4
HET GDP D 171 28
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 5 MG MG 2+
FORMUL 6 BEF BE F3 1-
FORMUL 7 GDP C10 H15 N5 O11 P2
FORMUL 8 HOH *10(H2 O)
HELIX 1 1 ARG A 88 PHE A 94 1 7
HELIX 2 2 ASN A 152 LEU A 159 1 8
HELIX 3 3 LYS A 176 GLU A 186 1 11
HELIX 4 4 GLU A 207 SER A 212 1 6
HELIX 5 5 SER A 217 GLY A 228 1 12
HELIX 6 6 GLN A 234 PHE A 236 5 3
HELIX 7 7 GLN A 281 GLY A 289 1 9
HELIX 8 8 GLY A 358 TYR A 377 1 20
HELIX 9 9 ALA A 379 SER A 407 1 29
HELIX 10 10 ASN B 84 ALA B 87 5 4
HELIX 11 11 ARG B 88 PHE B 94 1 7
HELIX 12 12 ASN B 152 CYS B 161 1 10
HELIX 13 13 LYS B 176 GLU B 186 1 11
HELIX 14 14 SER B 206 SER B 212 1 7
HELIX 15 15 ALA B 219 GLY B 228 1 10
HELIX 16 16 GLN B 281 GLY B 289 1 9
HELIX 17 17 VAL B 305 ILE B 309 5 5
HELIX 18 18 GLY B 358 LYS B 378 1 21
HELIX 19 19 ALA B 379 SER B 407 1 29
HELIX 20 20 ARG C 88 PHE C 94 1 7
HELIX 21 21 ASN C 152 CYS C 161 1 10
HELIX 22 22 LYS C 176 GLU C 186 1 11
HELIX 23 23 THR C 270 LEU C 272 5 3
HELIX 24 24 HIS C 287 ASP C 291 5 5
HELIX 25 25 PRO C 359 TYR C 377 1 19
HELIX 26 26 ALA C 379 GLY C 410 1 32
HELIX 27 27 GLY D 15 GLY D 26 1 12
HELIX 28 28 PHE D 64 GLY D 75 1 12
HELIX 29 29 GLN D 87 ASP D 92 1 6
HELIX 30 30 LEU D 93 ASP D 105 1 13
HELIX 31 31 LEU D 120 ARG D 124 5 5
HELIX 32 32 GLY D 127 TRP D 138 1 12
HELIX 33 33 ASN D 155 ARG D 167 1 13
SHEET 1 A 5 THR A 137 PRO A 143 0
SHEET 2 A 5 GLN A 124 ARG A 132 -1 N LEU A 131 O TYR A 138
SHEET 3 A 5 GLY A 110 ILE A 121 -1 N SER A 115 O LEU A 130
SHEET 4 A 5 PHE A 100 ASP A 106 -1 N TYR A 102 O PHE A 114
SHEET 5 A 5 TYR A 170 PRO A 171 -1 O TYR A 170 N TYR A 103
SHEET 1 B 7 GLN A 229 LYS A 232 0
SHEET 2 B 7 GLU A 253 ASN A 258 -1 O TYR A 256 N GLN A 229
SHEET 3 B 7 GLU A 263 VAL A 268 -1 O ILE A 264 N CYS A 257
SHEET 4 B 7 ASN A 192 GLN A 200 1 N PHE A 193 O MET A 265
SHEET 5 B 7 VAL A 293 GLN A 298 1 O VAL A 295 N GLY A 196
SHEET 6 B 7 ALA A 316 GLN A 321 1 O VAL A 320 N VAL A 296
SHEET 7 B 7 LYS A 333 THR A 337 -1 O SER A 335 N VAL A 319
SHEET 1 C 5 THR B 137 ASP B 140 0
SHEET 2 C 5 GLN B 124 ARG B 132 -1 N LEU B 129 O ASP B 140
SHEET 3 C 5 GLY B 110 ILE B 121 -1 N SER B 115 O LEU B 130
SHEET 4 C 5 PHE B 100 ASP B 106 -1 N TYR B 102 O PHE B 114
SHEET 5 C 5 TYR B 170 PRO B 171 -1 O TYR B 170 N TYR B 103
SHEET 1 D 8 GLN B 229 LYS B 232 0
SHEET 2 D 8 GLU B 253 CYS B 257 -1 O SER B 254 N VAL B 231
SHEET 3 D 8 GLU B 263 VAL B 268 -1 O ILE B 264 N CYS B 257
SHEET 4 D 8 ASN B 192 GLN B 200 1 N PHE B 195 O HIS B 267
SHEET 5 D 8 VAL B 293 GLN B 298 1 O VAL B 295 N GLY B 196
SHEET 6 D 8 ALA B 316 GLN B 321 1 O VAL B 320 N VAL B 296
SHEET 7 D 8 LEU B 331 ALA B 338 -1 O THR B 337 N TYR B 317
SHEET 8 D 8 VAL B 354 ARG B 356 -1 O PHE B 355 N TYR B 332
SHEET 1 E 5 THR C 137 VAL C 141 0
SHEET 2 E 5 GLN C 124 THR C 133 -1 N LEU C 129 O ASP C 140
SHEET 3 E 5 GLY C 110 ILE C 121 -1 N SER C 115 O LEU C 130
SHEET 4 E 5 HIS C 99 ASP C 106 -1 N TYR C 102 O PHE C 114
SHEET 5 E 5 TYR C 170 PRO C 171 -1 O TYR C 170 N TYR C 103
SHEET 1 F 6 GLN C 229 VAL C 231 0
SHEET 2 F 6 SER C 254 ASN C 258 -1 O TYR C 256 N GLN C 229
SHEET 3 F 6 GLU C 263 VAL C 268 -1 O PHE C 266 N VAL C 255
SHEET 4 F 6 ASN C 192 TYR C 199 1 N VAL C 197 O HIS C 267
SHEET 5 F 6 VAL C 293 PHE C 297 1 O VAL C 295 N GLY C 196
SHEET 6 F 6 ALA C 316 VAL C 320 1 O VAL C 318 N VAL C 296
SHEET 1 G 6 ASP D 38 GLU D 45 0
SHEET 2 G 6 GLN D 50 ASP D 57 -1 O ILE D 55 N TYR D 40
SHEET 3 G 6 ARG D 2 GLY D 10 1 N LEU D 6 O GLU D 54
SHEET 4 G 6 GLY D 77 SER D 83 1 O GLY D 77 N VAL D 7
SHEET 5 G 6 MET D 111 ASN D 116 1 O ILE D 112 N LEU D 80
SHEET 6 G 6 ALA D 142 GLU D 145 1 O ALA D 142 N LEU D 113
SITE 1 AC1 4 SER D 17 THR D 35 HOH D 174 HOH D 175
SITE 1 AC2 9 ASN B 290 GLY D 12 GLY D 13 LYS D 16
SITE 2 AC2 9 TYR D 32 PRO D 34 THR D 35 GLY D 60
SITE 3 AC2 9 HOH D 175
SITE 1 AC3 18 GLN B 280 GLY D 13 GLY D 15 LYS D 16
SITE 2 AC3 18 SER D 17 ALA D 18 GLU D 30 LYS D 31
SITE 3 AC3 18 TYR D 32 ASN D 116 LYS D 117 ASP D 119
SITE 4 AC3 18 LEU D 120 SER D 147 ALA D 148 LYS D 149
SITE 5 AC3 18 HOH D 174 HOH D 175
CRYST1 209.723 209.723 108.217 90.00 90.00 120.00 P 31 2 1 18
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 0.004768 0.002753 0.000000 0.00000
SCALE2 0.000000 0.005506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END