HEADER SIGNALING PROTEIN 31-MAR-06 2GJS
TITLE THE CRYSTAL STRUCTURE OF HUMAN RRAD IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN RAD;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RAS ASSOCIATED WITH DIABETES, RAD1;
COMPND 5 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: RRAD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS RRAD, GDP/GTP BINDING, GTP HYDROLYSIS, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.TURNBULL,X.YANG,M.SOUNDARARAJAN,G.SCHOCH,J.DEBRECZENI,J.M.ELKINS,
AUTHOR 2 C.GILEADI,G.BERRIDGE,N.PANTIC,N.BURGESS,C.E.A.SMEE,J.BRAY,F.VON
AUTHOR 3 DELFT,J.WEIGELT,A.EDWARDS,C.ARROWSMITH,M.SUNDSTROM,D.DOYLE,
AUTHOR 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 03-APR-24 2GJS 1 REMARK
REVDAT 4 14-FEB-24 2GJS 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2GJS 1 VERSN
REVDAT 2 24-FEB-09 2GJS 1 VERSN
REVDAT 1 11-APR-06 2GJS 0
JRNL AUTH A.P.TURNBULL,X.YANG,M.SOUNDARARAJAN,G.SCHOCH,J.DEBRECZENI,
JRNL AUTH 2 J.M.ELKINS,C.GILEADI,G.BERRIDGE,N.PANTIC,N.BURGESS,
JRNL AUTH 3 C.E.A.SMEE,J.BRAY,F.VON DELFT,J.WEIGELT,A.EDWARDS,
JRNL AUTH 4 C.ARROWSMITH,M.SUNDSTROM,D.DOYLE
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN RRAD IN COMPLEX WITH GDP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 23536
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1266
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1604
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2184
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 1.53000
REMARK 3 B33 (A**2) : -1.79000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.493
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2311 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1553 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3132 ; 1.605 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3755 ; 0.948 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 6.442 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;35.476 ;22.292
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;15.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;17.429 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 365 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2532 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 494 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 404 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1577 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1100 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1289 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 77 ; 0.185 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.324 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 24 ; 0.329 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.550 ; 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): 1471 ; 1.010 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 600 ; 0.235 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2287 ; 1.535 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 966 ; 2.280 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 840 ; 3.466 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 174
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7146 35.9884 20.9079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2273 T22: 0.0308
REMARK 3 T33: 0.1819 T12: -0.0151
REMARK 3 T13: -0.0446 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.5949 L22: 1.6641
REMARK 3 L33: 4.4193 L12: -0.2852
REMARK 3 L13: 1.2507 L23: -0.7024
REMARK 3 S TENSOR
REMARK 3 S11: -0.1706 S12: 0.0128 S13: 0.5299
REMARK 3 S21: 0.1414 S22: -0.1066 S23: -0.3213
REMARK 3 S31: -0.4423 S32: 0.4459 S33: 0.2772
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 175 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5696 28.2385 13.2821
REMARK 3 T TENSOR
REMARK 3 T11: 0.0192 T22: -0.1332
REMARK 3 T33: -0.1045 T12: 0.0477
REMARK 3 T13: 0.0221 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 2.3257 L22: 2.9081
REMARK 3 L33: 5.4739 L12: 0.1746
REMARK 3 L13: 0.7502 L23: -0.9441
REMARK 3 S TENSOR
REMARK 3 S11: -0.0572 S12: 0.3051 S13: 0.0843
REMARK 3 S21: -0.3074 S22: -0.0755 S23: -0.2209
REMARK 3 S31: 0.1382 S32: 0.4499 S33: 0.1327
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 91 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3462 28.3324 -14.7163
REMARK 3 T TENSOR
REMARK 3 T11: 0.0388 T22: 0.3235
REMARK 3 T33: 0.0791 T12: 0.0084
REMARK 3 T13: -0.0246 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 6.1784 L22: 2.4122
REMARK 3 L33: 5.2283 L12: -0.1250
REMARK 3 L13: 2.3274 L23: -0.2341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0568 S12: -0.1363 S13: 0.2098
REMARK 3 S21: -0.0615 S22: 0.0588 S23: 0.5728
REMARK 3 S31: -0.0939 S32: -1.3975 S33: -0.1156
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 173 B 256
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6705 24.2177 -7.3988
REMARK 3 T TENSOR
REMARK 3 T11: 0.0145 T22: -0.0181
REMARK 3 T33: -0.1015 T12: -0.0542
REMARK 3 T13: 0.0201 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 3.2351 L22: 2.9672
REMARK 3 L33: 5.8980 L12: -0.7631
REMARK 3 L13: -0.5758 L23: -0.7086
REMARK 3 S TENSOR
REMARK 3 S11: -0.1741 S12: -0.1992 S13: 0.0458
REMARK 3 S21: 0.3207 S22: 0.1512 S23: 0.1905
REMARK 3 S31: 0.2482 S32: -0.7122 S33: 0.0229
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2GJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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) : 0.95
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24816
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: PHASER
REMARK 200 STARTING MODEL: SWISSMODEL (FIRST APPROACH MODE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M SODIUM MALATE, 20% (W/V) PEG
REMARK 280 3350, PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 29.28000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 SER A 85
REMARK 465 MET A 86
REMARK 465 SER A 87
REMARK 465 ASP A 88
REMARK 465 GLU A 89
REMARK 465 SER A 90
REMARK 465 GLU A 115
REMARK 465 ASP A 116
REMARK 465 GLY A 117
REMARK 465 PRO A 118
REMARK 465 GLU A 119
REMARK 465 ALA A 120
REMARK 465 GLU A 121
REMARK 465 ALA A 122
REMARK 465 ALA A 123
REMARK 465 GLU A 147
REMARK 465 GLN A 148
REMARK 465 ASP A 149
REMARK 465 GLY A 150
REMARK 465 GLY A 151
REMARK 465 ARG A 152
REMARK 465 TRP A 153
REMARK 465 THR A 193
REMARK 465 ASP A 194
REMARK 465 GLU A 259
REMARK 465 ALA A 260
REMARK 465 SER B 85
REMARK 465 MET B 86
REMARK 465 SER B 87
REMARK 465 ASP B 88
REMARK 465 GLU B 89
REMARK 465 SER B 90
REMARK 465 ASP B 116
REMARK 465 GLY B 117
REMARK 465 PRO B 118
REMARK 465 GLU B 119
REMARK 465 ALA B 120
REMARK 465 GLU B 121
REMARK 465 ALA B 122
REMARK 465 ALA B 123
REMARK 465 GLY B 124
REMARK 465 TRP B 146
REMARK 465 GLU B 147
REMARK 465 GLN B 148
REMARK 465 ASP B 149
REMARK 465 GLY B 150
REMARK 465 GLY B 151
REMARK 465 ARG B 152
REMARK 465 TRP B 153
REMARK 465 LEU B 154
REMARK 465 PRO B 155
REMARK 465 GLY B 156
REMARK 465 HIS B 157
REMARK 465 CYS B 158
REMARK 465 MET B 159
REMARK 465 ALA B 160
REMARK 465 GLN B 192
REMARK 465 THR B 193
REMARK 465 ASP B 194
REMARK 465 SER B 257
REMARK 465 LYS B 258
REMARK 465 GLU B 259
REMARK 465 ALA B 260
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 GLU A 137 CD OE1 OE2
REMARK 470 ARG A 189 CZ NH1 NH2
REMARK 470 GLN A 192 CG CD OE1 NE2
REMARK 470 ARG A 254 CZ NH1 NH2
REMARK 470 LYS A 258 CE NZ
REMARK 470 LYS B 93 CG CD CE NZ
REMARK 470 ASP B 128 OD1 OD2
REMARK 470 SER B 130 OG
REMARK 470 VAL B 132 CB CG1 CG2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 SER B 139 OG
REMARK 470 LYS B 179 NZ
REMARK 470 ARG B 189 CD NE CZ NH1 NH2
REMARK 470 ARG B 191 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 195 CG OD1 OD2
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2
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 O HOH A 1186 O HOH A 1193 1.26
REMARK 500 MG MG A 1 O HOH A 1193 1.37
REMARK 500 O HOH A 1225 O HOH A 1226 2.16
REMARK 500 OG SER A 181 O HOH A 1220 2.17
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 ARG A 211 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH2 ANGL. DEV. = -5.7 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 ARG A 129 133.09 179.89
REMARK 500 ARG A 129 134.61 178.78
REMARK 500 LYS A 204 34.94 74.98
REMARK 500 LYS B 204 30.59 80.26
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 ALA A 160 MET A 161 -148.97
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 A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 105 OG
REMARK 620 2 GDP A1184 O2B 93.0
REMARK 620 3 HOH A1186 O 83.2 86.8
REMARK 620 4 HOH A1203 O 94.3 99.7 173.1
REMARK 620 5 HOH A1207 O 88.1 174.4 87.8 85.7
REMARK 620 6 HOH A1211 O 174.4 89.3 91.8 90.3 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 105 OG
REMARK 620 2 GDP B1184 O2B 87.1
REMARK 620 3 HOH B1203 O 80.3 100.4
REMARK 620 4 HOH B1204 O 93.8 88.5 169.0
REMARK 620 5 HOH B1205 O 88.1 174.5 76.3 94.3
REMARK 620 6 HOH B1214 O 172.9 97.2 93.4 91.9 87.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1184
DBREF 2GJS A 87 260 UNP P55042 RAD_HUMAN 85 260
DBREF 2GJS B 87 260 UNP P55042 RAD_HUMAN 85 260
SEQADV 2GJS SER A 85 UNP P55042 CLONING ARTIFACT
SEQADV 2GJS MET A 86 UNP P55042 CLONING ARTIFACT
SEQADV 2GJS SER B 85 UNP P55042 CLONING ARTIFACT
SEQADV 2GJS MET B 86 UNP P55042 CLONING ARTIFACT
SEQRES 1 A 176 SER MET SER ASP GLU SER VAL TYR LYS VAL LEU LEU LEU
SEQRES 2 A 176 GLY ALA PRO GLY VAL GLY LYS SER ALA LEU ALA ARG ILE
SEQRES 3 A 176 PHE GLY GLY VAL GLU ASP GLY PRO GLU ALA GLU ALA ALA
SEQRES 4 A 176 GLY HIS THR TYR ASP ARG SER ILE VAL VAL ASP GLY GLU
SEQRES 5 A 176 GLU ALA SER LEU MET VAL TYR ASP ILE TRP GLU GLN ASP
SEQRES 6 A 176 GLY GLY ARG TRP LEU PRO GLY HIS CYS MET ALA MET GLY
SEQRES 7 A 176 ASP ALA TYR VAL ILE VAL TYR SER VAL THR ASP LYS GLY
SEQRES 8 A 176 SER PHE GLU LYS ALA SER GLU LEU ARG VAL GLN LEU ARG
SEQRES 9 A 176 ARG ALA ARG GLN THR ASP ASP VAL PRO ILE ILE LEU VAL
SEQRES 10 A 176 GLY ASN LYS SER ASP LEU VAL ARG SER ARG GLU VAL SER
SEQRES 11 A 176 VAL ASP GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES 12 A 176 LYS PHE ILE GLU THR SER ALA ALA LEU HIS HIS ASN VAL
SEQRES 13 A 176 GLN ALA LEU PHE GLU GLY VAL VAL ARG GLN ILE ARG LEU
SEQRES 14 A 176 ARG ARG ASP SER LYS GLU ALA
SEQRES 1 B 176 SER MET SER ASP GLU SER VAL TYR LYS VAL LEU LEU LEU
SEQRES 2 B 176 GLY ALA PRO GLY VAL GLY LYS SER ALA LEU ALA ARG ILE
SEQRES 3 B 176 PHE GLY GLY VAL GLU ASP GLY PRO GLU ALA GLU ALA ALA
SEQRES 4 B 176 GLY HIS THR TYR ASP ARG SER ILE VAL VAL ASP GLY GLU
SEQRES 5 B 176 GLU ALA SER LEU MET VAL TYR ASP ILE TRP GLU GLN ASP
SEQRES 6 B 176 GLY GLY ARG TRP LEU PRO GLY HIS CYS MET ALA MET GLY
SEQRES 7 B 176 ASP ALA TYR VAL ILE VAL TYR SER VAL THR ASP LYS GLY
SEQRES 8 B 176 SER PHE GLU LYS ALA SER GLU LEU ARG VAL GLN LEU ARG
SEQRES 9 B 176 ARG ALA ARG GLN THR ASP ASP VAL PRO ILE ILE LEU VAL
SEQRES 10 B 176 GLY ASN LYS SER ASP LEU VAL ARG SER ARG GLU VAL SER
SEQRES 11 B 176 VAL ASP GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES 12 B 176 LYS PHE ILE GLU THR SER ALA ALA LEU HIS HIS ASN VAL
SEQRES 13 B 176 GLN ALA LEU PHE GLU GLY VAL VAL ARG GLN ILE ARG LEU
SEQRES 14 B 176 ARG ARG ASP SER LYS GLU ALA
HET MG A 1 1
HET GDP A1184 28
HET MG B 1 1
HET GDP B1184 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 GDP 2(C10 H15 N5 O11 P2)
FORMUL 7 HOH *80(H2 O)
HELIX 1 1 GLY A 103 GLY A 113 1 11
HELIX 2 2 LEU A 154 ALA A 160 1 7
HELIX 3 3 ASP A 173 ARG A 191 1 19
HELIX 4 4 LEU A 207 ARG A 211 5 5
HELIX 5 5 SER A 214 ASP A 226 1 13
HELIX 6 6 ASN A 239 LYS A 258 1 20
HELIX 7 7 GLY B 103 GLY B 113 1 11
HELIX 8 8 ASP B 173 ARG B 191 1 19
HELIX 9 9 LEU B 207 ARG B 211 5 5
HELIX 10 10 SER B 214 ASP B 226 1 13
HELIX 11 11 ASN B 239 ASP B 256 1 18
SHEET 1 A 6 HIS A 125 VAL A 133 0
SHEET 2 A 6 GLU A 136 ASP A 144 -1 O ALA A 138 N ILE A 131
SHEET 3 A 6 TYR A 92 LEU A 97 1 N TYR A 92 O MET A 141
SHEET 4 A 6 ALA A 164 SER A 170 1 O VAL A 166 N LEU A 97
SHEET 5 A 6 ILE A 198 ASN A 203 1 O ASN A 203 N TYR A 169
SHEET 6 A 6 LYS A 228 GLU A 231 1 O LYS A 228 N LEU A 200
SHEET 1 B 6 THR B 126 VAL B 133 0
SHEET 2 B 6 GLU B 136 TYR B 143 -1 O ALA B 138 N ILE B 131
SHEET 3 B 6 TYR B 92 LEU B 97 1 N TYR B 92 O MET B 141
SHEET 4 B 6 ALA B 164 SER B 170 1 O VAL B 168 N LEU B 97
SHEET 5 B 6 ILE B 198 ASN B 203 1 O ASN B 203 N TYR B 169
SHEET 6 B 6 LYS B 228 GLU B 231 1 O LYS B 228 N LEU B 200
LINK MG MG A 1 OG SER A 105 1555 1555 1.98
LINK MG MG A 1 O2B GDP A1184 1555 1555 2.10
LINK MG MG A 1 O HOH A1186 1555 1555 2.57
LINK MG MG A 1 O HOH A1203 1555 1555 2.04
LINK MG MG A 1 O HOH A1207 1555 1555 2.25
LINK MG MG A 1 O HOH A1211 1555 1555 2.00
LINK MG MG B 1 OG SER B 105 1555 1555 2.16
LINK MG MG B 1 O2B GDP B1184 1555 1555 2.13
LINK MG MG B 1 O HOH B1203 1555 1555 2.30
LINK MG MG B 1 O HOH B1204 1555 1555 1.95
LINK MG MG B 1 O HOH B1205 1555 1555 2.20
LINK MG MG B 1 O HOH B1214 1555 1555 1.81
SITE 1 AC1 7 SER A 105 GDP A1184 HOH A1186 HOH A1193
SITE 2 AC1 7 HOH A1203 HOH A1207 HOH A1211
SITE 1 AC2 6 SER B 105 GDP B1184 HOH B1203 HOH B1204
SITE 2 AC2 6 HOH B1205 HOH B1214
SITE 1 AC3 23 MG A 1 GLY A 101 VAL A 102 GLY A 103
SITE 2 AC3 23 LYS A 104 SER A 105 ALA A 106 ASN A 203
SITE 3 AC3 23 LYS A 204 ASP A 206 LEU A 207 SER A 233
SITE 4 AC3 23 ALA A 234 ALA A 235 HOH A1193 HOH A1203
SITE 5 AC3 23 HOH A1211 HOH A1213 HOH A1217 ASP B 206
SITE 6 AC3 23 LEU B 207 GDP B1184 HOH B1193
SITE 1 AC4 19 GDP A1184 HOH A1224 MG B 1 GLY B 101
SITE 2 AC4 19 VAL B 102 GLY B 103 LYS B 104 SER B 105
SITE 3 AC4 19 ALA B 106 ASN B 203 LYS B 204 ASP B 206
SITE 4 AC4 19 LEU B 207 SER B 233 ALA B 234 ALA B 235
SITE 5 AC4 19 HOH B1203 HOH B1204 HOH B1214
CRYST1 51.427 58.560 53.603 90.00 97.18 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019445 0.000000 0.002450 0.00000
SCALE2 0.000000 0.017077 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
