REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.TANAKA,R.L.WILLIAMS,T.H.RABBITTS REMARK 1 TITL TUMOUR PREVENTION BY A SINGLE ANTIBODY DOMAIN REMARK 1 TITL 2 TARGETING THE INTERACTION OF SIGNAL TRANSDUCTION REMARK 1 TITL 3 PROTEINS WITH RAS. REMARK 1 REF EMBO J. V. 26 3250 2007 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 17568777 REMARK 1 DOI 10.1038/SJ.EMBOJ.7601744 REMARK 2 REMARK 2 RESOLUTION. 2.7 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.18 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 11076 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.291 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 586 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 802 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2470 REMARK 3 BIN FREE R VALUE SET COUNT : 53 REMARK 3 BIN FREE R VALUE : 0.3970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3003 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 36 REMARK 3 SOLVENT ATOMS : 42 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.76 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.35000 REMARK 3 B22 (A**2) : 1.17000 REMARK 3 B33 (A**2) : 0.18000 REMARK 3 B12 (A**2) : 0.00000 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): 0.422 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.332 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.530 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3092 ; 0.011 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4192 ; 1.387 ; 1.964 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 381 ; 6.408 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;33.528 ;23.830 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 519 ;18.283 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.017 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.096 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2325 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1329 ; 0.213 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2043 ; 0.305 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.147 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.370 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.614 ; 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): 1953 ; 0.360 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3062 ; 0.609 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1320 ; 1.009 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1130 ; 1.624 ; 4.500 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 : 3 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 : R 1 R 1000 REMARK 3 ORIGIN FOR THE GROUP (A): -.4628 19.1436 33.6485 REMARK 3 T TENSOR REMARK 3 T11: -.1203 T22: .0161 REMARK 3 T33: -.1241 T12: -.0109 REMARK 3 T13: .0049 T23: -.0525 REMARK 3 L TENSOR REMARK 3 L11: 2.1907 L22: 1.8448 REMARK 3 L33: 3.0986 L12: .4871 REMARK 3 L13: -.3261 L23: -.3998 REMARK 3 S TENSOR REMARK 3 S11: .0102 S12: -.0044 S13: .1231 REMARK 3 S21: .2215 S22: -.0001 S23: .1489 REMARK 3 S31: -.0141 S32: -.2647 S33: -.0101 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 : H 1 H 1000 REMARK 3 ORIGIN FOR THE GROUP (A): 12.2156 10.8085 5.5954 REMARK 3 T TENSOR REMARK 3 T11: -.0756 T22: -.1470 REMARK 3 T33: -.1121 T12: .0150 REMARK 3 T13: -.0019 T23: .0087 REMARK 3 L TENSOR REMARK 3 L11: 3.0386 L22: 2.3655 REMARK 3 L33: 4.1097 L12: -.1673 REMARK 3 L13: -1.0690 L23: 1.1457 REMARK 3 S TENSOR REMARK 3 S11: .1012 S12: -.1124 S13: .0077 REMARK 3 S21: -.2602 S22: -.0389 S23: -.0956 REMARK 3 S31: .1507 S32: .2824 S33: -.0622 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 : L 1 L 1000 REMARK 3 ORIGIN FOR THE GROUP (A): 4.8661 30.6635 -.5587 REMARK 3 T TENSOR REMARK 3 T11: .0024 T22: -.1301 REMARK 3 T33: .1369 T12: .0338 REMARK 3 T13: .0503 T23: .0507 REMARK 3 L TENSOR REMARK 3 L11: 6.3357 L22: 6.7324 REMARK 3 L33: 4.6949 L12: -.2483 REMARK 3 L13: -2.5805 L23: -.4033 REMARK 3 S TENSOR REMARK 3 S11: .2651 S12: .2582 S13: 1.1452 REMARK 3 S21: -.4153 S22: .1713 S23: -.1360 REMARK 3 S31: -.3756 S32: -.3401 S33: -.4364 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2VH5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-07. REMARK 100 THE PDBE ID CODE IS EBI-34455. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-DEC-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : OSMIC CONFOCAL OPTICS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11682 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70 REMARK 200 RESOLUTION RANGE LOW (A) : 42.18 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.7 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 4.4 REMARK 200 R MERGE (I) : 0.13 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.40 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM REMARK 280 17-18 % PEG3350, 320 MM ZINC ACETATE, 100 MM SODIUM REMARK 280 CACODYLATE, PH 5.8, 0.03 % DICHLOROMETHANE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 37.93150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.70150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.93150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.70150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 3710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN R, GLY 12 TO VAL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 REMARK 500 OE2 GLU H 1 NE2 HIS R 166 4556 1.97 REMARK 500 CE1 HIS R 27 OE2 GLU R 98 4556 2.05 REMARK 500 OE2 GLU R 31 OD2 ASP R 107 4556 2.13 REMARK 500 OE2 GLU R 98 CE1 HIS R 27 4456 2.05 REMARK 500 OD2 ASP R 107 OE2 GLU R 31 4456 2.13 REMARK 500 NE2 HIS R 166 OE2 GLU H 1 4456 1.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP R 108 CB - CG - OD1 ANGL. DEV. = 6.3 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 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 H 55 -2.81 72.59 REMARK 500 THR H 91 109.47 -58.26 REMARK 500 LEU L 13 114.21 -174.57 REMARK 500 THR L 22 67.08 82.93 REMARK 500 SER L 32 79.78 34.06 REMARK 500 SER L 33 -20.71 73.46 REMARK 500 ALA L 53 -56.24 72.16 REMARK 500 ASN R 26 18.94 54.70 REMARK 500 ILE R 36 -65.04 -94.59 REMARK 500 ASP R 108 61.39 -105.34 REMARK 500 LYS R 117 33.26 73.32 REMARK 500 ARG R 149 -1.08 78.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 THR L 22 22.4 L L OUTSIDE RANGE REMARK 500 ASP R 107 21.4 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): 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 R1168 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER R 17 OG REMARK 620 2 THR R 35 OG1 94.8 REMARK 620 3 GTP R1167 O2G 164.0 82.8 REMARK 620 4 GTP R1167 O1B 94.9 169.9 88.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP R1167 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R1168 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H1115 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H1116 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN R1169 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 121P RELATED DB: PDB REMARK 900 RELATED ID: 1AA9 RELATED DB: PDB REMARK 900 HUMAN C-HA-RAS(1-171)(DOT)GDP, NMR, REMARK 900 MINIMIZED AVERAGE STRUCTURE REMARK 900 RELATED ID: 1AGP RELATED DB: PDB REMARK 900 RELATED ID: 1BKD RELATED DB: PDB REMARK 900 COMPLEX OF HUMAN H-RAS WITH HUMAN SOS-1 REMARK 900 RELATED ID: 1CRR RELATED DB: PDB REMARK 900 RELATED ID: 1CTQ RELATED DB: PDB REMARK 900 STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP REMARK 900 AT 100 K REMARK 900 RELATED ID: 1GNR RELATED DB: PDB REMARK 900 RELATED ID: 1IAQ RELATED DB: PDB REMARK 900 C-H-RAS P21 PROTEIN MUTANT WITH THR 35 REMARK 900 REPLACED BY SER(T35S) COMPLEXED WITH REMARK 900 GUANOSINE-5'-[B,G-IMIDO] TRIPHOSPHATE REMARK 900 RELATED ID: 1JAI RELATED DB: PDB REMARK 900 H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED REMARK 900 WITHGUANOSINE-5'-[BETA,GAMMA-METHYLENE] REMARK 900 TRIPHOSPHATEAND MANGANESE REMARK 900 RELATED ID: 1LF0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF RASA59G IN THE GTP- REMARK 900 BOUND FORM REMARK 900 RELATED ID: 1NVU RELATED DB: PDB REMARK 900 STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY REMARK 900 RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE REMARK 900 EXCHANGE FACTOR SOS REMARK 900 RELATED ID: 1NVV RELATED DB: PDB REMARK 900 STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY REMARK 900 RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE REMARK 900 EXCHANGE FACTOR SOS REMARK 900 RELATED ID: 1NVW RELATED DB: PDB REMARK 900 STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY REMARK 900 RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE REMARK 900 EXCHANGE FACTOR SOS REMARK 900 RELATED ID: 1NVX RELATED DB: PDB REMARK 900 STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY REMARK 900 RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE REMARK 900 EXCHANGE FACTOR SOS REMARK 900 RELATED ID: 1P2S RELATED DB: PDB REMARK 900 H-RAS 166 IN 50% 2,2,2 TRIFLOUROETHANOL REMARK 900 RELATED ID: 1PLK RELATED DB: PDB REMARK 900 RELATED ID: 1QRA RELATED DB: PDB REMARK 900 STRUCTURE OF P21RAS IN COMPLEX WITH GTP AT REMARK 900 100 K REMARK 900 RELATED ID: 1RVD RELATED DB: PDB REMARK 900 H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA REMARK 900 ,GAMMA-IMIDO- GTP REMARK 900 RELATED ID: 1WQ1 RELATED DB: PDB REMARK 900 RAS-RASGAP COMPLEX REMARK 900 RELATED ID: 1XCM RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE GPPNHP-BOUND H- REMARK 900 RAS G60A MUTANT REMARK 900 RELATED ID: 1XD2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A TERNARY RAS:SOS:RAS REMARK 900 *GDP COMPLEX REMARK 900 RELATED ID: 1ZVQ RELATED DB: PDB REMARK 900 STRUCTURE OF THE Q61G MUTANT OF RAS IN REMARK 900 THE GDP-BOUND FORM REMARK 900 RELATED ID: 1ZW6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE GTP-BOUND FORM OF REMARK 900 RASQ61G REMARK 900 RELATED ID: 2C5L RELATED DB: PDB REMARK 900 STRUCTURE OF PLC EPSILON RAS ASSOCIATION REMARK 900 DOMAIN WITH HRAS REMARK 900 RELATED ID: 2CL6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH S- REMARK 900 CAGED GTP REMARK 900 RELATED ID: 2CL7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH GTP REMARK 900 RELATED ID: 2CLC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH GTP ( REMARK 900 2) REMARK 900 RELATED ID: 2CLD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH GDP ( REMARK 900 2) REMARK 900 RELATED ID: 1CLU RELATED DB: PDB REMARK 900 H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA REMARK 900 ,GAMMA-IMIDO- GTP REMARK 900 RELATED ID: 1CRP RELATED DB: PDB REMARK 900 RELATED ID: 1CRQ RELATED DB: PDB REMARK 900 RELATED ID: 1GNP RELATED DB: PDB REMARK 900 RELATED ID: 1GNQ RELATED DB: PDB REMARK 900 RELATED ID: 1HE8 RELATED DB: PDB REMARK 900 RAS G12V - PI 3-KINASE GAMMA COMPLEX REMARK 900 RELATED ID: 1IOZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE C-HA-RAS PROTEIN REMARK 900 PREPARED BY THECELL-FREE SYNTHESIS REMARK 900 RELATED ID: 1JAH RELATED DB: PDB REMARK 900 H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED REMARK 900 WITHGUANOSINE-5'-[BETA,GAMMA-METHYLENE] REMARK 900 TRIPHOSPHATE ANDMAGNESIUM REMARK 900 RELATED ID: 1K8R RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF RAS-BRY2RBD COMPLEX REMARK 900 RELATED ID: 1LF5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF RASA59G IN THE GDP- REMARK 900 BOUND FORM REMARK 900 RELATED ID: 1LFD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN REMARK 900 COMPLEXED WITHTHE RAS-INTERACTING DOMAIN OF REMARK 900 RALGDS REMARK 900 RELATED ID: 1P2T RELATED DB: PDB REMARK 900 H-RAS 166 IN AQUEOUS MOTHER LIQOUR, RT REMARK 900 RELATED ID: 1P2U RELATED DB: PDB REMARK 900 H-RAS IN 50% ISOPROPANOL REMARK 900 RELATED ID: 1P2V RELATED DB: PDB REMARK 900 H-RAS 166 IN 60 % 1,6 HEXANEDIOL REMARK 900 RELATED ID: 1PLL RELATED DB: PDB REMARK 900 RELATED ID: 1Q21 RELATED DB: PDB REMARK 900 RELATED ID: 1XJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE GDP-BOUND FORM OF REMARK 900 THE RASG60AMUTANT REMARK 900 RELATED ID: 221P RELATED DB: PDB REMARK 900 RELATED ID: 2CE2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH GDP REMARK 900 RELATED ID: 2CL0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RAS P21 IN COMPLEX WITH GPPNHP REMARK 900 RELATED ID: 2GDP RELATED DB: PDB REMARK 900 RELATED ID: 2Q21 RELATED DB: PDB REMARK 900 RELATED ID: 2UZI RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS REMARK 900 FV COMPLEX REMARK 900 RELATED ID: 4Q21 RELATED DB: PDB REMARK 900 RELATED ID: 5P21 RELATED DB: PDB REMARK 900 RELATED ID: 621P RELATED DB: PDB REMARK 900 RELATED ID: 6Q21 RELATED DB: PDB REMARK 900 RELATED ID: 821P RELATED DB: PDB REMARK 900 RELATED ID: 2EVW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT REMARK 900 FORM OF H-RASP21 IN COMPLEX WITH R-CAGED REMARK 900 GTP REMARK 900 RELATED ID: 421P RELATED DB: PDB REMARK 900 RELATED ID: 521P RELATED DB: PDB REMARK 900 RELATED ID: 721P RELATED DB: PDB