HEADER SIGNALING PROTEIN 02-MAY-11 3RSL
TITLE H-RAS SOAKED IN 90% R,S,R-BISFURANOL: ONE OF 10 IN MSCS SET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE HRAS;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: H-RAS-1, HA-RAS, TRANSFORMING PROTEIN P21, C-H-RAS, P21RAS,
COMPND 5 GTPASE HRAS, N-TERMINALLY PROCESSED;
COMPND 6 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: HRAS, HRAS1;
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: PET21
KEYWDS GTP-BINDING, NUCLEOTIDE BINDING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MATTOS,G.BUHRMAN,B.KEARNEY
REVDAT 5 28-FEB-24 3RSL 1 REMARK LINK
REVDAT 4 08-NOV-17 3RSL 1 REMARK
REVDAT 3 09-NOV-11 3RSL 1 JRNL
REVDAT 2 12-OCT-11 3RSL 1 JRNL
REVDAT 1 21-SEP-11 3RSL 0
JRNL AUTH G.BUHRMAN,C.O CONNOR,B.ZERBE,B.M.KEARNEY,R.NAPOLEON,
JRNL AUTH 2 E.A.KOVRIGINA,S.VAJDA,D.KOZAKOV,E.L.KOVRIGIN,C.MATTOS
JRNL TITL ANALYSIS OF BINDING SITE HOT SPOTS ON THE SURFACE OF RAS
JRNL TITL 2 GTPASE.
JRNL REF J.MOL.BIOL. V. 413 773 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21945529
JRNL DOI 10.1016/J.JMB.2011.09.011
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 21819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2168
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.3949 - 4.1907 0.93 1356 145 0.2584 0.2636
REMARK 3 2 4.1907 - 3.3272 1.00 1381 152 0.1749 0.1924
REMARK 3 3 3.3272 - 2.9069 1.00 1365 158 0.1766 0.2056
REMARK 3 4 2.9069 - 2.6413 0.99 1349 159 0.1880 0.2220
REMARK 3 5 2.6413 - 2.4520 1.00 1374 123 0.1827 0.2109
REMARK 3 6 2.4520 - 2.3075 0.99 1346 148 0.1913 0.2003
REMARK 3 7 2.3075 - 2.1919 0.99 1313 150 0.1731 0.1940
REMARK 3 8 2.1919 - 2.0965 0.98 1333 148 0.1731 0.2153
REMARK 3 9 2.0965 - 2.0158 0.98 1335 131 0.1712 0.1873
REMARK 3 10 2.0158 - 1.9463 0.97 1298 142 0.1733 0.2174
REMARK 3 11 1.9463 - 1.8854 0.96 1269 154 0.1766 0.2142
REMARK 3 12 1.8854 - 1.8316 0.95 1280 142 0.1852 0.2334
REMARK 3 13 1.8316 - 1.7833 0.94 1260 134 0.1939 0.2500
REMARK 3 14 1.7833 - 1.7398 0.91 1225 146 0.2139 0.2581
REMARK 3 15 1.7398 - 1.7000 0.88 1167 136 0.2200 0.2509
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.45
REMARK 3 B_SOL : 69.22
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.51820
REMARK 3 B22 (A**2) : -0.51820
REMARK 3 B33 (A**2) : 1.03160
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 1429
REMARK 3 ANGLE : 1.204 1945
REMARK 3 CHIRALITY : 0.078 238
REMARK 3 PLANARITY : 0.004 225
REMARK 3 DIHEDRAL : 16.231 488
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RSL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 200MM CALCIUM CHLORIDE,
REMARK 280 PH 7.5, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 44.57000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 25.73250
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 44.36300
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 44.57000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 25.73250
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 44.36300
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 44.57000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 25.73250
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 44.36300
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 44.57000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 25.73250
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.36300
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 44.57000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 25.73250
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 44.36300
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 44.57000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 25.73250
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 44.36300
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.46500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 88.72600
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 51.46500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 88.72600
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 51.46500
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 88.72600
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 51.46500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 88.72600
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 51.46500
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 88.72600
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 51.46500
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 88.72600
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 596 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 392 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 440 LIES ON A SPECIAL POSITION.
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 GLU A 62
REMARK 465 GLU A 63
REMARK 465 TYR A 64
REMARK 465 SER A 65
REMARK 465 ALA A 66
REMARK 465 MET A 67
REMARK 465 ARG A 68
REMARK 465 ASP A 69
REMARK 465 GLN A 70
REMARK 465 TYR A 71
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 ARG A 73 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 342 O HOH A 526 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 338 O HOH A 342 2665 2.16
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 THR A 2 95.27 64.47
REMARK 500 ILE A 36 -73.53 -97.78
REMARK 500 ARG A 149 -2.68 73.68
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 592 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 81.1
REMARK 620 3 GNP A 190 O2G 172.5 93.1
REMARK 620 4 GNP A 190 O2B 92.1 172.9 93.9
REMARK 620 5 HOH A 301 O 92.6 88.4 92.0 89.7
REMARK 620 6 HOH A 303 O 85.1 91.3 90.3 90.3 177.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 591 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 28 O
REMARK 620 2 ASP A 30 OD2 85.3
REMARK 620 3 HOH A 309 O 89.0 82.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 593 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 102 O
REMARK 620 2 ASP A 105 OD2 83.1
REMARK 620 3 ASP A 105 OD1 109.1 51.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 596 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 153 OE1
REMARK 620 2 ASP A 154 OD1 88.6
REMARK 620 3 HOH A 321 O 79.6 49.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RSF A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 592
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 596
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 593
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RRY RELATED DB: PDB
REMARK 900 H-RAS CROSSLINKED AND SOAKED IN AQUEOUS SOLUTION: 1 OF 10 IN MSCS
REMARK 900 SET
REMARK 900 RELATED ID: 3RRZ RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 70% GLYCEROL: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS0 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN NEAT CYCLOPENTANOL: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS2 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 50% TRIFLUOROETHANOL: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS3 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN NEAT HEXANE: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS4 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 60% 1,6-HEXANEDIOL: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS5 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 55% DIMETHYLFORMAMIDE: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RS7 RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 50% ISOPROPANOL: 1 OF 10 IN MSCS SET
REMARK 900 RELATED ID: 3RSO RELATED DB: PDB
REMARK 900 H-RAS SOAKED IN 20% S,R,S-BISFURANOL: 1 OF 10 IN MSCS SET
DBREF 3RSL A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES 2 A 166 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES 3 A 166 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 166 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES 5 A 166 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES 6 A 166 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES 7 A 166 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES 8 A 166 ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES 9 A 166 ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES 10 A 166 CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES 11 A 166 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES 12 A 166 THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES 13 A 166 TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET GNP A 190 32
HET RSF A 203 9
HET RSF A 204 9
HET RSF A 206 9
HET RSF A 209 9
HET RSF A 207 9
HET RSF A 211 9
HET RSF A 208 9
HET RSF A 212 9
HET RSF A 213 9
HET RSF A 214 9
HET RSF A 205 9
HET RSF A 215 9
HET RSF A 210 9
HET MG A 592 1
HET CA A 591 1
HET CA A 596 1
HET CA A 593 1
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM RSF (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-OL
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
FORMUL 2 GNP C10 H17 N6 O13 P3
FORMUL 3 RSF 13(C6 H10 O3)
FORMUL 16 MG MG 2+
FORMUL 17 CA 3(CA 2+)
FORMUL 20 HOH *48(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 ASN A 86 ASP A 92 1 7
HELIX 3 3 ASP A 92 ASP A 105 1 14
HELIX 4 4 GLU A 126 GLY A 138 1 13
HELIX 5 5 GLY A 151 ARG A 164 1 14
SHEET 1 A 6 GLU A 37 ILE A 46 0
SHEET 2 A 6 GLU A 49 THR A 58 -1 O ASP A 57 N ASP A 38
SHEET 3 A 6 GLU A 3 GLY A 10 1 N LEU A 6 O LEU A 56
SHEET 4 A 6 GLY A 77 ALA A 83 1 O VAL A 81 N VAL A 9
SHEET 5 A 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 A 6 TYR A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK OG SER A 17 MG MG A 592 1555 1555 2.18
LINK O PHE A 28 CA CA A 591 1555 1555 2.36
LINK OD2 ASP A 30 CA CA A 591 1555 1555 2.37
LINK OG1 THR A 35 MG MG A 592 1555 1555 2.09
LINK O ARG A 102 CA CA A 593 1555 1555 2.38
LINK OD2 ASP A 105 CA CA A 593 1555 1555 2.49
LINK OD1 ASP A 105 CA CA A 593 1555 1555 2.62
LINK OE1 GLU A 153 CA CA A 596 1555 1555 2.40
LINK OD1 ASP A 154 CA CA A 596 1555 1555 2.29
LINK O2G GNP A 190 MG MG A 592 1555 1555 2.08
LINK O2B GNP A 190 MG MG A 592 1555 1555 2.11
LINK O HOH A 301 MG MG A 592 1555 1555 2.19
LINK O HOH A 303 MG MG A 592 1555 1555 2.16
LINK O HOH A 309 CA CA A 591 1555 1555 2.52
LINK O HOH A 321 CA CA A 596 1555 1555 3.19
SITE 1 AC1 30 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC1 30 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC1 30 VAL A 29 ASP A 30 GLU A 31 TYR A 32
SITE 4 AC1 30 PRO A 34 THR A 35 GLY A 60 GLN A 61
SITE 5 AC1 30 ASN A 116 LYS A 117 ASP A 119 LEU A 120
SITE 6 AC1 30 SER A 145 ALA A 146 LYS A 147 RSF A 206
SITE 7 AC1 30 RSF A 209 HOH A 301 HOH A 303 HOH A 304
SITE 8 AC1 30 HOH A 305 MG A 592
SITE 1 AC2 4 GLN A 25 HIS A 27 TYR A 40 HOH A 310
SITE 1 AC3 5 PHE A 28 ASP A 30 LYS A 147 RSF A 211
SITE 2 AC3 5 HOH A 309
SITE 1 AC4 4 ASP A 30 TYR A 32 GNP A 190 RSF A 213
SITE 1 AC5 4 ASP A 30 HIS A 94 LYS A 147 GNP A 190
SITE 1 AC6 5 LEU A 23 LYS A 42 VAL A 44 ARG A 149
SITE 2 AC6 5 TYR A 157
SITE 1 AC7 4 ASP A 33 RSF A 204 RSF A 210 HOH A 309
SITE 1 AC8 5 GLY A 12 GLY A 13 TYR A 32 ASN A 86
SITE 2 AC8 5 RSF A 205
SITE 1 AC9 4 GLU A 37 ALA A 59 TYR A 96 GLN A 99
SITE 1 BC1 4 GLN A 95 GLN A 99 RSF A 206 HOH A 529
SITE 1 BC2 7 ILE A 46 ASP A 47 GLU A 143 GLN A 150
SITE 2 BC2 7 GLY A 151 TYR A 157 HOH A 318
SITE 1 BC3 6 ALA A 11 GLY A 12 ASN A 86 LYS A 88
SITE 2 BC3 6 SER A 89 RSF A 208
SITE 1 BC4 5 ILE A 24 GLN A 25 ASP A 38 SER A 39
SITE 2 BC4 5 ARG A 41
SITE 1 BC5 4 GLN A 25 ASN A 26 PRO A 34 RSF A 211
SITE 1 BC6 5 SER A 17 THR A 35 GNP A 190 HOH A 301
SITE 2 BC6 5 HOH A 303
SITE 1 BC7 6 PHE A 28 ASP A 30 GLU A 31 ASP A 33
SITE 2 BC7 6 HOH A 309 HOH A 319
SITE 1 BC8 2 GLU A 153 ASP A 154
SITE 1 BC9 2 ARG A 102 ASP A 105
CRYST1 89.140 89.140 133.089 90.00 90.00 120.00 H 3 2 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 0.011218 0.006477 0.000000 0.00000
SCALE2 0.000000 0.012954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
