REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 25816 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) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1369 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) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1824 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2080 REMARK 3 BIN FREE R VALUE SET COUNT : 114 REMARK 3 BIN FREE R VALUE : 0.2930 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 : 38 REMARK 3 SOLVENT ATOMS : 289 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.27 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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): 0.206 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.749 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3094 ; 0.019 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4193 ; 1.812 ; 1.963 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 381 ; 6.885 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;36.865 ;23.873 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 521 ;16.388 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.435 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 463 ; 0.142 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2329 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1498 ; 0.243 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2064 ; 0.309 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 291 ; 0.200 ; 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): 28 ; 0.283 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.419 ; 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): 1964 ; 1.183 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3061 ; 1.796 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1326 ; 2.870 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1132 ; 4.154 ; 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 : 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 REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2UZI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-APR-07. REMARK 100 THE PDBE ID CODE IS EBI-32368. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-05 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : TRUNCATE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27214 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.320 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.700 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 3.380 REMARK 200 R MERGE (I) : 0.10000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.35 REMARK 200 R MERGE FOR SHELL (I) : 0.36000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.670 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1AGP, 1A2Y REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.2 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM REMARK 280 17-18 % PEG3350, 400 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 37.76400 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.31600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.76400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.31600 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 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 375 REMARK 375 SPECIAL POSITION REMARK 375 HOH R2096 LIES ON A SPECIAL POSITION. 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 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 VAL L 21 - N ILE L 77 2.14 REMARK 500 OG1 THR L 24 - O HOH L 2012 2.20 REMARK 500 OE1 GLN L 81 - O HOH L 2043 2.18 REMARK 500 O HOH R 2001 - O HOH R 2003 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS H 96 CB CYS H 96 SG -0.097 REMARK 500 THR L 24 C CYS L 25 N 0.163 REMARK 500 MET R 1 N MET R 1 CA 0.147 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 THR L 22 N - CA - C ANGL. DEV. = 26.8 DEGREES REMARK 500 ASP R 30 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 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 L 32 -126.28 56.91 REMARK 500 ALA L 53 -18.67 73.69 REMARK 500 SER L 54 12.99 -158.69 REMARK 500 ILE R 36 -64.05 -99.08 REMARK 500 LYS R 117 34.84 70.25 REMARK 500 ARG R 149 -10.89 78.71 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 VAL L 21 THR L 22 37.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 VAL L 21 11.58 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 10.4 L L OUTSIDE RANGE REMARK 500 THR R 2 24.5 L L OUTSIDE RANGE REMARK 500 ASP R 107 21.8 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 ZN H1115 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H2106 O REMARK 620 2 HOH H2071 O 167.8 REMARK 620 3 ASP H 73 OD1 80.7 87.2 REMARK 620 4 SER H 75 OG 90.4 88.5 76.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H1116 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 62 OD2 REMARK 620 2 ASP H 62 OD1 51.4 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN R1169 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU R 98 OE2 REMARK 620 2 HOH R2127 O 141.2 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN R1171 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP R 108 OD1 REMARK 620 2 ASP R 108 OD2 51.6 REMARK 620 3 HIS R 166 NE2 123.2 90.8 REMARK 620 4 GLU H 1 OE1 120.1 96.5 102.9 REMARK 620 5 GLU H 1 OE2 71.8 80.3 151.0 51.6 REMARK 620 N 1 2 3 4 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 82.6 REMARK 620 3 HOH R2049 O 85.5 88.9 REMARK 620 4 GTP R1167 O2G 171.4 91.3 100.4 REMARK 620 5 GTP R1167 O1B 93.6 174.1 86.3 92.9 REMARK 620 6 HOH R2022 O 86.0 89.8 171.5 88.0 94.5 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 ZN H1115 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H1116 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R1168 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN R1169 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN R1170 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN R1171 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP R1167 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: 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: 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: 1GNP RELATED DB: PDB REMARK 900 RELATED ID: 1GNQ RELATED DB: PDB REMARK 900 RELATED ID: 1GNR RELATED DB: PDB REMARK 900 RELATED ID: 1HE8 RELATED DB: PDB REMARK 900 RAS G12V - PI 3-KINASE GAMMA COMPLEX 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: 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: 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: 1K8R RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF RAS-BRY2RBD COMPLEX 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: 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: 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: 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: 1PLJ RELATED DB: PDB REMARK 900 RELATED ID: 1PLK RELATED DB: PDB REMARK 900 RELATED ID: 1PLL RELATED DB: PDB REMARK 900 RELATED ID: 1Q21 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: 1XJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE GDP-BOUND FORM OF REMARK 900 THE RASG60AMUTANT 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: 221P RELATED DB: PDB 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: 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: 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: 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: 2GDP RELATED DB: PDB REMARK 900 RELATED ID: 2Q21 RELATED DB: PDB REMARK 900 RELATED ID: 421P RELATED DB: PDB REMARK 900 RELATED ID: 4Q21 RELATED DB: PDB REMARK 900 RELATED ID: 521P 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: 721P RELATED DB: PDB REMARK 900 RELATED ID: 821P RELATED DB: PDB