Header list of 1zgw.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION REGULATOR/DNA 22-APR-05 1ZGW TITLE NMR STRUCTURE OF E. COLI ADA PROTEIN IN COMPLEX WITH DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5'-D(*GP*CP*AP*AP*AP*TP*TP*AP*AP*AP*GP*CP*GP*CP*AP*AP*GP*A) COMPND 3 -3'; COMPND 4 CHAIN: B; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5'-D(*TP*CP*TP*TP*GP*CP*GP*CP*TP*TP*TP*AP*AP*TP*TP*TP*GP*C) COMPND 8 -3'; COMPND 9 CHAIN: C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: ADA POLYPROTEIN; COMPND 13 CHAIN: A; COMPND 14 FRAGMENT: N-TERMINAL DOMAIN; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: DNA SYNTHESIZER; SOURCE 4 MOL_ID: 2; SOURCE 5 SYNTHETIC: YES; SOURCE 6 OTHER_DETAILS: DNA SYNTHESIZER; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 9 ORGANISM_TAXID: 562; SOURCE 10 GENE: ADA; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PET30A KEYWDS PROTEIN-DNA COMPLEX, HELIX-TURN-HELIX, ZINC LIGAND, TRANSCRIPTION KEYWDS 2 REGULATOR-DNA COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.HE,J.C.HUS,L.J.SUN,P.ZHOU,D.P.NORMAN,V.DOETSCH,H.WEI,J.D.GROSS, AUTHOR 2 W.S.LANE,G.WAGNER,G.L.VERDINE REVDAT 3 02-MAR-22 1ZGW 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1ZGW 1 VERSN REVDAT 1 18-OCT-05 1ZGW 0 JRNL AUTH C.HE,J.C.HUS,L.J.SUN,P.ZHOU,D.P.NORMAN,V.DOETSCH,H.WEI, JRNL AUTH 2 J.D.GROSS,W.S.LANE,G.WAGNER,G.L.VERDINE JRNL TITL A METHYLATION-DEPENDENT ELECTROSTATIC SWITCH CONTROLS DNA JRNL TITL 2 REPAIR AND TRANSCRIPTIONAL ACTIVATION BY E. COLI ADA. JRNL REF MOL.CELL V. 20 117 2005 JRNL REFN ISSN 1097-2765 JRNL PMID 16209950 JRNL DOI 10.1016/J.MOLCEL.2005.08.013 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2001, X-PLOR 3.851 REMARK 3 AUTHORS : DELAGLIO, F.; BAX, A. (NMRPIPE), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ZGW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000032707. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 25 MM SODIUM PHOSPHATE; 50 MM REMARK 210 NACL; 5 MM DTT REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 13C; 15N; 70% 2H; 15N; ILE REMARK 210 DELTA1, LEU DELTA1, DELTA2, VAL REMARK 210 GAMMA1, GAMMA2 13C; 2H; VAL, ILE, REMARK 210 LEU METHYL GROUP 13C; PHE AND REMARK 210 TYR 1H; 2H; 15N, 2H; 10% 13C; REMARK 210 13C C5A LABELED THYMINE TOP OR REMARK 210 BOTTOM STRAND; UNLABELED PROTEIN; REMARK 210 13C; 15N; 2H; 13C; 15N; 15N REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY-HNCA; TROSY-HN(CO)CA; REMARK 210 TROSY-HN(CA)CB; TROSY-HN(COCA)CB; REMARK 210 TROSY-HN(CA)CO; TROSY-HNCO; REMARK 210 H(CC_CO)NH-TOCSY; (H)C(C-CO)NH- REMARK 210 TOCSY; HCCH-TOCSY; 1H-13C HSQC; REMARK 210 H/D EXCHANGE 1H-15N HSQC; 15N- REMARK 210 SEPARATED NOESY (60MS); 13C- REMARK 210 SEPARATED NOESY (100MS); 13C- REMARK 210 SEPARATED NOESY (200MS); 2D REMARK 210 NOESY; 15N-SEPARATED NOESY REMARK 210 (200MS); 2D NOESY (100MS); 13C- REMARK 210 SEPARATED NOESY (100MS) IN 90% REMARK 210 H2O 10% D2O UNLABELED PROTEIN REMARK 210 AND 13C METHYL CYS38 REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 2001, DYANA 1.5, REMARK 210 PROCHECK_NMR 3.5.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 HAVE NO RESTRAINT VIOLATIONS AND REMARK 210 LOWEST ENERGIES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 OP2 DT C 224 HB3 LYS A 129 1.50 REMARK 500 O ALA A 4 H CYS A 6 1.53 REMARK 500 O2 DT B 195 HH22 ARG A 45 1.53 REMARK 500 H ALA A 4 OG1 THR A 8 1.56 REMARK 500 O2 DT C 234 HH21 ARG A 45 1.56 REMARK 500 OE2 GLU A 97 OG1 THR A 101 1.65 REMARK 500 O3' DT C 234 O HIS A 46 1.96 REMARK 500 O ASP A 24 CG ASN A 78 2.14 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 1 DG B 190 C3' DG B 190 C2' -0.111 REMARK 500 1 DG B 190 C2' DG B 190 C1' -0.089 REMARK 500 1 DC B 191 C3' DC B 191 C2' -0.114 REMARK 500 1 DC B 191 C2' DC B 191 C1' -0.071 REMARK 500 1 DA B 192 C3' DA B 192 C2' -0.096 REMARK 500 1 DA B 192 C2' DA B 192 C1' -0.068 REMARK 500 1 DA B 193 C3' DA B 193 C2' -0.101 REMARK 500 1 DA B 193 C2' DA B 193 C1' -0.090 REMARK 500 1 DA B 194 C3' DA B 194 C2' -0.105 REMARK 500 1 DA B 194 C2' DA B 194 C1' -0.067 REMARK 500 1 DT B 195 C3' DT B 195 C2' -0.098 REMARK 500 1 DT B 196 C3' DT B 196 C2' -0.106 REMARK 500 1 DA B 197 C3' DA B 197 C2' -0.099 REMARK 500 1 DA B 197 C2' DA B 197 C1' -0.076 REMARK 500 1 DA B 198 C3' DA B 198 C2' -0.098 REMARK 500 1 DA B 198 C2' DA B 198 C1' -0.069 REMARK 500 1 DA B 199 C3' DA B 199 C2' -0.106 REMARK 500 1 DA B 199 C2' DA B 199 C1' -0.064 REMARK 500 1 DG B 200 C3' DG B 200 C2' -0.099 REMARK 500 1 DG B 200 C2' DG B 200 C1' -0.063 REMARK 500 1 DC B 201 C3' DC B 201 C2' -0.106 REMARK 500 1 DC B 201 C2' DC B 201 C1' -0.085 REMARK 500 1 DG B 202 C3' DG B 202 C2' -0.104 REMARK 500 1 DC B 203 C3' DC B 203 C2' -0.105 REMARK 500 1 DC B 203 C2' DC B 203 C1' -0.068 REMARK 500 1 DA B 204 C3' DA B 204 C2' -0.100 REMARK 500 1 DA B 204 C2' DA B 204 C1' -0.084 REMARK 500 1 DA B 205 C3' DA B 205 C2' -0.105 REMARK 500 1 DA B 205 C2' DA B 205 C1' -0.073 REMARK 500 1 DG B 206 C3' DG B 206 C2' -0.097 REMARK 500 1 DG B 206 C2' DG B 206 C1' -0.084 REMARK 500 1 DA B 207 C3' DA B 207 C2' -0.101 REMARK 500 1 DA B 207 C2' DA B 207 C1' -0.082 REMARK 500 1 DT C 221 C3' DT C 221 C2' -0.109 REMARK 500 1 DC C 222 C3' DC C 222 C2' -0.100 REMARK 500 1 DC C 222 C2' DC C 222 C1' -0.070 REMARK 500 1 DT C 223 C3' DT C 223 C2' -0.098 REMARK 500 1 DT C 223 C2' DT C 223 C1' -0.080 REMARK 500 1 DT C 224 C3' DT C 224 C2' -0.101 REMARK 500 1 DT C 224 C2' DT C 224 C1' -0.084 REMARK 500 1 DT C 224 C5 DT C 224 C7 0.039 REMARK 500 1 DG C 225 C3' DG C 225 C2' -0.099 REMARK 500 1 DG C 225 C2' DG C 225 C1' -0.087 REMARK 500 1 DC C 226 C3' DC C 226 C2' -0.098 REMARK 500 1 DC C 226 C2' DC C 226 C1' -0.071 REMARK 500 1 DG C 227 C3' DG C 227 C2' -0.100 REMARK 500 1 DG C 227 C2' DG C 227 C1' -0.075 REMARK 500 1 DC C 228 C3' DC C 228 C2' -0.096 REMARK 500 1 DC C 228 C2' DC C 228 C1' -0.074 REMARK 500 1 DT C 229 C3' DT C 229 C2' -0.104 REMARK 500 REMARK 500 THIS ENTRY HAS 1337 BOND DEVIATIONS. 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 1 DG B 190 C3' - C2' - C1' ANGL. DEV. = 12.3 DEGREES REMARK 500 1 DG B 190 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES REMARK 500 1 DG B 190 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES REMARK 500 1 DG B 190 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES REMARK 500 1 DC B 191 C3' - C2' - C1' ANGL. DEV. = 11.2 DEGREES REMARK 500 1 DC B 191 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES REMARK 500 1 DA B 192 C3' - C2' - C1' ANGL. DEV. = 12.4 DEGREES REMARK 500 1 DA B 192 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES REMARK 500 1 DA B 192 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 DA B 193 C3' - C2' - C1' ANGL. DEV. = 12.4 DEGREES REMARK 500 1 DA B 193 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES REMARK 500 1 DA B 193 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 DA B 194 C3' - C2' - C1' ANGL. DEV. = 12.0 DEGREES REMARK 500 1 DA B 194 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES REMARK 500 1 DA B 194 N7 - C8 - N9 ANGL. DEV. = 3.6 DEGREES REMARK 500 1 DT B 195 C3' - C2' - C1' ANGL. DEV. = 11.7 DEGREES REMARK 500 1 DT B 195 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 DT B 196 C3' - C2' - C1' ANGL. DEV. = 11.6 DEGREES REMARK 500 1 DT B 196 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES REMARK 500 1 DA B 197 C3' - C2' - C1' ANGL. DEV. = 12.4 DEGREES REMARK 500 1 DA B 197 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 DA B 197 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 DA B 197 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES REMARK 500 1 DA B 198 C3' - C2' - C1' ANGL. DEV. = 12.3 DEGREES REMARK 500 1 DA B 198 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 DA B 198 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 DA B 198 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES REMARK 500 1 DA B 199 C3' - C2' - C1' ANGL. DEV. = 12.7 DEGREES REMARK 500 1 DA B 199 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES REMARK 500 1 DA B 199 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 DA B 199 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES REMARK 500 1 DG B 200 C3' - C2' - C1' ANGL. DEV. = 12.2 DEGREES REMARK 500 1 DG B 200 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES REMARK 500 1 DG B 200 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES REMARK 500 1 DG B 200 C8 - N9 - C4 ANGL. DEV. = -3.5 DEGREES REMARK 500 1 DC B 201 C3' - C2' - C1' ANGL. DEV. = 12.1 DEGREES REMARK 500 1 DG B 202 C3' - C2' - C1' ANGL. DEV. = 12.0 DEGREES REMARK 500 1 DG B 202 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES REMARK 500 1 DG B 202 N7 - C8 - N9 ANGL. DEV. = 4.4 DEGREES REMARK 500 1 DG B 202 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES REMARK 500 1 DC B 203 C3' - C2' - C1' ANGL. DEV. = 12.4 DEGREES REMARK 500 1 DC B 203 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 DA B 204 C3' - C2' - C1' ANGL. DEV. = 13.2 DEGREES REMARK 500 1 DA B 204 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 DA B 204 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 DA B 205 C3' - C2' - C1' ANGL. DEV. = 12.4 DEGREES REMARK 500 1 DA B 205 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 DA B 205 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 DG B 206 C3' - C2' - C1' ANGL. DEV. = 12.3 DEGREES REMARK 500 1 DG B 206 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 2027 ANGLE DEVIATIONS. 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 1 LYS A 2 91.84 51.58 REMARK 500 1 ALA A 4 -154.56 -67.82 REMARK 500 1 THR A 5 44.24 -65.70 REMARK 500 1 CYS A 6 36.25 79.46 REMARK 500 1 LEU A 7 64.02 179.78 REMARK 500 1 ASP A 9 -31.58 -39.62 REMARK 500 1 PRO A 21 6.43 -67.75 REMARK 500 1 ARG A 45 178.58 172.06 REMARK 500 1 LYS A 70 -0.17 -56.78 REMARK 500 1 ALA A 77 -111.87 -85.40 REMARK 500 1 GLU A 97 -155.66 -87.44 REMARK 500 1 THR A 98 -61.15 -105.32 REMARK 500 1 ALA A 110 35.90 79.67 REMARK 500 1 MET A 126 48.93 -159.49 REMARK 500 1 THR A 127 89.01 -170.81 REMARK 500 1 PRO A 128 -108.30 -70.16 REMARK 500 2 ALA A 4 -154.84 -74.37 REMARK 500 2 THR A 5 45.34 -72.50 REMARK 500 2 CYS A 6 68.01 79.56 REMARK 500 2 LEU A 7 27.55 -176.95 REMARK 500 2 ASP A 9 -31.07 -40.00 REMARK 500 2 ARG A 45 -173.35 168.90 REMARK 500 2 LYS A 70 -5.70 -52.78 REMARK 500 2 ALA A 77 -115.53 -84.43 REMARK 500 2 GLU A 97 -155.47 -87.64 REMARK 500 2 THR A 98 -66.63 -105.19 REMARK 500 2 MET A 126 49.47 -160.56 REMARK 500 2 THR A 127 78.66 -170.38 REMARK 500 2 PRO A 128 -106.76 -72.26 REMARK 500 3 ALA A 4 -154.91 -82.17 REMARK 500 3 THR A 5 41.25 -73.58 REMARK 500 3 CYS A 6 51.83 79.36 REMARK 500 3 ASP A 9 -32.24 -38.94 REMARK 500 3 ARG A 45 175.10 173.76 REMARK 500 3 LYS A 70 -2.98 -55.88 REMARK 500 3 ALA A 77 -121.17 -92.75 REMARK 500 3 GLU A 97 -155.42 -87.22 REMARK 500 3 THR A 98 -62.93 -98.54 REMARK 500 3 LEU A 102 -33.96 -132.53 REMARK 500 3 MET A 126 48.95 -157.36 REMARK 500 3 THR A 127 83.90 -170.95 REMARK 500 3 PRO A 128 -108.27 -71.65 REMARK 500 4 LYS A 2 132.27 62.14 REMARK 500 4 LYS A 3 -129.98 -108.99 REMARK 500 4 ALA A 4 -154.34 -107.04 REMARK 500 4 THR A 5 22.84 -63.67 REMARK 500 4 CYS A 6 -154.85 79.74 REMARK 500 4 LEU A 7 -14.98 68.46 REMARK 500 4 ARG A 45 180.00 174.97 REMARK 500 4 LYS A 70 -9.77 -50.12 REMARK 500 REMARK 500 THIS ENTRY HAS 299 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 DG B 200 0.06 SIDE CHAIN REMARK 500 1 DG C 227 0.07 SIDE CHAIN REMARK 500 2 DG B 200 0.06 SIDE CHAIN REMARK 500 2 DG C 227 0.06 SIDE CHAIN REMARK 500 3 DG B 200 0.06 SIDE CHAIN REMARK 500 3 DG C 227 0.06 SIDE CHAIN REMARK 500 4 DG B 200 0.06 SIDE CHAIN REMARK 500 4 DG C 227 0.05 SIDE CHAIN REMARK 500 5 DG B 200 0.06 SIDE CHAIN REMARK 500 5 DG C 227 0.06 SIDE CHAIN REMARK 500 6 DG B 200 0.05 SIDE CHAIN REMARK 500 6 DG C 227 0.07 SIDE CHAIN REMARK 500 7 DG B 200 0.06 SIDE CHAIN REMARK 500 7 DG C 227 0.06 SIDE CHAIN REMARK 500 8 DG B 200 0.06 SIDE CHAIN REMARK 500 8 DG C 227 0.06 SIDE CHAIN REMARK 500 9 DG B 200 0.06 SIDE CHAIN REMARK 500 9 DG C 227 0.07 SIDE CHAIN REMARK 500 10 DG B 200 0.06 SIDE CHAIN REMARK 500 10 DG C 227 0.06 SIDE CHAIN REMARK 500 11 DG B 200 0.06 SIDE CHAIN REMARK 500 11 DG C 227 0.06 SIDE CHAIN REMARK 500 12 DG B 200 0.06 SIDE CHAIN REMARK 500 12 DG C 227 0.07 SIDE CHAIN REMARK 500 13 DG B 200 0.05 SIDE CHAIN REMARK 500 13 DG C 227 0.06 SIDE CHAIN REMARK 500 14 DG B 200 0.06 SIDE CHAIN REMARK 500 14 DG C 227 0.07 SIDE CHAIN REMARK 500 15 DG B 200 0.06 SIDE CHAIN REMARK 500 15 DG C 227 0.06 SIDE CHAIN REMARK 500 16 DG B 200 0.06 SIDE CHAIN REMARK 500 16 DG C 227 0.07 SIDE CHAIN REMARK 500 17 DG B 200 0.06 SIDE CHAIN REMARK 500 17 DG C 227 0.07 SIDE CHAIN REMARK 500 18 DG B 200 0.06 SIDE CHAIN REMARK 500 18 DG C 227 0.07 SIDE CHAIN REMARK 500 19 DG B 200 0.06 SIDE CHAIN REMARK 500 19 DG C 227 0.06 SIDE CHAIN REMARK 500 20 DG B 200 0.06 SIDE CHAIN REMARK 500 20 DG C 227 0.06 SIDE CHAIN 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 ZN A 500 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SMC A 38 SG REMARK 620 2 CYS A 42 SG 104.7 REMARK 620 3 CYS A 69 SG 100.4 122.5 REMARK 620 4 CYS A 72 SG 116.4 101.7 111.8 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 ZN A 500 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1U8B RELATED DB: PDB REMARK 900 X-RAY STRUCTURE REMARK 900 RELATED ID: 1ADN RELATED DB: PDB DBREF 1ZGW A 1 139 UNP P06134 ADA_ECOLI 1 139 DBREF 1ZGW B 190 207 PDB 1ZGW 1ZGW 190 207 DBREF 1ZGW C 221 238 PDB 1ZGW 1ZGW 221 238 SEQADV 1ZGW SMC A 38 UNP P06134 CYS 38 MODIFIED RESIDUE SEQRES 1 B 18 DG DC DA DA DA DT DT DA DA DA DG DC DG SEQRES 2 B 18 DC DA DA DG DA SEQRES 1 C 18 DT DC DT DT DG DC DG DC DT DT DT DA DA SEQRES 2 C 18 DT DT DT DG DC SEQRES 1 A 139 MET LYS LYS ALA THR CYS LEU THR ASP ASP GLN ARG TRP SEQRES 2 A 139 GLN SER VAL LEU ALA ARG ASP PRO ASN ALA ASP GLY GLU SEQRES 3 A 139 PHE VAL PHE ALA VAL ARG THR THR GLY ILE PHE SMC ARG SEQRES 4 A 139 PRO SER CYS ARG ALA ARG HIS ALA LEU ARG GLU ASN VAL SEQRES 5 A 139 SER PHE TYR ALA ASN ALA SER GLU ALA LEU ALA ALA GLY SEQRES 6 A 139 PHE ARG PRO CYS LYS ARG CYS GLN PRO ASP LYS ALA ASN SEQRES 7 A 139 PRO ARG GLN HIS ARG LEU ASP LYS ILE THR HIS ALA CYS SEQRES 8 A 139 ARG LEU LEU GLU GLN GLU THR PRO VAL THR LEU GLU ALA SEQRES 9 A 139 LEU ALA ASP GLN VAL ALA MET SER PRO PHE HIS LEU HIS SEQRES 10 A 139 ARG LEU PHE LYS ALA THR THR GLY MET THR PRO LYS ALA SEQRES 11 A 139 TRP GLN GLN ALA TRP ARG ALA ARG ARG MODRES 1ZGW SMC A 38 CYS S-METHYLCYSTEINE HET SMC A 38 14 HET ZN A 500 1 HETNAM SMC S-METHYLCYSTEINE HETNAM ZN ZINC ION FORMUL 3 SMC C4 H9 N O2 S FORMUL 4 ZN ZN 2+ HELIX 1 1 THR A 8 ARG A 19 1 12 HELIX 2 2 ASN A 57 ALA A 64 1 8 HELIX 3 3 ALA A 77 GLU A 97 1 21 HELIX 4 4 LEU A 102 ALA A 110 1 9 HELIX 5 5 SER A 112 GLY A 125 1 14 HELIX 6 6 PRO A 128 ARG A 139 1 12 SHEET 1 A 4 VAL A 52 TYR A 55 0 SHEET 2 A 4 VAL A 28 VAL A 31 -1 N ALA A 30 O SER A 53 SHEET 3 A 4 ILE A 36 SMC A 38 -1 O SMC A 38 N PHE A 29 SHEET 4 A 4 ARG A 67 PRO A 68 1 O ARG A 67 N PHE A 37 LINK C PHE A 37 N SMC A 38 1555 1555 1.29 LINK C SMC A 38 N ARG A 39 1555 1555 1.29 LINK SG SMC A 38 ZN ZN A 500 1555 1555 2.33 LINK SG CYS A 42 ZN ZN A 500 1555 1555 2.32 LINK SG CYS A 69 ZN ZN A 500 1555 1555 2.33 LINK SG CYS A 72 ZN ZN A 500 1555 1555 2.33 SITE 1 AC1 4 SMC A 38 CYS A 42 CYS A 69 CYS A 72 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - r 2 2 Bytes