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: ADA POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-
COMPND 8 D(*GP*CP*AP*AP*AP*TP*TP*AP*AP*AP*GP*CP*GP*CP*AP*AP*GP*A)-
COMPND 9 3';
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 5'-
COMPND 14 D(*TP*CP*TP*TP*GP*CP*GP*CP*TP*TP*TP*AP*AP*TP*TP*TP*GP*C)-
COMPND 15 3';
COMPND 16 CHAIN: C;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ADA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET30A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: DNA SYNTHESIZER;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: DNA SYNTHESIZER
KEYWDS PROTEIN-DNA COMPLEX, HELIX-TURN-HELIX, ZINC LIGAND,
KEYWDS 2 TRANSCRIPTION 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,
AUTHOR 2 J.D.GROSS,W.S.LANE,G.WAGNER,G.L.VERDINE
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,
JRNL AUTH 2 H.WEI,J.D.GROSS,W.S.LANE,G.WAGNER,G.L.VERDINE
JRNL TITL A METHYLATION-DEPENDENT ELECTROSTATIC SWITCH
JRNL TITL 2 CONTROLS DNA REPAIR AND TRANSCRIPTIONAL ACTIVATION
JRNL TITL 3 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 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
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 RCSB ID CODE IS RCSB032707.
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,
REMARK 210 VAL GAMMA1, GAMMA2 13C; 2H;
REMARK 210 VAL, ILE, LEU METHYL GROUP
REMARK 210 13C; PHE AND TYR 1H; 2H; 15N,
REMARK 210 2H; 10% 13C; 13C C5A LABELED
REMARK 210 THYMINE TOP OR BOTTOM STRAND;
REMARK 210 UNLABELED PROTEIN; 13C; 15N;
REMARK 210 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)
REMARK 210 CB, TROSY-HN(CA)CO, TROSY-
REMARK 210 HNCO, H(CC_CO)NH-TOCSY, (H)C(C
REMARK 210 -CO)NH-TOCSY, HCCH-TOCSY, 1H-
REMARK 210 13C HSQC, H/D EXCHANGE 1H-15N
REMARK 210 HSQC, 15N-SEPARATED NOESY
REMARK 210 (60MS), 13C-SEPARATED NOESY
REMARK 210 (100MS), 13C-SEPARATED NOESY
REMARK 210 (200MS), 2D NOESY, 15N-
REMARK 210 SEPARATED NOESY (200MS), 2D
REMARK 210 NOESY (100MS), 13C-SEPARATED
REMARK 210 NOESY (100MS) IN 90% H2O 10%
REMARK 210 D2O UNLABELED PROTEIN AND 13C
REMARK 210 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 : NMRPIPE 2001, XEASY 2001,
REMARK 210 DYANA 1.5, 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
REMARK 210 MODELS HAVE NO RESTRAINT
REMARK 210 VIOLATIONS AND 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 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 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. = 12.6 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. = 12.0 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 4 ALA A 77 -106.36 -85.05
REMARK 500 4 GLN A 96 -65.48 -90.04
REMARK 500 4 GLU A 97 -155.34 -88.45
REMARK 500 4 THR A 98 -60.52 -105.39
REMARK 500 4 LEU A 102 -32.71 -133.20
REMARK 500 4 ALA A 110 39.28 79.76
REMARK 500 4 MET A 126 49.46 -157.47
REMARK 500 4 THR A 127 82.57 -170.59
REMARK 500 4 PRO A 128 -107.66 -73.89
REMARK 500 5 LYS A 2 92.90 53.39
REMARK 500 5 ALA A 4 -154.56 -65.78
REMARK 500 5 THR A 5 34.09 -67.94
REMARK 500 5 CYS A 6 53.06 79.84
REMARK 500 5 LEU A 7 35.58 -171.61
REMARK 500 5 ARG A 19 31.27 88.74
REMARK 500 5 ARG A 45 172.18 177.45
REMARK 500 5 LYS A 70 0.52 -56.36
REMARK 500 5 ALA A 77 -112.56 -82.41
REMARK 500 5 GLU A 97 -155.58 -87.24
REMARK 500 5 THR A 98 -71.37 -105.32
REMARK 500 5 ALA A 110 32.58 79.69
REMARK 500 5 MET A 126 49.17 -162.04
REMARK 500 5 THR A 127 80.24 -170.69
REMARK 500 5 PRO A 128 -106.00 -69.79
REMARK 500 6 LYS A 2 94.28 52.11
REMARK 500 6 LYS A 3 70.43 -167.08
REMARK 500 6 ALA A 4 -154.70 -78.88
REMARK 500 6 THR A 5 38.37 -70.62
REMARK 500 6 CYS A 6 61.98 79.41
REMARK 500 6 LEU A 7 28.95 -157.90
REMARK 500 6 ASP A 9 -32.48 -39.61
REMARK 500 6 ARG A 45 -169.81 169.24
REMARK 500 6 LYS A 70 -2.26 -55.53
REMARK 500 6 ALA A 77 -122.04 -156.05
REMARK 500 6 GLU A 97 -155.82 -79.32
REMARK 500 6 THR A 98 -67.24 -105.41
REMARK 500 6 LEU A 102 -41.52 -131.13
REMARK 500 6 ALA A 110 30.22 79.62
REMARK 500 6 MET A 126 49.10 -160.01
REMARK 500 6 THR A 127 92.81 -170.77
REMARK 500 6 PRO A 128 -108.06 -66.27
REMARK 500 7 LYS A 2 -137.43 65.15
REMARK 500 7 LYS A 3 149.00 63.87
REMARK 500 7 THR A 5 77.69 -66.12
REMARK 500 7 CYS A 6 -178.27 89.37
REMARK 500 7 ARG A 19 36.21 83.07
REMARK 500 7 ARG A 45 172.64 177.67
REMARK 500 7 LEU A 48 161.30 -49.18
REMARK 500 7 LYS A 70 -0.10 -56.66
REMARK 500 7 ALA A 77 -109.02 -87.87
REMARK 500 7 GLU A 97 -155.94 -87.83
REMARK 500 7 THR A 98 -60.25 -105.05
REMARK 500 7 MET A 126 49.65 -155.26
REMARK 500 7 THR A 127 83.25 -170.17
REMARK 500 7 PRO A 128 -111.21 -69.64
REMARK 500 8 ALA A 4 -154.40 -122.48
REMARK 500 8 THR A 5 25.02 -60.61
REMARK 500 8 CYS A 6 120.80 79.63
REMARK 500 8 ASP A 9 -28.04 -38.91
REMARK 500 8 ARG A 45 177.96 174.42
REMARK 500 8 LYS A 70 -8.84 -49.79
REMARK 500 8 LYS A 76 74.13 -115.02
REMARK 500 8 ALA A 77 -129.65 -87.31
REMARK 500 8 GLU A 97 -155.93 -87.21
REMARK 500 8 THR A 98 -70.05 -103.32
REMARK 500 8 MET A 126 48.28 -158.40
REMARK 500 8 THR A 127 93.22 -171.30
REMARK 500 8 PRO A 128 -109.30 -66.75
REMARK 500 9 LYS A 2 95.96 53.66
REMARK 500 9 ALA A 4 -162.19 -71.14
REMARK 500 9 CYS A 6 71.73 79.41
REMARK 500 9 LEU A 7 37.85 175.57
REMARK 500 9 PRO A 21 6.39 -67.96
REMARK 500 9 ARG A 45 168.70 176.60
REMARK 500 9 LYS A 70 10.72 -64.41
REMARK 500 9 ALA A 77 -115.96 -96.25
REMARK 500 9 GLU A 97 -155.86 -87.50
REMARK 500 9 THR A 98 -63.55 -105.37
REMARK 500 9 LEU A 102 -36.62 -131.93
REMARK 500 9 ALA A 110 31.81 81.78
REMARK 500 9 MET A 126 49.31 -160.41
REMARK 500 9 THR A 127 81.61 -170.34
REMARK 500 9 PRO A 128 -110.98 -70.31
REMARK 500 10 LYS A 2 -72.44 64.65
REMARK 500 10 ALA A 4 -154.89 -74.67
REMARK 500 10 THR A 5 41.47 -70.33
REMARK 500 10 CYS A 6 53.81 79.35
REMARK 500 10 PRO A 21 6.39 -68.90
REMARK 500 10 ARG A 45 -179.12 170.57
REMARK 500 10 LYS A 70 -2.21 -55.10
REMARK 500 10 ALA A 77 -130.42 -110.43
REMARK 500 10 PRO A 79 -3.16 -59.99
REMARK 500 10 GLU A 95 -11.37 -143.81
REMARK 500 10 GLU A 97 -155.69 -74.52
REMARK 500 10 THR A 98 -71.04 -105.13
REMARK 500 10 LEU A 102 -53.04 -131.54
REMARK 500 10 MET A 126 49.49 -159.18
REMARK 500 10 THR A 127 85.07 -170.41
REMARK 500 10 PRO A 128 -109.23 -69.70
REMARK 500 11 ALA A 4 -154.94 -125.23
REMARK 500 11 ASP A 9 -33.52 -39.79
REMARK 500 11 ARG A 19 37.87 75.14
REMARK 500 11 ARG A 45 -179.09 174.02
REMARK 500 11 LYS A 70 9.00 -64.90
REMARK 500 11 ALA A 77 -112.14 -87.09
REMARK 500 11 GLN A 96 -65.02 -90.25
REMARK 500 11 GLU A 97 -156.52 -88.25
REMARK 500 11 THR A 98 -74.41 -106.11
REMARK 500 11 LEU A 102 -37.41 -131.62
REMARK 500 11 ALA A 110 30.08 79.70
REMARK 500 11 MET A 126 49.18 -158.86
REMARK 500 11 THR A 127 82.02 -170.72
REMARK 500 11 PRO A 128 -102.01 -72.82
REMARK 500 12 LYS A 2 -38.20 -169.78
REMARK 500 12 ALA A 4 -154.67 -92.21
REMARK 500 12 THR A 5 41.47 -69.81
REMARK 500 12 CYS A 6 50.43 79.49
REMARK 500 12 LEU A 7 39.79 -172.12
REMARK 500 12 PRO A 21 6.18 -69.62
REMARK 500 12 ARG A 45 178.53 174.87
REMARK 500 12 LYS A 70 5.39 -59.74
REMARK 500 12 ALA A 77 -115.11 -99.18
REMARK 500 12 GLU A 97 -155.91 -87.55
REMARK 500 12 THR A 98 -63.89 -105.35
REMARK 500 12 ALA A 110 41.67 79.72
REMARK 500 12 MET A 126 48.67 -157.65
REMARK 500 12 THR A 127 84.16 -171.04
REMARK 500 12 PRO A 128 -112.16 -72.34
REMARK 500 13 ALA A 4 -154.66 -111.21
REMARK 500 13 THR A 5 49.20 -66.35
REMARK 500 13 CYS A 6 101.44 79.55
REMARK 500 13 LEU A 7 80.28 94.57
REMARK 500 13 ASP A 9 -29.43 -39.18
REMARK 500 13 ARG A 45 177.34 170.91
REMARK 500 13 LYS A 70 -2.85 -53.33
REMARK 500 13 ALA A 77 -132.85 -98.33
REMARK 500 13 ARG A 80 -70.00 -43.48
REMARK 500 13 GLU A 97 -155.49 -87.34
REMARK 500 13 LEU A 102 -47.96 -133.96
REMARK 500 13 MET A 126 49.15 -159.25
REMARK 500 13 THR A 127 85.25 -170.81
REMARK 500 13 PRO A 128 -103.84 -72.11
REMARK 500 14 LYS A 2 -44.14 67.88
REMARK 500 14 ALA A 4 -154.85 -63.07
REMARK 500 14 THR A 5 41.76 -71.83
REMARK 500 14 CYS A 6 94.12 79.53
REMARK 500 14 LEU A 7 -19.73 179.50
REMARK 500 14 ARG A 45 178.14 174.55
REMARK 500 14 LEU A 48 161.38 -49.76
REMARK 500 14 LYS A 70 0.42 -56.60
REMARK 500 14 ALA A 77 -120.04 -88.18
REMARK 500 14 ARG A 80 -72.54 -47.44
REMARK 500 14 GLU A 97 -155.40 -87.49
REMARK 500 14 THR A 98 -66.49 -105.02
REMARK 500 14 LEU A 102 -46.36 -132.59
REMARK 500 14 ALA A 110 31.71 79.62
REMARK 500 14 MET A 126 49.41 -156.66
REMARK 500 14 THR A 127 82.58 -170.57
REMARK 500 14 PRO A 128 -107.96 -72.57
REMARK 500 15 LYS A 3 123.15 -170.90
REMARK 500 15 ALA A 4 -158.65 -82.34
REMARK 500 15 CYS A 6 68.45 79.55
REMARK 500 15 LEU A 7 30.06 -178.07
REMARK 500 15 THR A 8 64.16 -104.98
REMARK 500 15 PRO A 21 6.29 -69.31
REMARK 500 15 ARG A 45 -176.43 172.47
REMARK 500 15 LYS A 70 -6.85 -52.06
REMARK 500 15 ALA A 77 -119.79 -84.50
REMARK 500 15 GLU A 97 -155.56 -85.86
REMARK 500 15 THR A 98 -66.09 -105.09
REMARK 500 15 LEU A 102 -47.86 -132.02
REMARK 500 15 ALA A 110 30.57 138.71
REMARK 500 15 MET A 126 48.97 -159.76
REMARK 500 15 THR A 127 89.02 -170.83
REMARK 500 15 PRO A 128 -116.45 -67.17
REMARK 500 16 LYS A 3 -165.13 -108.80
REMARK 500 16 ALA A 4 -154.17 -148.36
REMARK 500 16 THR A 5 46.52 -55.15
REMARK 500 16 CYS A 6 96.11 79.56
REMARK 500 16 LEU A 7 77.67 80.46
REMARK 500 16 ASP A 9 -31.76 -39.81
REMARK 500 16 PRO A 21 6.25 -67.52
REMARK 500 16 ARG A 45 -178.50 173.97
REMARK 500 16 LEU A 48 160.79 -47.89
REMARK 500 16 LYS A 70 2.88 -55.82
REMARK 500 16 ALA A 77 -116.24 -91.34
REMARK 500 16 GLU A 97 -156.06 -84.83
REMARK 500 16 THR A 98 -61.28 -105.70
REMARK 500 16 LEU A 102 -64.85 -131.24
REMARK 500 16 MET A 126 49.25 -159.06
REMARK 500 16 THR A 127 89.50 -170.56
REMARK 500 16 PRO A 128 -109.88 -68.07
REMARK 500 17 LYS A 2 -1.77 68.72
REMARK 500 17 PRO A 21 6.24 -68.76
REMARK 500 17 ARG A 45 175.80 174.12
REMARK 500 17 LYS A 70 -5.56 -53.49
REMARK 500 17 ALA A 77 -112.41 -79.52
REMARK 500 17 GLU A 97 -155.65 -87.54
REMARK 500 17 THR A 98 -61.42 -105.16
REMARK 500 17 LEU A 102 -53.94 -132.78
REMARK 500 17 MET A 126 49.31 -158.88
REMARK 500 17 THR A 127 91.59 -170.74
REMARK 500 17 PRO A 128 -104.91 -69.69
REMARK 500 18 ALA A 4 -154.37 -129.13
REMARK 500 18 THR A 5 46.80 -62.19
REMARK 500 18 CYS A 6 107.16 79.62
REMARK 500 18 LEU A 7 75.83 93.81
REMARK 500 18 ASP A 9 -28.17 -39.51
REMARK 500 18 ARG A 19 29.80 95.15
REMARK 500 18 ARG A 45 172.88 169.99
REMARK 500 18 LYS A 70 0.51 -56.68
REMARK 500 18 ALA A 77 -134.96 -103.81
REMARK 500 18 GLU A 97 -155.34 -87.34
REMARK 500 18 THR A 98 -60.95 -103.76
REMARK 500 18 LEU A 102 -42.18 -132.70
REMARK 500 18 ALA A 110 33.88 79.99
REMARK 500 18 MET A 126 48.81 -161.05
REMARK 500 18 THR A 127 92.70 -170.94
REMARK 500 18 PRO A 128 -110.51 -66.95
REMARK 500 19 LYS A 2 -57.75 -151.60
REMARK 500 19 LYS A 3 166.40 56.48
REMARK 500 19 ALA A 4 -154.67 -112.92
REMARK 500 19 THR A 5 48.28 -66.80
REMARK 500 19 CYS A 6 40.15 79.51
REMARK 500 19 LEU A 7 75.93 168.19
REMARK 500 19 ARG A 45 175.25 174.82
REMARK 500 19 LYS A 70 -1.67 -54.58
REMARK 500 19 ALA A 77 -112.55 -87.02
REMARK 500 19 GLU A 97 -155.60 -87.54
REMARK 500 19 THR A 98 -60.84 -105.02
REMARK 500 19 ALA A 110 32.29 79.64
REMARK 500 19 MET A 126 48.15 -160.19
REMARK 500 19 THR A 127 91.20 -171.51
REMARK 500 19 PRO A 128 -114.81 -67.21
REMARK 500 20 ALA A 4 72.40 -39.39
REMARK 500 20 CYS A 6 28.19 95.17
REMARK 500 20 LEU A 7 88.97 81.47
REMARK 500 20 ASP A 9 -28.45 -39.42
REMARK 500 20 PRO A 21 6.42 -65.68
REMARK 500 20 ARG A 45 175.53 171.27
REMARK 500 20 LYS A 70 -6.77 -50.27
REMARK 500 20 ALA A 77 -116.06 -80.04
REMARK 500 20 GLU A 97 -155.68 -87.20
REMARK 500 20 THR A 98 -65.36 -105.29
REMARK 500 20 LEU A 102 -36.37 -131.55
REMARK 500 20 ALA A 110 38.42 79.98
REMARK 500 20 MET A 126 48.54 -157.98
REMARK 500 20 THR A 127 86.68 -171.34
REMARK 500 20 PRO A 128 -118.81 -71.47
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 1 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 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
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
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
(ATOM LINES ARE NOT SHOWN.)
END
