Header list of 1adn.pdb file
Complete list - 16 20 Bytes
HEADER TRANSCRIPTION REGULATION 30-SEP-93 1ADN
TITLE SOLUTION STRUCTURE OF THE DNA METHYLPHOSPHOTRIESTER REPAIR DOMAIN OF
TITLE 2 ESCHERICHIA COLI ADA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ADA 10;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR L.C.MYERS,G.L.VERDINE,G.WAGNER
REVDAT 4 16-FEB-22 1ADN 1 REMARK LINK
REVDAT 3 19-MAY-09 1ADN 1 REMARK
REVDAT 2 24-FEB-09 1ADN 1 VERSN
REVDAT 1 31-JAN-94 1ADN 0
JRNL AUTH L.C.MYERS,G.L.VERDINE,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF THE DNA METHYL PHOSPHOTRIESTER REPAIR
JRNL TITL 2 DOMAIN OF ESCHERICHIA COLI ADA.
JRNL REF BIOCHEMISTRY V. 32 14089 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8260490
JRNL DOI 10.1021/BI00214A003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.C.MYERS,M.P.TERRANOVA,A.E.FERENTZ,G.WAGNER,G.L.VERDINE
REMARK 1 TITL REPAIR OF DNA METHYLPHOSPHOTRIESTERS THROUGH A
REMARK 1 TITL 2 METALLOACTIVATED CYSTEINE NUCLEOPHILE
REMARK 1 REF SCIENCE V. 261 1164 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DATA WERE COLLECTED AT PH 6.4 AND AT 25
REMARK 3 DEGREES CELSIUS. RESTRAINTS USED FOR THE STRUCTURE CALCULATIONS
REMARK 3 INCLUDED 547 NOE RESTRAINTS CONSISTING OF 108 INTRA-RESIDUE, 175
REMARK 3 SEQUENTIAL, 91 MEDIUM (1<|I-J|<6) AND 173 LONG RANGE NOES.
REMARK 3 ADDITIONALLY, 50 HYDROGEN BONDING DISTANCES AS WELL AS DIHEDRAL
REMARK 3 ANGLE RESTRAINTS FOR 69 PHI ANGLES AND 8 CHI-1 ANGLES WERE
REMARK 3 INCLUDED. STEREOSPECIFIC ASSIGNMENTS HAVE BEEN MADE FOR THE
REMARK 3 METHYLENE PROTONS OF ASN 22, CYS 42, ASN 51, SER 53, PHE 54 AND
REMARK 3 TYR 55. STEREOSPECIFIC ASSIGNMENTS HAVE ALSO BEEN MADE FOR THE
REMARK 3 METHYL GROUPS OF VAL 16, LEU 17, VAL 28, LEU 48, VAL 52, LEU 62,
REMARK 3 AND LEU 84. THIS STUDY AND REFERENCE 1 ABOVE SHOW THAT CYS 38,
REMARK 3 CYS 42, CYS 69, AND CYS 72 ARE THE LIGANDS FOR A TIGHTLY BOUND
REMARK 3 ZINC ION. A 2.3 ANGSTROM THIOL - ZINC DISTANCE RESTRAINT WAS
REMARK 3 IMPOSED ON THE FOUR CYSTEINE METAL LIGANDS. ADDITIONAL DISTANCE
REMARK 3 AND DIHEDRAL RESTRAINTS WERE APPLIED TO ENFORCE A TETRAHEDRAL
REMARK 3 METAL LIGATION AND TO MAINTAIN PROPER SP3 HYBRIDIZATION
REMARK 3 GEOMETRIES OF THE COORDINATED SULFUR ATOMS. A DIHEDRAL ANGLE
REMARK 3 RESTRAINT MAINTAINS AN S TYPE LIGAND CONFIGURATION.
REMARK 4
REMARK 4 1ADN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170689.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 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 MET A 1 C LYS A 2 N 0.143
REMARK 500 1 LYS A 2 C LYS A 3 N 0.144
REMARK 500 1 LYS A 3 C ALA A 4 N 0.144
REMARK 500 1 ALA A 4 C THR A 5 N 0.143
REMARK 500 1 THR A 5 C CYS A 6 N 0.143
REMARK 500 1 CYS A 6 C LEU A 7 N 0.142
REMARK 500 1 LEU A 7 C THR A 8 N 0.144
REMARK 500 1 THR A 8 C ASP A 9 N 0.145
REMARK 500 1 ASP A 9 C ASP A 10 N 0.144
REMARK 500 1 ASP A 10 C GLN A 11 N 0.144
REMARK 500 1 GLN A 11 C ARG A 12 N 0.143
REMARK 500 1 ARG A 12 C TRP A 13 N 0.153
REMARK 500 1 TRP A 13 C GLN A 14 N 0.146
REMARK 500 1 GLN A 14 C SER A 15 N 0.147
REMARK 500 1 SER A 15 C VAL A 16 N 0.156
REMARK 500 1 VAL A 16 C LEU A 17 N 0.141
REMARK 500 1 LEU A 17 C ALA A 18 N 0.152
REMARK 500 1 ALA A 18 C ARG A 19 N 0.143
REMARK 500 1 ARG A 19 C ASP A 20 N 0.148
REMARK 500 1 ASP A 20 C PRO A 21 N 0.139
REMARK 500 1 PRO A 21 C ASN A 22 N 0.142
REMARK 500 1 ASN A 22 C ALA A 23 N 0.146
REMARK 500 1 ALA A 23 C ASP A 24 N 0.144
REMARK 500 1 ASP A 24 C GLY A 25 N 0.143
REMARK 500 1 GLY A 25 C GLU A 26 N 0.144
REMARK 500 1 GLU A 26 CD GLU A 26 OE2 0.110
REMARK 500 1 GLU A 26 C PHE A 27 N 0.142
REMARK 500 1 PHE A 27 C VAL A 28 N 0.141
REMARK 500 1 VAL A 28 C PHE A 29 N 0.142
REMARK 500 1 PHE A 29 C ALA A 30 N 0.143
REMARK 500 1 ALA A 30 C VAL A 31 N 0.142
REMARK 500 1 VAL A 31 C ARG A 32 N 0.144
REMARK 500 1 ARG A 32 C THR A 33 N 0.142
REMARK 500 1 THR A 33 C THR A 34 N 0.143
REMARK 500 1 THR A 34 C GLY A 35 N 0.143
REMARK 500 1 GLY A 35 C ILE A 36 N 0.147
REMARK 500 1 ILE A 36 C PHE A 37 N 0.143
REMARK 500 1 PHE A 37 C CYS A 38 N 0.141
REMARK 500 1 CYS A 38 C ARG A 39 N 0.143
REMARK 500 1 ARG A 39 C PRO A 40 N 0.137
REMARK 500 1 PRO A 40 C SER A 41 N 0.141
REMARK 500 1 SER A 41 C CYS A 42 N 0.156
REMARK 500 1 CYS A 42 C ARG A 43 N 0.145
REMARK 500 1 ARG A 43 C ALA A 44 N 0.142
REMARK 500 1 ALA A 44 C ARG A 45 N 0.148
REMARK 500 1 ARG A 45 C HIS A 46 N 0.146
REMARK 500 1 HIS A 46 C ALA A 47 N 0.144
REMARK 500 1 ALA A 47 C LEU A 48 N 0.143
REMARK 500 1 LEU A 48 C ARG A 49 N 0.145
REMARK 500 1 ARG A 49 C GLU A 50 N 0.145
REMARK 500
REMARK 500 THIS ENTRY HAS 1306 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 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ASP A 10 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 PRO A 40 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 1 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 CYS A 72 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 ASP A 75 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ASP A 85 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 9 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ASP A 10 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASN A 22 N - CA - CB ANGL. DEV. = 15.5 DEGREES
REMARK 500 2 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASP A 75 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 85 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ASP A 10 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ASP A 20 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ASP A 24 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 258 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 -64.88 -107.74
REMARK 500 1 ALA A 4 -90.90 -59.24
REMARK 500 1 CYS A 6 154.25 -41.12
REMARK 500 1 LEU A 7 -79.40 -75.76
REMARK 500 1 ARG A 12 -73.45 -41.34
REMARK 500 1 ALA A 18 -96.14 -56.68
REMARK 500 1 ARG A 19 -85.57 179.53
REMARK 500 1 PRO A 21 104.18 -48.75
REMARK 500 1 ALA A 23 -85.16 -91.17
REMARK 500 1 PRO A 40 -37.33 -11.50
REMARK 500 1 SER A 41 43.39 -98.89
REMARK 500 1 ALA A 44 143.69 -39.06
REMARK 500 1 ARG A 45 95.98 -39.59
REMARK 500 1 ALA A 47 172.48 -48.82
REMARK 500 1 PRO A 68 95.73 -63.05
REMARK 500 1 ARG A 71 40.80 -158.77
REMARK 500 1 CYS A 72 55.29 6.42
REMARK 500 1 GLN A 73 99.14 -41.33
REMARK 500 1 ASP A 75 95.37 167.94
REMARK 500 1 ALA A 77 75.36 0.35
REMARK 500 1 ASN A 78 85.21 52.61
REMARK 500 1 GLN A 81 -86.05 -46.93
REMARK 500 1 ARG A 83 -96.76 -175.49
REMARK 500 1 LEU A 84 91.90 50.21
REMARK 500 1 LYS A 86 -165.53 -117.88
REMARK 500 1 THR A 88 69.07 -112.36
REMARK 500 1 ALA A 90 -42.86 -142.25
REMARK 500 1 CYS A 91 -168.88 -124.45
REMARK 500 2 LYS A 2 175.13 59.89
REMARK 500 2 LYS A 3 73.38 -102.31
REMARK 500 2 THR A 5 -149.36 -138.68
REMARK 500 2 THR A 8 -66.70 -138.92
REMARK 500 2 ARG A 12 -76.72 -41.60
REMARK 500 2 PRO A 21 -95.41 -81.58
REMARK 500 2 ALA A 23 -38.97 -153.82
REMARK 500 2 ASP A 24 -100.65 -42.93
REMARK 500 2 PRO A 40 82.48 -15.97
REMARK 500 2 SER A 41 -34.33 -152.48
REMARK 500 2 CYS A 42 100.03 -56.14
REMARK 500 2 HIS A 46 -96.67 40.48
REMARK 500 2 PRO A 68 104.16 -59.21
REMARK 500 2 LYS A 70 -80.23 -90.46
REMARK 500 2 ARG A 71 -74.29 -62.12
REMARK 500 2 CYS A 72 76.47 178.68
REMARK 500 2 GLN A 73 144.76 -39.58
REMARK 500 2 PRO A 74 -72.67 -52.04
REMARK 500 2 ASP A 75 -73.55 178.63
REMARK 500 2 ALA A 77 81.75 -13.45
REMARK 500 2 ASN A 78 87.86 39.15
REMARK 500 2 PRO A 79 -169.64 -66.87
REMARK 500
REMARK 500 THIS ENTRY HAS 366 RAMACHANDRAN OUTLIERS.
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 93 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 CYS A 42 SG 96.1
REMARK 620 3 CYS A 69 SG 102.5 118.4
REMARK 620 4 CYS A 72 SG 121.5 98.7 118.3
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 93
DBREF 1ADN A 1 92 UNP P06134 ADA_ECOLI 1 92
SEQRES 1 A 92 MET LYS LYS ALA THR CYS LEU THR ASP ASP GLN ARG TRP
SEQRES 2 A 92 GLN SER VAL LEU ALA ARG ASP PRO ASN ALA ASP GLY GLU
SEQRES 3 A 92 PHE VAL PHE ALA VAL ARG THR THR GLY ILE PHE CYS ARG
SEQRES 4 A 92 PRO SER CYS ARG ALA ARG HIS ALA LEU ARG GLU ASN VAL
SEQRES 5 A 92 SER PHE TYR ALA ASN ALA SER GLU ALA LEU ALA ALA GLY
SEQRES 6 A 92 PHE ARG PRO CYS LYS ARG CYS GLN PRO ASP LYS ALA ASN
SEQRES 7 A 92 PRO ARG GLN HIS ARG LEU ASP LYS ILE THR HIS ALA CYS
SEQRES 8 A 92 ARG
HET ZN A 93 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 THR A 8 ALA A 18 1 11
HELIX 2 H2 ASP A 24 PHE A 27 5 4
HELIX 3 H3 ALA A 58 ALA A 64 1 7
SHEET 1 S1 4 VAL A 52 TYR A 55 0
SHEET 2 S1 4 PHE A 27 ARG A 32 1 O VAL A 28 N TYR A 55
SHEET 3 S1 4 ILE A 36 ARG A 39 1 N CYS A 38 O PHE A 29
SHEET 4 S1 4 ARG A 67 CYS A 69 -1 N CYS A 69 O PHE A 37
LINK SG CYS A 38 ZN ZN A 93 1555 1555 2.27
LINK SG CYS A 42 ZN ZN A 93 1555 1555 2.36
LINK SG CYS A 69 ZN ZN A 93 1555 1555 2.23
LINK SG CYS A 72 ZN ZN A 93 1555 1555 2.40
SITE 1 AC1 4 CYS 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 - 16 20 Bytes