Header list of 2def.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 15-DEC-97 2DEF
TITLE PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE DEFORMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ACTIVE CATALYTIC CORE, RESIDUES 1 - 147;
COMPND 5 EC: 3.5.1.31;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: ACTIVE FORM CONTAINING ONE NICKEL ION IN THE METAL
COMPND 9 BINDING SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: PAL421TR;
SOURCE 5 GENE: FMS (CODONS 1-147);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUC18 (IPTG-INDUCIBLE LAC PROMOTOR),
SOURCE 9 PDEF-EC1-147;
SOURCE 10 EXPRESSION_SYSTEM_GENE: FMS (CODONS 1-147)
KEYWDS HYDROLASE, METALLOPROTEASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.MEINNEL,F.DARDEL
REVDAT 3 09-MAR-22 2DEF 1 REMARK LINK
REVDAT 2 24-FEB-09 2DEF 1 VERSN
REVDAT 1 18-MAR-98 2DEF 0
JRNL AUTH F.DARDEL,S.RAGUSA,C.LAZENNEC,S.BLANQUET,T.MEINNEL
JRNL TITL SOLUTION STRUCTURE OF NICKEL-PEPTIDE DEFORMYLASE.
JRNL REF J.MOL.BIOL. V. 280 501 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9665852
JRNL DOI 10.1006/JMBI.1998.1882
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.MEINNEL,C.LAZENNEC,F.DARDEL,J.M.SCHMITTER,S.BLANQUET
REMARK 1 TITL THE C-TERMINAL DOMAIN OF PEPTIDE DEFORMYLASE IS DISORDERED
REMARK 1 TITL 2 AND DISPENSABLE FOR ACTIVITY
REMARK 1 REF FEBS LETT. V. 385 91 1996
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.MEINNEL,S.BLANQUET,F.DARDEL
REMARK 1 TITL A NEW SUBCLASS OF THE ZINC METALLOPROTEASES SUPERFAMILY
REMARK 1 TITL 2 REVEALED BY THE SOLUTION STRUCTURE OF PEPTIDE DEFORMYLASE
REMARK 1 REF J.MOL.BIOL. V. 262 375 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.MEINNEL,C.LAZENNEC,S.BLANQUET
REMARK 1 TITL MAPPING OF THE ACTIVE SITE ZINC LIGANDS OF PEPTIDE
REMARK 1 TITL 2 DEFORMYLASE
REMARK 1 REF J.MOL.BIOL. V. 254 175 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.MEINNEL,S.BLANQUET
REMARK 1 TITL EVIDENCE THAT PEPTIDE DEFORMYLASE AND METHIONYL-TRNA(FMET)
REMARK 1 TITL 2 FORMYLTRANSFERASE ARE ENCODED WITHIN THE SAME OPERON IN
REMARK 1 TITL 3 ESCHERICHIA COLI
REMARK 1 REF J.BACTERIOL. V. 175 7737 1993
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMULATED ANNEALING USING
REMARK 3 1948 NOE RESTRAINTS -389 INTRARESIDUE -330 SEQUENTIAL -328
REMARK 3 MEDIUM RANGE -901 LONG RANGE 227 DIHEDRAL ANGLE RESTRAINTS -96
REMARK 3 PHI -13 PSI -118 CHI1 86 RESTRAINTS FOR 43 H-BONDS
REMARK 4
REMARK 4 2DEF 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_1000177990.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; CT-HSQC; HNCA;
REMARK 210 NOESY-HMQC; HCCH-TOCSY; HMBC-
REMARK 210 HSQC; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600 & DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA & X-PLOR3.1 X-PLOR3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST DIANA TARGET FUNCTION
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
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
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 HIS A 136 NE2 HIS A 136 CD2 -0.068
REMARK 500 2 HIS A 136 NE2 HIS A 136 CD2 -0.066
REMARK 500 3 HIS A 132 NE2 HIS A 132 CD2 -0.068
REMARK 500 3 HIS A 136 NE2 HIS A 136 CD2 -0.072
REMARK 500 4 HIS A 136 NE2 HIS A 136 CD2 -0.068
REMARK 500 6 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 7 HIS A 136 NE2 HIS A 136 CD2 -0.066
REMARK 500 8 HIS A 132 NE2 HIS A 132 CD2 -0.067
REMARK 500 8 HIS A 136 NE2 HIS A 136 CD2 -0.071
REMARK 500 9 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 10 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 11 HIS A 54 NE2 HIS A 54 CD2 -0.071
REMARK 500 11 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 12 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 13 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 14 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 15 HIS A 136 NE2 HIS A 136 CD2 -0.066
REMARK 500 16 HIS A 136 NE2 HIS A 136 CD2 -0.067
REMARK 500 18 HIS A 136 NE2 HIS A 136 CD2 -0.066
REMARK 500 19 HIS A 136 NE2 HIS A 136 CD2 -0.066
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 ASN A 24 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 1 ASN A 24 CA - CB - CG ANGL. DEV. = -13.5 DEGREES
REMARK 500 1 PHE A 35 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 PHE A 35 CB - CG - CD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 TYR A 39 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 TYR A 39 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 GLU A 42 CA - CB - CG ANGL. DEV. = -13.8 DEGREES
REMARK 500 1 VAL A 51 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 1 VAL A 51 N - CA - C ANGL. DEV. = -22.3 DEGREES
REMARK 500 1 HIS A 54 CA - CB - CG ANGL. DEV. = -11.6 DEGREES
REMARK 500 1 CYS A 90 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 VAL A 100 CG1 - CB - CG2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 1 ARG A 102 NH1 - CZ - NH2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 1 ARG A 102 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 1 PHE A 142 CB - CG - CD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 1 PHE A 142 CB - CG - CD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 TYR A 145 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 TYR A 145 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASN A 24 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 2 ASN A 24 CA - CB - CG ANGL. DEV. = -13.8 DEGREES
REMARK 500 2 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 PHE A 35 CB - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 2 PHE A 35 CB - CG - CD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 TYR A 39 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TYR A 39 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 VAL A 51 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 2 VAL A 51 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 2 HIS A 54 CA - CB - CG ANGL. DEV. = -10.9 DEGREES
REMARK 500 2 ASP A 61 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 2 CYS A 90 CA - CB - SG ANGL. DEV. = 10.8 DEGREES
REMARK 500 2 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ASP A 112 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 LEU A 120 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 2 PHE A 142 CB - CG - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 2 PHE A 142 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 2 TYR A 145 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 TYR A 145 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ASN A 24 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 3 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 3 PHE A 35 CB - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 3 PHE A 35 CB - CG - CD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TYR A 39 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 TYR A 39 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 VAL A 51 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 3 VAL A 51 N - CA - C ANGL. DEV. = -22.8 DEGREES
REMARK 500 3 HIS A 54 CA - CB - CG ANGL. DEV. = -11.2 DEGREES
REMARK 500 3 VAL A 100 CG1 - CB - CG2 ANGL. DEV. = -14.7 DEGREES
REMARK 500 3 ARG A 102 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 HIS A 132 CA - CB - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 3 PHE A 142 CB - CG - CD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 288 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 GLU A 11 -62.42 -105.69
REMARK 500 1 ASN A 24 -149.81 -150.02
REMARK 500 1 MET A 38 -39.93 -33.11
REMARK 500 1 ALA A 40 -37.82 -35.08
REMARK 500 1 GLU A 41 -108.30 -90.92
REMARK 500 1 GLU A 42 47.32 -159.97
REMARK 500 1 VAL A 51 -97.78 -90.33
REMARK 500 1 ASP A 52 97.77 -164.94
REMARK 500 1 ASN A 65 72.71 -117.33
REMARK 500 1 ARG A 66 56.55 37.47
REMARK 500 1 ILE A 73 -70.57 -95.57
REMARK 500 1 ASN A 74 70.17 -113.58
REMARK 500 1 LEU A 78 -59.26 -120.86
REMARK 500 1 LYS A 80 85.38 -152.74
REMARK 500 1 CYS A 90 -124.20 -92.54
REMARK 500 1 LEU A 91 -74.74 -120.14
REMARK 500 1 ILE A 93 150.39 -27.25
REMARK 500 1 GLU A 95 -42.70 -29.52
REMARK 500 1 VAL A 100 133.71 -36.61
REMARK 500 1 ARG A 102 -159.94 -120.94
REMARK 500 1 ARG A 113 -44.49 -29.79
REMARK 500 1 PHE A 142 40.04 -86.76
REMARK 500 2 ASN A 24 -143.42 -147.70
REMARK 500 2 ALA A 40 -33.05 -37.26
REMARK 500 2 GLU A 41 -125.50 -93.86
REMARK 500 2 GLU A 42 49.36 -148.16
REMARK 500 2 VAL A 51 -97.86 -88.11
REMARK 500 2 ASP A 52 98.01 -165.53
REMARK 500 2 ARG A 56 61.05 -102.83
REMARK 500 2 ARG A 66 50.61 38.87
REMARK 500 2 ASN A 74 57.40 -142.15
REMARK 500 2 LEU A 78 -54.95 -125.17
REMARK 500 2 LYS A 80 83.47 -153.14
REMARK 500 2 GLU A 87 58.99 -92.05
REMARK 500 2 CYS A 90 -119.29 -92.85
REMARK 500 2 LEU A 91 -77.21 -124.13
REMARK 500 2 ILE A 93 151.25 -27.13
REMARK 500 2 GLU A 95 -38.39 -29.74
REMARK 500 2 ARG A 102 -165.34 -124.66
REMARK 500 2 ALA A 110 -169.08 -127.42
REMARK 500 2 PHE A 142 36.09 -88.75
REMARK 500 3 ASN A 24 -149.29 -147.83
REMARK 500 3 ALA A 40 -33.11 -39.03
REMARK 500 3 GLU A 41 -125.20 -94.44
REMARK 500 3 GLU A 42 50.17 -146.91
REMARK 500 3 ALA A 48 35.51 -98.93
REMARK 500 3 VAL A 51 -96.73 -90.88
REMARK 500 3 ASP A 52 97.18 -164.55
REMARK 500 3 ARG A 66 50.90 37.89
REMARK 500 3 ILE A 73 -75.48 -89.95
REMARK 500
REMARK 500 THIS ENTRY HAS 406 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 ARG A 12 0.31 SIDE CHAIN
REMARK 500 1 ARG A 14 0.30 SIDE CHAIN
REMARK 500 1 ARG A 29 0.30 SIDE CHAIN
REMARK 500 1 ARG A 56 0.30 SIDE CHAIN
REMARK 500 1 ARG A 66 0.17 SIDE CHAIN
REMARK 500 1 ARG A 69 0.26 SIDE CHAIN
REMARK 500 1 ARG A 97 0.29 SIDE CHAIN
REMARK 500 1 ARG A 102 0.27 SIDE CHAIN
REMARK 500 1 ARG A 109 0.28 SIDE CHAIN
REMARK 500 1 ARG A 113 0.32 SIDE CHAIN
REMARK 500 2 ARG A 12 0.30 SIDE CHAIN
REMARK 500 2 ARG A 14 0.31 SIDE CHAIN
REMARK 500 2 ARG A 29 0.28 SIDE CHAIN
REMARK 500 2 ARG A 56 0.32 SIDE CHAIN
REMARK 500 2 ARG A 66 0.31 SIDE CHAIN
REMARK 500 2 ARG A 69 0.32 SIDE CHAIN
REMARK 500 2 ARG A 97 0.32 SIDE CHAIN
REMARK 500 2 ARG A 102 0.25 SIDE CHAIN
REMARK 500 2 ARG A 109 0.30 SIDE CHAIN
REMARK 500 2 ARG A 113 0.30 SIDE CHAIN
REMARK 500 3 ARG A 12 0.25 SIDE CHAIN
REMARK 500 3 ARG A 14 0.31 SIDE CHAIN
REMARK 500 3 ARG A 29 0.24 SIDE CHAIN
REMARK 500 3 ARG A 56 0.27 SIDE CHAIN
REMARK 500 3 ARG A 66 0.24 SIDE CHAIN
REMARK 500 3 ARG A 69 0.31 SIDE CHAIN
REMARK 500 3 ARG A 97 0.23 SIDE CHAIN
REMARK 500 3 ARG A 102 0.29 SIDE CHAIN
REMARK 500 3 ARG A 109 0.27 SIDE CHAIN
REMARK 500 3 ARG A 113 0.32 SIDE CHAIN
REMARK 500 4 ARG A 12 0.25 SIDE CHAIN
REMARK 500 4 ARG A 14 0.31 SIDE CHAIN
REMARK 500 4 ARG A 29 0.30 SIDE CHAIN
REMARK 500 4 ARG A 56 0.26 SIDE CHAIN
REMARK 500 4 ARG A 66 0.27 SIDE CHAIN
REMARK 500 4 ARG A 69 0.26 SIDE CHAIN
REMARK 500 4 ARG A 97 0.31 SIDE CHAIN
REMARK 500 4 ARG A 102 0.25 SIDE CHAIN
REMARK 500 4 ARG A 109 0.30 SIDE CHAIN
REMARK 500 4 ARG A 113 0.31 SIDE CHAIN
REMARK 500 5 ARG A 12 0.25 SIDE CHAIN
REMARK 500 5 ARG A 14 0.31 SIDE CHAIN
REMARK 500 5 ARG A 29 0.31 SIDE CHAIN
REMARK 500 5 ARG A 56 0.28 SIDE CHAIN
REMARK 500 5 ARG A 66 0.22 SIDE CHAIN
REMARK 500 5 ARG A 69 0.32 SIDE CHAIN
REMARK 500 5 ARG A 97 0.17 SIDE CHAIN
REMARK 500 5 ARG A 102 0.24 SIDE CHAIN
REMARK 500 5 ARG A 109 0.32 SIDE CHAIN
REMARK 500 5 ARG A 113 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 199 PLANE DEVIATIONS.
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 NI A 148 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 90 SG
REMARK 620 2 HIS A 132 NE2 91.8
REMARK 620 3 HIS A 136 NE2 111.3 100.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CATALYTIC NICKEL ION.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 148
DBREF 2DEF A 2 147 UNP P0A6K3 DEF_ECOLI 2 147
SEQRES 1 A 147 ALA VAL LEU GLN VAL LEU HIS ILE PRO ASP GLU ARG LEU
SEQRES 2 A 147 ARG LYS VAL ALA LYS PRO VAL GLU GLU VAL ASN ALA GLU
SEQRES 3 A 147 ILE GLN ARG ILE VAL ASP ASP MET PHE GLU THR MET TYR
SEQRES 4 A 147 ALA GLU GLU GLY ILE GLY LEU ALA ALA THR GLN VAL ASP
SEQRES 5 A 147 ILE HIS GLN ARG ILE ILE VAL ILE ASP VAL SER GLU ASN
SEQRES 6 A 147 ARG ASP GLU ARG LEU VAL LEU ILE ASN PRO GLU LEU LEU
SEQRES 7 A 147 GLU LYS SER GLY GLU THR GLY ILE GLU GLU GLY CYS LEU
SEQRES 8 A 147 SER ILE PRO GLU GLN ARG ALA LEU VAL PRO ARG ALA GLU
SEQRES 9 A 147 LYS VAL LYS ILE ARG ALA LEU ASP ARG ASP GLY LYS PRO
SEQRES 10 A 147 PHE GLU LEU GLU ALA ASP GLY LEU LEU ALA ILE CYS ILE
SEQRES 11 A 147 GLN HIS GLU MET ASP HIS LEU VAL GLY LYS LEU PHE MET
SEQRES 12 A 147 ASP TYR LEU SER
HET NI A 148 1
HETNAM NI NICKEL (II) ION
FORMUL 2 NI NI 2+
HELIX 1 1 ILE A 27 ALA A 40 1 14
HELIX 2 2 GLY A 124 VAL A 138 1 15
SHEET 1 A 3 GLY A 45 ALA A 47 0
SHEET 2 A 3 ILE A 58 ASP A 61 -1 N VAL A 59 O LEU A 46
SHEET 3 A 3 ARG A 69 LEU A 72 -1 N LEU A 72 O ILE A 58
SHEET 1 B 3 PHE A 118 ALA A 122 0
SHEET 2 B 3 LYS A 105 ALA A 110 -1 N ALA A 110 O PHE A 118
SHEET 3 B 3 GLU A 76 SER A 81 -1 N SER A 81 O LYS A 105
LINK SG CYS A 90 NI NI A 148 1555 1555 2.30
LINK NE2 HIS A 132 NI NI A 148 1555 1555 2.00
LINK NE2 HIS A 136 NI NI A 148 1555 1555 1.99
CISPEP 1 ILE A 8 PRO A 9 1 -0.56
CISPEP 2 ILE A 8 PRO A 9 2 -0.28
CISPEP 3 ILE A 8 PRO A 9 3 -0.48
CISPEP 4 ILE A 8 PRO A 9 4 -0.43
CISPEP 5 ILE A 8 PRO A 9 5 -0.15
CISPEP 6 ILE A 8 PRO A 9 6 -0.41
CISPEP 7 ILE A 8 PRO A 9 7 -0.15
CISPEP 8 ILE A 8 PRO A 9 8 -0.27
CISPEP 9 ILE A 8 PRO A 9 9 -0.27
CISPEP 10 ILE A 8 PRO A 9 10 -0.32
CISPEP 11 ILE A 8 PRO A 9 11 -0.21
CISPEP 12 ILE A 8 PRO A 9 12 -0.39
CISPEP 13 ILE A 8 PRO A 9 13 -0.55
CISPEP 14 ILE A 8 PRO A 9 14 -0.36
CISPEP 15 ILE A 8 PRO A 9 15 -0.35
CISPEP 16 ILE A 8 PRO A 9 16 -0.56
CISPEP 17 ILE A 8 PRO A 9 17 -0.30
CISPEP 18 ILE A 8 PRO A 9 18 -0.40
CISPEP 19 ILE A 8 PRO A 9 19 -0.43
CISPEP 20 ILE A 8 PRO A 9 20 -0.35
SITE 1 CAT 3 CYS A 90 HIS A 132 HIS A 136
SITE 1 AC1 3 CYS A 90 HIS A 132 HIS A 136
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 9 2 Bytes