Header list of 1z2e.pdb file
Complete list - r 2 2 Bytes
HEADER OXIDOREDUCTASE 08-MAR-05 1Z2E
TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS ARSC IN OXIDIZED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARSENATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ARSENICAL PUMP MODIFIER;
COMPND 5 EC: 1.20.4.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACILLUS SUBTILIS, ARSENATE REDUCTASE, SOLUTION STRUCTURE, STRUCTURAL
KEYWDS 2 GENOMICS, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.JIN,Y.LI
REVDAT 4 02-MAR-22 1Z2E 1 REMARK
REVDAT 3 24-FEB-09 1Z2E 1 VERSN
REVDAT 2 06-DEC-05 1Z2E 1 JRNL
REVDAT 1 04-OCT-05 1Z2E 0
JRNL AUTH X.GUO,Y.LI,K.PENG,Y.HU,C.LI,B.XIA,C.JIN
JRNL TITL SOLUTION STRUCTURES AND BACKBONE DYNAMICS OF ARSENATE
JRNL TITL 2 REDUCTASE FROM BACILLUS SUBTILIS: REVERSIBLE CONFORMATIONAL
JRNL TITL 3 SWITCH ASSOCIATED WITH ARSENATE REDUCTION
JRNL REF J.BIOL.CHEM. V. 280 39601 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16192272
JRNL DOI 10.1074/JBC.M508132200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z2E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.85
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4MM ARSC U-15N, 13C; 20MM TRIS
REMARK 210 BUFFER; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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: 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 OE1 GLU A 21 HG SER A 36 1.58
REMARK 500 OD1 ASP A 58 HG SER A 60 1.59
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 2 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 8 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 9 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 12 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 12 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 13 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 17 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 19 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.3 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
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 CYS A 15 -93.81 -134.33
REMARK 500 1 ASP A 30 8.45 58.69
REMARK 500 1 LYS A 33 97.30 -67.62
REMARK 500 1 ALA A 37 -166.31 -160.89
REMARK 500 1 CYS A 89 87.71 44.87
REMARK 500 2 CYS A 15 -87.12 -137.88
REMARK 500 2 ASP A 30 14.32 57.14
REMARK 500 2 LYS A 33 97.42 -67.54
REMARK 500 2 ALA A 37 -168.17 -161.34
REMARK 500 2 ASP A 87 44.23 37.53
REMARK 500 2 CYS A 89 86.07 42.86
REMARK 500 3 CYS A 15 -99.45 -126.49
REMARK 500 3 ASP A 30 5.80 57.56
REMARK 500 3 LYS A 33 97.86 -68.92
REMARK 500 3 CYS A 89 95.58 60.51
REMARK 500 4 CYS A 15 -105.81 -131.68
REMARK 500 4 ASP A 30 11.44 56.35
REMARK 500 4 LYS A 33 98.78 -67.67
REMARK 500 4 THR A 63 176.76 56.07
REMARK 500 4 CYS A 89 122.62 53.56
REMARK 500 4 TRP A 101 58.10 -119.90
REMARK 500 5 CYS A 15 -90.57 -136.30
REMARK 500 5 ASP A 30 6.24 59.21
REMARK 500 5 LYS A 33 97.62 -69.46
REMARK 500 5 ALA A 37 -166.85 -161.51
REMARK 500 5 THR A 63 -173.24 52.04
REMARK 500 5 CYS A 89 90.27 43.37
REMARK 500 5 ALA A 109 95.67 -58.71
REMARK 500 6 ASN A 13 45.72 -82.80
REMARK 500 6 CYS A 15 -106.22 -145.91
REMARK 500 6 ALA A 37 -168.04 -161.09
REMARK 500 6 ASP A 87 56.77 33.17
REMARK 500 6 CYS A 89 94.63 44.05
REMARK 500 6 TRP A 101 55.54 -116.40
REMARK 500 7 CYS A 15 -106.08 -128.86
REMARK 500 7 THR A 63 -175.68 51.20
REMARK 500 7 CYS A 89 112.19 37.32
REMARK 500 7 PHE A 103 -100.37 -136.69
REMARK 500 8 THR A 11 32.69 -77.97
REMARK 500 8 CYS A 15 -90.40 -138.81
REMARK 500 8 ASP A 87 28.83 46.44
REMARK 500 8 CYS A 89 109.88 54.69
REMARK 500 9 CYS A 15 -98.56 -137.98
REMARK 500 9 ASP A 30 16.06 56.12
REMARK 500 9 LYS A 33 94.25 -67.64
REMARK 500 9 CYS A 82 72.89 -68.65
REMARK 500 9 ASP A 87 55.39 34.64
REMARK 500 9 CYS A 89 84.80 42.51
REMARK 500 9 TRP A 101 59.67 -119.11
REMARK 500 10 CYS A 15 -90.93 -139.03
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 TYR A 7 0.10 SIDE CHAIN
REMARK 500 1 ARG A 98 0.09 SIDE CHAIN
REMARK 500 1 ARG A 130 0.09 SIDE CHAIN
REMARK 500 2 TYR A 7 0.09 SIDE CHAIN
REMARK 500 3 TYR A 7 0.09 SIDE CHAIN
REMARK 500 3 ARG A 98 0.08 SIDE CHAIN
REMARK 500 4 TYR A 7 0.10 SIDE CHAIN
REMARK 500 5 TYR A 7 0.09 SIDE CHAIN
REMARK 500 5 ARG A 98 0.09 SIDE CHAIN
REMARK 500 6 TYR A 7 0.09 SIDE CHAIN
REMARK 500 7 TYR A 7 0.09 SIDE CHAIN
REMARK 500 8 TYR A 7 0.09 SIDE CHAIN
REMARK 500 8 ARG A 98 0.08 SIDE CHAIN
REMARK 500 9 TYR A 7 0.07 SIDE CHAIN
REMARK 500 10 TYR A 7 0.10 SIDE CHAIN
REMARK 500 11 TYR A 7 0.08 SIDE CHAIN
REMARK 500 11 ARG A 98 0.09 SIDE CHAIN
REMARK 500 12 TYR A 7 0.10 SIDE CHAIN
REMARK 500 12 ARG A 98 0.08 SIDE CHAIN
REMARK 500 12 ARG A 108 0.08 SIDE CHAIN
REMARK 500 13 TYR A 7 0.07 SIDE CHAIN
REMARK 500 13 ARG A 98 0.09 SIDE CHAIN
REMARK 500 14 TYR A 7 0.10 SIDE CHAIN
REMARK 500 14 ARG A 98 0.09 SIDE CHAIN
REMARK 500 15 TYR A 7 0.10 SIDE CHAIN
REMARK 500 15 ARG A 98 0.09 SIDE CHAIN
REMARK 500 15 ARG A 130 0.09 SIDE CHAIN
REMARK 500 16 TYR A 7 0.08 SIDE CHAIN
REMARK 500 16 ARG A 98 0.08 SIDE CHAIN
REMARK 500 17 TYR A 7 0.09 SIDE CHAIN
REMARK 500 17 ARG A 98 0.08 SIDE CHAIN
REMARK 500 18 TYR A 7 0.09 SIDE CHAIN
REMARK 500 19 TYR A 7 0.09 SIDE CHAIN
REMARK 500 19 ARG A 98 0.09 SIDE CHAIN
REMARK 500 20 TYR A 7 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JL3 RELATED DB: PDB
REMARK 900 OXIDOREDUCTASE
REMARK 900 RELATED ID: 1Z2D RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN REDUCED STATE
DBREF 1Z2E A 1 139 UNP P45947 ARSC_BACSU 1 139
SEQRES 1 A 139 MET GLU ASN LYS ILE ILE TYR PHE LEU CYS THR GLY ASN
SEQRES 2 A 139 SER CYS ARG SER GLN MET ALA GLU GLY TRP ALA LYS GLN
SEQRES 3 A 139 TYR LEU GLY ASP GLU TRP LYS VAL TYR SER ALA GLY ILE
SEQRES 4 A 139 GLU ALA HIS GLY LEU ASN PRO ASN ALA VAL LYS ALA MET
SEQRES 5 A 139 LYS GLU VAL GLY ILE ASP ILE SER ASN GLN THR SER ASP
SEQRES 6 A 139 ILE ILE ASP SER ASP ILE LEU ASN ASN ALA ASP LEU VAL
SEQRES 7 A 139 VAL THR LEU CYS GLY ASP ALA ALA ASP LYS CYS PRO MET
SEQRES 8 A 139 THR PRO PRO HIS VAL LYS ARG GLU HIS TRP GLY PHE ASP
SEQRES 9 A 139 ASP PRO ALA ARG ALA GLN GLY THR GLU GLU GLU LYS TRP
SEQRES 10 A 139 ALA PHE PHE GLN ARG VAL ARG ASP GLU ILE GLY ASN ARG
SEQRES 11 A 139 LEU LYS GLU PHE ALA GLU THR GLY LYS
HELIX 1 1 CYS A 15 LEU A 28 1 14
HELIX 2 2 ASN A 45 GLU A 54 1 10
HELIX 3 3 ASP A 68 ASN A 73 1 6
HELIX 4 4 ASP A 105 ALA A 109 5 5
HELIX 5 5 THR A 112 THR A 137 1 26
SHEET 1 A 4 TRP A 32 GLY A 38 0
SHEET 2 A 4 LYS A 4 CYS A 10 1 N LYS A 4 O LYS A 33
SHEET 3 A 4 LEU A 77 CYS A 82 1 O VAL A 79 N LEU A 9
SHEET 4 A 4 ARG A 98 PHE A 103 1 O TRP A 101 N THR A 80
SSBOND 1 CYS A 82 CYS A 89 1555 1555 2.04
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