Header list of 1b9r.pdb file
Complete list - b 16 2 Bytes
HEADER FERREDOXIN 15-FEB-99 1B9R
TITLE TERPREDOXIN FROM PSEUDOMONAS SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TERPREDOXIN);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 306;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS STRUCTURE FROM MOLMOL, FERREDOXIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR H.MO,S.S.POCHAPSKY,T.C.POCHAPSKY
REVDAT 3 16-FEB-22 1B9R 1 REMARK
REVDAT 2 24-FEB-09 1B9R 1 VERSN
REVDAT 1 11-MAY-99 1B9R 0
JRNL AUTH H.MO,S.S.POCHAPSKY,T.C.POCHAPSKY
JRNL TITL A MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED TERPREDOXIN,
JRNL TITL 2 A FE2S2 FERREDOXIN FROM PSEUDOMONAS.
JRNL REF BIOCHEMISTRY V. 38 5666 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10220356
JRNL DOI 10.1021/BI983063R
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.PETERSON,J.Y.LU,J.GEISSELSODER,S.GRAHAM-LORENCE,
REMARK 1 AUTH 2 C.CARMONA,F.WITNEY,M.C.LORENCE
REMARK 1 TITL CYTOCHROME P-450TERP. ISOLATION AND PURIFICATION OF THE
REMARK 1 TITL 2 PROTEIN AND CLONING AND SEQUENCING OF ITS OPERON.
REMARK 1 REF J.BIOL.CHEM. V. 267 14193 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B9R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000488.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING DOUBLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 15N- LABELED TERPREDOXIN
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 H GLU A 53 O ILE A 98 1.47
REMARK 500 O VAL A 4 H VAL A 99 1.47
REMARK 500 O TRP A 56 H VAL A 60 1.48
REMARK 500 H VAL A 3 O VAL A 15 1.54
REMARK 500 O SER A 85 H VAL A 88 1.59
REMARK 500 O ASP A 91 H SER A 93 1.60
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 12 144.31 168.86
REMARK 500 1 TYR A 13 61.77 -150.93
REMARK 500 1 VAL A 15 -156.20 -156.74
REMARK 500 1 ALA A 27 -74.30 -27.90
REMARK 500 1 PRO A 33 -28.15 -33.72
REMARK 500 1 ILE A 35 78.74 -63.52
REMARK 500 1 VAL A 36 -90.27 -159.93
REMARK 500 1 GLU A 38 -79.77 -94.86
REMARK 500 1 CYS A 43 44.24 72.01
REMARK 500 1 ALA A 46 41.68 -146.26
REMARK 500 1 ARG A 49 75.54 -69.71
REMARK 500 1 ASP A 54 22.56 -78.14
REMARK 500 1 GLU A 62 170.23 -45.78
REMARK 500 1 ASN A 64 175.01 -53.54
REMARK 500 1 PRO A 65 5.14 -69.83
REMARK 500 1 LEU A 84 91.78 -51.81
REMARK 500 1 PRO A 92 23.83 -59.23
REMARK 500 1 PRO A 104 92.02 -53.08
REMARK 500 2 SER A 10 -32.21 -170.59
REMARK 500 2 GLU A 12 142.18 171.65
REMARK 500 2 TYR A 13 62.78 -151.47
REMARK 500 2 VAL A 15 -155.52 -161.62
REMARK 500 2 ASP A 19 107.37 -34.86
REMARK 500 2 ALA A 27 -74.48 -28.29
REMARK 500 2 PRO A 33 -155.38 -55.87
REMARK 500 2 ILE A 35 159.49 -37.80
REMARK 500 2 VAL A 36 130.05 -26.67
REMARK 500 2 ALA A 37 -159.56 -78.48
REMARK 500 2 CYS A 43 35.34 36.06
REMARK 500 2 CYS A 45 -164.37 -116.37
REMARK 500 2 ALA A 46 21.61 -157.89
REMARK 500 2 CYS A 48 40.15 -94.66
REMARK 500 2 ASP A 54 20.80 -79.04
REMARK 500 2 GLU A 62 -117.76 -48.09
REMARK 500 2 PRO A 77 -168.95 -65.76
REMARK 500 2 MET A 78 -166.49 -124.97
REMARK 500 2 THR A 79 -160.66 -106.09
REMARK 500 2 ILE A 90 163.88 -47.11
REMARK 500 2 PRO A 92 45.82 -66.15
REMARK 500 2 SER A 93 -36.96 -141.62
REMARK 500 2 PRO A 104 98.35 -54.28
REMARK 500 3 ASP A 7 -166.78 -171.14
REMARK 500 3 GLU A 12 144.24 169.81
REMARK 500 3 TYR A 13 57.33 -146.97
REMARK 500 3 VAL A 15 -154.71 -168.02
REMARK 500 3 ASP A 19 107.42 -43.35
REMARK 500 3 ALA A 27 -72.86 -28.55
REMARK 500 3 VAL A 32 160.14 -49.80
REMARK 500 3 ILE A 35 -90.78 35.59
REMARK 500 3 VAL A 36 127.56 -171.16
REMARK 500
REMARK 500 THIS ENTRY HAS 288 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 FES A 106 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 FES A 106 S1 105.2
REMARK 620 3 FES A 106 S2 105.1 105.3
REMARK 620 4 CYS A 45 SG 128.9 107.3 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 106 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 48 SG
REMARK 620 2 FES A 106 S1 106.2
REMARK 620 3 FES A 106 S2 107.9 105.4
REMARK 620 4 CYS A 86 SG 122.0 107.9 106.3
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 FES A 106
DBREF 1B9R A 1 105 UNP P33007 TERPB_PSESP 1 105
SEQRES 1 A 105 PRO ARG VAL VAL PHE ILE ASP GLU GLN SER GLY GLU TYR
SEQRES 2 A 105 ALA VAL ASP ALA GLN ASP GLY GLN SER LEU MET GLU VAL
SEQRES 3 A 105 ALA THR GLN ASN GLY VAL PRO GLY ILE VAL ALA GLU CYS
SEQRES 4 A 105 GLY GLY SER CYS VAL CYS ALA THR CYS ARG ILE GLU ILE
SEQRES 5 A 105 GLU ASP ALA TRP VAL GLU ILE VAL GLY GLU ALA ASN PRO
SEQRES 6 A 105 ASP GLU ASN ASP LEU LEU GLN SER THR GLY GLU PRO MET
SEQRES 7 A 105 THR ALA GLY THR ARG LEU SER CYS GLN VAL PHE ILE ASP
SEQRES 8 A 105 PRO SER MET ASP GLY LEU ILE VAL ARG VAL PRO LEU PRO
SEQRES 9 A 105 ALA
HET FES A 106 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 H1 LEU A 23 ASN A 30 5 8
HELIX 2 H2 ALA A 55 VAL A 60 5 6
HELIX 3 H3 PRO A 65 SER A 73 5 9
SHEET 1 S1 1 PRO A 1 ASP A 7 0
SHEET 1 S2 1 GLU A 12 ALA A 17 0
SHEET 1 S3 1 GLN A 21 SER A 22 0
SHEET 1 S4 1 ILE A 50 GLU A 53 0
SHEET 1 S5 1 THR A 82 ARG A 83 0
SHEET 1 S6 1 VAL A 88 ILE A 90 0
SHEET 1 S7 1 LEU A 97 VAL A 101 0
LINK SG CYS A 39 FE1 FES A 106 1555 1555 2.20
LINK SG CYS A 45 FE1 FES A 106 1555 1555 2.20
LINK SG CYS A 48 FE2 FES A 106 1555 1555 2.20
LINK SG CYS A 86 FE2 FES A 106 1555 1555 2.20
SITE 1 AC1 6 GLU A 38 CYS A 39 CYS A 45 CYS A 48
SITE 2 AC1 6 LEU A 84 CYS A 86
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 - b 16 2 Bytes