Header list of 1noe.pdb file
Complete list - v 3 2 Bytes
HEADER ELECTRON TRANSPORT 07-JAN-96 1NOE
TITLE NMR STUDY OF REDUCED HIGH POTENTIAL IRON SULFUR PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH POTENTIAL IRON SULFUR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HIPIP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: REDUCED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALLOCHROMATIUM VINOSUM;
SOURCE 3 ORGANISM_TAXID: 1049;
SOURCE 4 GENE: POTENTIAL
KEYWDS ELECTRON TRANSPORT, IRON-SULFUR, 4FE-4S
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR D.BENTROP,I.BERTINI,F.CAPOZZI,A.DIKIY,L.ELTIS,C.LUCHINAT
REVDAT 5 03-NOV-21 1NOE 1 REMARK SEQADV LINK
REVDAT 4 24-MAR-09 1NOE 1 ATOM CONECT
REVDAT 3 24-FEB-09 1NOE 1 VERSN
REVDAT 2 01-SEP-99 1NOE 1 JRNL
REVDAT 1 10-JUN-96 1NOE 0
JRNL AUTH D.BENTROP,I.BERTINI,F.CAPOZZI,A.DIKIY,L.ELTIS,C.LUCHINAT
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE REDUCED C77S MUTANT OF
JRNL TITL 2 THE CHROMATIUM VINOSUM HIGH-POTENTIAL IRON-SULFUR PROTEIN
JRNL TITL 3 THROUGH NUCLEAR MAGNETIC RESONANCE: COMPARISON WITH THE
JRNL TITL 4 SOLUTION STRUCTURE OF THE WILD-TYPE PROTEIN.
JRNL REF BIOCHEMISTRY V. 35 5928 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8639555
JRNL DOI 10.1021/BI9528513
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.BABINI,I.BERTINI,M.BORSARI,F.CAPOZZI,A.DIKIY,L.D.ELTIS,
REMARK 1 AUTH 2 C.LUCHINAT
REMARK 1 TITL A SERINE->CYSTEINE LIGAND MUTATION IN THE HIGH POTENTIAL
REMARK 1 TITL 2 IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM PROVIDES INSIGHT
REMARK 1 TITL 3 INTO THE ELECTRONIC STRUCTURE OF THE [4FE-4S] CLUSTER
REMARK 1 REF J.AM.CHEM.SOC. V. 118 75 1996
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.BANCI,I.BERTINI,A.DIKIY,D.H.KASTRAU,C.LUCHINAT,
REMARK 1 AUTH 2 P.SOMPORNPISUT
REMARK 1 TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED
REMARK 1 TITL 2 HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM
REMARK 1 TITL 3 THROUGH NMR
REMARK 1 REF BIOCHEMISTRY V. 34 206 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NOE 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_1000175346.
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 : 15
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 SER A 77 CB SER A 77 OG 0.393
REMARK 500 2 SER A 77 CB SER A 77 OG 0.396
REMARK 500 3 SER A 77 CB SER A 77 OG 0.391
REMARK 500 4 SER A 77 CB SER A 77 OG 0.394
REMARK 500 5 SER A 77 CB SER A 77 OG 0.393
REMARK 500 6 SER A 77 CB SER A 77 OG 0.392
REMARK 500 7 SER A 77 CB SER A 77 OG 0.395
REMARK 500 8 SER A 77 CB SER A 77 OG 0.397
REMARK 500 9 SER A 77 CB SER A 77 OG 0.399
REMARK 500 10 SER A 77 CB SER A 77 OG 0.388
REMARK 500 11 SER A 77 CB SER A 77 OG 0.395
REMARK 500 12 SER A 77 CB SER A 77 OG 0.391
REMARK 500 13 SER A 77 CB SER A 77 OG 0.389
REMARK 500 14 SER A 77 CB SER A 77 OG 0.395
REMARK 500 15 SER A 77 CB SER A 77 OG 0.394
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 GLU A 59 OE1 - CD - OE2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 7 GLU A 59 OE1 - CD - OE2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 12 LEU A 82 CB - CG - CD2 ANGL. DEV. = 13.2 DEGREES
REMARK 500 14 GLU A 59 OE1 - CD - OE2 ANGL. DEV. = -8.4 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 GLN A 21 -43.20 70.89
REMARK 500 1 SER A 26 141.33 -35.75
REMARK 500 1 GLU A 27 -6.94 -59.33
REMARK 500 1 ALA A 32 69.97 27.42
REMARK 500 1 ALA A 54 84.00 -65.27
REMARK 500 1 TRP A 80 -75.21 -73.65
REMARK 500 1 THR A 81 108.54 68.77
REMARK 500 1 LYS A 83 100.99 -45.87
REMARK 500 2 ASN A 5 -70.27 -78.33
REMARK 500 2 ALA A 6 8.26 55.92
REMARK 500 2 VAL A 7 133.05 59.07
REMARK 500 2 ASP A 10 32.81 -98.46
REMARK 500 2 GLN A 21 -38.23 72.56
REMARK 500 2 SER A 26 140.40 -37.98
REMARK 500 2 ALA A 32 74.93 45.95
REMARK 500 2 PRO A 34 -166.89 -73.49
REMARK 500 2 GLU A 40 45.57 -106.87
REMARK 500 2 ALA A 54 87.50 -60.64
REMARK 500 2 THR A 57 -125.86 -117.99
REMARK 500 2 LYS A 61 -166.41 -129.90
REMARK 500 2 ASN A 74 42.92 -101.44
REMARK 500 2 TRP A 76 149.21 74.71
REMARK 500 2 SER A 79 3.77 98.63
REMARK 500 2 ALA A 84 -63.66 -125.70
REMARK 500 3 ASN A 5 -70.32 -76.79
REMARK 500 3 ALA A 6 9.16 55.29
REMARK 500 3 VAL A 7 132.51 58.47
REMARK 500 3 ASP A 10 42.00 -94.27
REMARK 500 3 GLN A 21 -50.21 71.77
REMARK 500 3 SER A 26 142.44 -37.92
REMARK 500 3 ALA A 32 80.21 44.65
REMARK 500 3 PRO A 34 -162.19 -74.75
REMARK 500 3 GLN A 47 55.04 24.50
REMARK 500 3 MET A 49 165.89 -40.58
REMARK 500 3 ASP A 52 41.77 -73.31
REMARK 500 3 ALA A 54 81.60 -65.67
REMARK 500 3 CYS A 63 -91.12 -75.74
REMARK 500 3 GLN A 64 -61.19 -156.31
REMARK 500 3 PHE A 66 77.17 -117.29
REMARK 500 3 SER A 79 -1.69 132.37
REMARK 500 3 LYS A 83 81.25 -61.33
REMARK 500 4 ALA A 6 11.88 53.64
REMARK 500 4 VAL A 7 112.21 55.75
REMARK 500 4 ALA A 32 70.59 24.10
REMARK 500 4 ALA A 54 87.07 -63.15
REMARK 500 4 PHE A 66 104.53 -57.31
REMARK 500 4 SER A 79 14.88 81.46
REMARK 500 4 LYS A 83 80.70 -55.95
REMARK 500 5 SER A 1 93.59 -49.36
REMARK 500 5 ALA A 6 15.98 50.92
REMARK 500
REMARK 500 THIS ENTRY HAS 209 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 84 GLY A 85 2 133.08
REMARK 500 ASN A 45 CYS A 46 3 141.53
REMARK 500 SER A 79 TRP A 80 4 144.59
REMARK 500 ALA A 84 GLY A 85 6 132.88
REMARK 500 SER A 79 TRP A 80 9 149.80
REMARK 500 ALA A 84 GLY A 85 14 137.56
REMARK 500 TYR A 19 ASN A 20 15 146.11
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 3 PHE A 48 0.09 SIDE CHAIN
REMARK 500 4 TYR A 19 0.07 SIDE CHAIN
REMARK 500 8 TYR A 19 0.07 SIDE CHAIN
REMARK 500 15 TYR A 19 0.09 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 SF4 A 86 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 SF4 A 86 S2 115.7
REMARK 620 3 SF4 A 86 S3 110.7 105.0
REMARK 620 4 SF4 A 86 S4 115.8 102.8 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 86 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 SF4 A 86 S1 115.0
REMARK 620 3 SF4 A 86 S3 113.8 103.8
REMARK 620 4 SF4 A 86 S4 111.9 105.8 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 86 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 63 SG
REMARK 620 2 SF4 A 86 S1 109.9
REMARK 620 3 SF4 A 86 S2 115.1 106.2
REMARK 620 4 SF4 A 86 S4 115.9 105.6 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 86 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 77 OG
REMARK 620 2 SF4 A 86 S1 113.9
REMARK 620 3 SF4 A 86 S2 111.8 105.9
REMARK 620 4 SF4 A 86 S3 115.3 104.0 105.0
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 SF4 A 86
DBREF 1NOE A 0 85 UNP P00260 HIP_CHRVI 37 122
SEQADV 1NOE SER A 77 UNP P00260 CYS 114 ENGINEERED MUTATION
SEQRES 1 A 86 ALA SER ALA PRO ALA ASN ALA VAL ALA ALA ASP ASP ALA
SEQRES 2 A 86 THR ALA ILE ALA LEU LYS TYR ASN GLN ASP ALA THR LYS
SEQRES 3 A 86 SER GLU ARG VAL ALA ALA ALA ARG PRO GLY LEU PRO PRO
SEQRES 4 A 86 GLU GLU GLN HIS CYS ALA ASN CYS GLN PHE MET GLN ALA
SEQRES 5 A 86 ASP ALA ALA GLY ALA THR ASP GLU TRP LYS GLY CYS GLN
SEQRES 6 A 86 LEU PHE PRO GLY LYS LEU ILE ASN VAL ASN GLY TRP SER
SEQRES 7 A 86 ALA SER TRP THR LEU LYS ALA GLY
HET SF4 A 86 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 2 SF4 FE4 S4
HELIX 1 1 ALA A 12 ALA A 16 1 5
HELIX 2 2 GLU A 27 ALA A 31 5 5
HELIX 3 3 PRO A 38 GLU A 40 5 3
HELIX 4 4 CYS A 43 ASN A 45 5 3
SHEET 1 A 3 MET A 49 GLN A 50 0
SHEET 2 A 3 TRP A 60 CYS A 63 -1 N GLY A 62 O GLN A 50
SHEET 3 A 3 PHE A 66 ASN A 72 -1 N PHE A 66 O CYS A 63
LINK SG CYS A 43 FE1 SF4 A 86 1555 1555 2.16
LINK SG CYS A 46 FE2 SF4 A 86 1555 1555 2.11
LINK SG CYS A 63 FE3 SF4 A 86 1555 1555 2.13
LINK OG SER A 77 FE4 SF4 A 86 1555 1555 2.12
SITE 1 AC1 6 CYS A 43 CYS A 46 CYS A 63 SER A 77
SITE 2 AC1 6 SER A 79 TRP A 80
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 - v 3 2 Bytes