Header list of 1cch.pdb file
Complete list - 10 202 Bytes
HEADER ELECTRON TRANSPORT 25-FEB-94 1CCH
TITLE THE SOLUTION CONFORMATION OF CYTOCHROME C-551 FROM P.STUTZERI ZOBELL
TITLE 2 DETERMINED BY NMR+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C551;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI;
SOURCE 3 ORGANISM_TAXID: 316
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR M.CAI,R.TIMKOVICH
REVDAT 3 10-MAR-21 1CCH 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK ATOM
REVDAT 2 24-FEB-09 1CCH 1 VERSN
REVDAT 1 30-APR-94 1CCH 0
JRNL AUTH M.CAI,E.G.BRADFORD,R.TIMKOVICH
JRNL TITL INVESTIGATION OF THE SOLUTION CONFORMATION OF CYTOCHROME
JRNL TITL 2 C-551 FROM PSEUDOMONAS STUTZERI.
JRNL REF BIOCHEMISTRY V. 31 8603 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1327105
JRNL DOI 10.1021/BI00151A030
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172229.
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 : 1
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 TRP A 77 CG TRP A 77 CD2 -0.105
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 TRP A 56 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 56 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 56 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 TRP A 56 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP A 77 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP A 77 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 77 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 TRP A 77 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 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 LYS A 8 -71.38 -66.89
REMARK 500 PRO A 11 -4.61 -54.25
REMARK 500 THR A 20 -125.20 -157.57
REMARK 500 LYS A 21 159.95 168.01
REMARK 500 MET A 22 -56.69 -148.87
REMARK 500 TRP A 56 -43.85 -134.63
REMARK 500 PRO A 58 27.16 -67.57
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 HEC A 83 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 HEC A 83 NA 89.4
REMARK 620 3 HEC A 83 NB 90.3 89.9
REMARK 620 4 HEC A 83 NC 90.2 179.6 89.9
REMARK 620 5 HEC A 83 ND 89.3 90.1 179.6 90.0
REMARK 620 6 MET A 61 SD 179.4 90.2 90.2 90.2 90.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 83
DBREF 1CCH A 1 82 UNP P00101 CY551_PSEST 23 104
SEQRES 1 A 82 GLN ASP GLY GLU ALA LEU PHE LYS SER LYS PRO CYS ALA
SEQRES 2 A 82 ALA CYS HIS SER VAL ASP THR LYS MET VAL GLY PRO ALA
SEQRES 3 A 82 LEU LYS GLU VAL ALA ALA LYS ASN ALA GLY VAL GLU GLY
SEQRES 4 A 82 ALA ALA ASP THR LEU ALA LEU HIS ILE LYS ASN GLY SER
SEQRES 5 A 82 GLN GLY VAL TRP GLY PRO ILE PRO MET PRO PRO ASN PRO
SEQRES 6 A 82 VAL THR GLU GLU GLU ALA LYS ILE LEU ALA GLU TRP VAL
SEQRES 7 A 82 LEU SER LEU LYS
HET HEC A 83 43
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 A1 GLU A 4 SER A 9 1 6
HELIX 2 A2 LEU A 27 LYS A 33 1 7
HELIX 3 A3 ALA A 40 LYS A 49 1 10
HELIX 4 A4 GLU A 69 LEU A 79 1 11
HELIX 5 P1 GLY A 24 ALA A 26 10A VERY SHORT PROLINE HELIX 3
HELIX 6 P2 ILE A 59 PRO A 63 10 5
LINK SG CYS A 12 CAB HEC A 83 1555 1555 1.81
LINK SG CYS A 15 CAC HEC A 83 1555 1555 1.82
LINK NE2 HIS A 16 FE HEC A 83 1555 1555 1.95
LINK SD MET A 61 FE HEC A 83 1555 1555 2.38
SITE 1 AC1 17 CYS A 12 CYS A 15 HIS A 16 LEU A 44
SITE 2 AC1 17 HIS A 47 ILE A 48 SER A 52 GLN A 53
SITE 3 AC1 17 GLY A 54 VAL A 55 TRP A 56 GLY A 57
SITE 4 AC1 17 ILE A 59 MET A 61 PRO A 62 ASN A 64
SITE 5 AC1 17 VAL A 66
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
Complete list - 10 202 Bytes