Header list of 1b5b.pdb file
Complete list - 8 20 Bytes
HEADER ELECTRON TRANSPORT 06-APR-98 1B5B
TITLE RAT FERROCYTOCHROME B5 B CONFORMATION, NMR, 1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERROCYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: HEME AS PROSTHETIC GROUP, WITH H63 AND H39 AS AXIAL
COMPND 6 LIGANDS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3C
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR B.DANGI,S.SARMA,C.YAN,D.BANVILLE,R.D.GUILES
REVDAT 4 08-AUG-18 1B5B 1 SOURCE REMARK
REVDAT 3 29-NOV-17 1B5B 1 REMARK HELIX
REVDAT 2 24-FEB-09 1B5B 1 VERSN
REVDAT 1 17-JUN-98 1B5B 0
JRNL AUTH B.DANGI,S.SARMA,C.YAN,D.L.BANVILLE,R.D.GUILES
JRNL TITL THE ORIGIN OF DIFFERENCES IN THE PHYSICAL PROPERTIES OF THE
JRNL TITL 2 EQUILIBRIUM FORMS OF CYTOCHROME B5 REVEALED THROUGH
JRNL TITL 3 HIGH-RESOLUTION NMR STRUCTURES AND BACKBONE DYNAMIC
JRNL TITL 4 ANALYSES.
JRNL REF BIOCHEMISTRY V. 37 8289 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9622481
JRNL DOI 10.1021/BI9801964
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B5B 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_1000171487.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : [U-13C; U-15N] CYTOCHROME B5,
REMARK 210 100 MM PHOSPHATE BUFFER, 0.5 MM
REMARK 210 TSP, PH 7.0, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; N15 3D
REMARK 210 NOESY-HMQC; N15 3D TOCSY-HMQC;
REMARK 210 3D HCCH-TOCSY; HNCO; CBCA(CO)NH;
REMARK 210 HSQC; HCACO< HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA 2.1, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO THE AVERAGE
REMARK 210 STRUCTURE, LOW TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE REPRESENTS THE A CONFORMATION OF THE RAT
REMARK 210 FERROCYTOCHROME B5. IT IS THE STRUCTURE CLOSEST TO THE
REMARK 210 AVERAGE AS ANALYZED BY X-PLOR. 200 STRUCTURES WERE
REMARK 210 CALCULATED USING DIANA 2.1 AND ONE STRUCTURE WAS CHOSEN TO
REMARK 210 REPRESENT THE FINAL RESULTS. THE STRUCTURE WAS DETERMINED USING 2D
REMARK 210 AND 3D EXPERIMENTS
REMARK 210 INCLUDING DISTANCE AND ANGULAR RESTRAINTS FROM HNHA.
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 O GLU A 44 H GLU A 48 1.49
REMARK 500 O TRP A 22 H GLY A 51 1.52
REMARK 500 O TYR A 7 H HIS A 80 1.58
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 ASP A 3 -57.58 76.32
REMARK 500 VAL A 4 159.54 -43.86
REMARK 500 HIS A 27 46.27 35.67
REMARK 500 PRO A 40 23.97 -75.03
REMARK 500 HIS A 63 133.55 -39.58
REMARK 500 TYR A 74 48.19 -92.27
REMARK 500 HIS A 80 145.92 -38.95
REMARK 500 ALA A 88 -76.28 67.23
REMARK 500 LYS A 89 123.27 171.99
REMARK 500 SER A 91 105.24 55.37
REMARK 500 GLU A 92 169.10 68.04
REMARK 500 THR A 93 -49.14 -160.38
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 HEM A 95 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 95 NA 86.6
REMARK 620 3 HEM A 95 NB 92.1 90.8
REMARK 620 4 HEM A 95 NC 94.0 179.1 89.8
REMARK 620 5 HEM A 95 ND 88.5 89.7 179.3 89.7
REMARK 620 6 HIS A 63 NE2 170.9 99.4 81.2 80.0 98.2
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 HEM A 95
DBREF 1B5B A 1 94 UNP P00173 CYB5_RAT 5 98
SEQRES 1 A 94 ASP LYS ASP VAL LYS TYR TYR THR LEU GLU GLU ILE GLN
SEQRES 2 A 94 LYS HIS LYS ASP SER LYS SER THR TRP VAL ILE LEU HIS
SEQRES 3 A 94 HIS LYS VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS
SEQRES 4 A 94 PRO GLY GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY
SEQRES 5 A 94 ASP ALA THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR
SEQRES 6 A 94 ASP ALA ARG GLU LEU SER LYS THR TYR ILE ILE GLY GLU
SEQRES 7 A 94 LEU HIS PRO ASP ASP ARG SER LYS ILE ALA LYS PRO SER
SEQRES 8 A 94 GLU THR LEU
HET HEM A 95 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 I LEU A 9 ILE A 12 1 4
HELIX 2 II THR A 33 GLU A 38 1 6
HELIX 3 III GLU A 44 ARG A 47 1 4
HELIX 4 IV ASP A 53 ASP A 60 1 8
HELIX 5 V THR A 65 SER A 71 1 7
HELIX 6 VI PRO A 81 LYS A 86 5 6
SHEET 1 I 5 LYS A 5 TYR A 7 0
SHEET 2 I 5 TYR A 74 HIS A 80 1 N GLU A 78 O LYS A 5
SHEET 3 I 5 HIS A 27 LEU A 32 -1 O HIS A 27 N LEU A 79
SHEET 4 I 5 THR A 21 LEU A 25 -1 O THR A 21 N LEU A 32
SHEET 5 I 5 GLY A 51 ALA A 54 1 N GLY A 51 O TRP A 22
LINK FE HEM A 95 NE2 HIS A 39 1555 1555 1.92
LINK FE HEM A 95 NE2 HIS A 63 1555 1555 2.01
SITE 1 AC1 13 VAL A 23 PHE A 35 HIS A 39 PRO A 40
SITE 2 AC1 13 GLY A 41 VAL A 45 LEU A 46 ALA A 54
SITE 3 AC1 13 ASN A 57 VAL A 61 HIS A 63 SER A 64
SITE 4 AC1 13 SER A 71
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 - 8 20 Bytes