Header list of 1f04.pdb file
Complete list - v 3 2 Bytes
HEADER ELECTRON TRANSPORT 14-MAY-00 1F04
TITLE SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT
TITLE 2 (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C
CAVEAT 1F04 CHIRALITY ERROR AT CA ATOM OF ALA A 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM83;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC 19
KEYWDS CYTOCHROME B5, PROTEIN RECOGNITION, SOLUTION STRUCTURE, PARAMAGNETIC
KEYWDS 2 NMR, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR Y.B.WU,J.LU,C.M.QIAN,W.X.TANG,E.C.LI,J.F.WANG,Y.H.WANG,W.H.WANG,
AUTHOR 2 J.X.LU,Y.XIE,Z.X.HUANG
REVDAT 5 03-NOV-21 1F04 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1F04 1 VERSN
REVDAT 3 01-APR-03 1F04 1 JRNL
REVDAT 2 23-MAY-01 1F04 1 JRNL
REVDAT 1 21-JUN-00 1F04 0
JRNL AUTH Y.WU,Y.WANG,C.QIAN,J.LU,E.LI,W.WANG,J.LU,Y.XIE,J.WANG,D.ZHU,
JRNL AUTH 2 Z.HUANG,W.TANG
JRNL TITL SOLUTION STRUCTURE OF CYTOCHROME B(5) MUTANT
JRNL TITL 2 (E44/48/56A/D60A) AND ITS INTERACTION WITH CYTOCHROME C.
JRNL REF EUR.J.BIOCHEM. V. 268 1620 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11248680
JRNL DOI 10.1046/J.1432-1327.2001.02033.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 5.0, AMBER 5.0, PSEUDOREM
REMARK 3 AUTHORS : GNTERT, MUMENTHALER, WTHRICH (DYANA), PEARLMAN,
REMARK 3 CASE, CALDWELL, ROSS, CHEATHAM, FERGUSON, SEIBEL,
REMARK 3 SINGH, WEINER, KOLLMAN (AMBER), BANCI, BERTINI,
REMARK 3 GORI SAVELLINI, ROMAGNOLI, TURANO, CREMONINI,
REMARK 3 LUCHINAT, GARY (PSEUDOREM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DYNAMICS SIMULATED ANNEALING,
REMARK 3 RESTRAINED ENERGY MINIMIZATION; PSEUDOCONTACT SHIFTS WERE USED
REMARK 3 IN THE CALCULATION AND IN THE MINIMIZATION AS FURTHER NON-
REMARK 3 CLASSICAL CONSTRAINTS
REMARK 4
REMARK 4 1F04 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011080.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 6 MM CYTOCHROME B5 MUTANT 1H; 6
REMARK 210 MM CYTOCHROME B5 MUTANT 1H
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PSEUDODYANA
REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 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 8 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 23 ASP A 83 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 27 ASP A 83 CB - CG - OD2 ANGL. DEV. = -5.5 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 1 ASN A 16 68.63 -162.97
REMARK 500 1 ASN A 17 -66.88 -130.20
REMARK 500 1 SER A 18 -66.21 -144.17
REMARK 500 1 LYS A 19 -63.18 -90.63
REMARK 500 1 SER A 20 107.31 -52.24
REMARK 500 1 LYS A 34 38.89 -96.68
REMARK 500 1 GLU A 43 94.66 -53.50
REMARK 500 1 ALA A 44 -69.85 179.61
REMARK 500 1 HIS A 63 156.84 63.75
REMARK 500 2 ASN A 16 -44.57 -131.77
REMARK 500 2 LYS A 19 -51.41 176.95
REMARK 500 2 ASP A 53 72.53 8.12
REMARK 500 2 VAL A 61 54.60 -107.45
REMARK 500 3 ASN A 16 29.75 -140.95
REMARK 500 3 SER A 18 -67.49 65.66
REMARK 500 3 LYS A 19 -44.24 -158.39
REMARK 500 3 SER A 20 99.85 -46.10
REMARK 500 3 LEU A 23 168.58 176.98
REMARK 500 3 LYS A 34 36.59 -96.65
REMARK 500 3 PHE A 35 12.34 -140.10
REMARK 500 3 GLU A 43 103.27 -42.39
REMARK 500 3 ALA A 44 -66.67 170.68
REMARK 500 3 HIS A 63 123.42 67.18
REMARK 500 4 HIS A 15 67.62 -113.41
REMARK 500 4 ASN A 16 63.53 -154.32
REMARK 500 4 ASN A 17 -56.55 -149.00
REMARK 500 4 SER A 18 -53.64 -172.76
REMARK 500 4 HIS A 63 89.77 54.45
REMARK 500 5 HIS A 15 62.69 -102.79
REMARK 500 5 ASN A 16 62.68 -177.00
REMARK 500 5 ASN A 17 84.74 -173.11
REMARK 500 5 LYS A 19 -82.15 -160.44
REMARK 500 5 LYS A 34 32.49 -97.77
REMARK 500 5 PHE A 35 14.98 -140.76
REMARK 500 5 HIS A 39 107.32 -54.84
REMARK 500 5 ASP A 53 35.56 -158.60
REMARK 500 6 ASN A 16 66.05 -160.95
REMARK 500 6 ASN A 17 -65.71 -155.28
REMARK 500 6 SER A 18 -48.15 -160.37
REMARK 500 6 ASP A 53 70.69 8.57
REMARK 500 7 SER A 18 -142.92 57.13
REMARK 500 7 SER A 20 108.67 -56.14
REMARK 500 7 LEU A 23 168.35 177.65
REMARK 500 7 PHE A 35 11.81 -146.55
REMARK 500 7 GLU A 43 81.91 -65.78
REMARK 500 7 ALA A 44 -71.05 -163.41
REMARK 500 7 HIS A 63 103.89 62.27
REMARK 500 8 SER A 18 70.27 -63.57
REMARK 500 8 LYS A 19 -40.00 -176.45
REMARK 500 8 TYR A 27 -0.23 67.52
REMARK 500
REMARK 500 THIS ENTRY HAS 235 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 3 VAL A 4 3 143.63
REMARK 500 ALA A 3 VAL A 4 11 147.20
REMARK 500 ALA A 3 VAL A 4 17 141.53
REMARK 500 ALA A 3 VAL A 4 18 139.74
REMARK 500 ALA A 3 VAL A 4 21 148.52
REMARK 500 ALA A 3 VAL A 4 25 141.99
REMARK 500 ALA A 3 VAL A 4 27 145.25
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 2 TYR A 30 0.06 SIDE CHAIN
REMARK 500 8 TYR A 30 0.13 SIDE CHAIN
REMARK 500 9 TYR A 6 0.08 SIDE CHAIN
REMARK 500 9 TYR A 27 0.11 SIDE CHAIN
REMARK 500 10 ARG A 47 0.09 SIDE CHAIN
REMARK 500 12 TYR A 27 0.08 SIDE CHAIN
REMARK 500 25 TYR A 6 0.07 SIDE CHAIN
REMARK 500 25 TYR A 7 0.08 SIDE CHAIN
REMARK 500 27 TYR A 6 0.07 SIDE CHAIN
REMARK 500 28 TYR A 27 0.07 SIDE CHAIN
REMARK 500 29 TYR A 27 0.07 SIDE CHAIN
REMARK 500 30 TYR A 27 0.07 SIDE CHAIN
REMARK 500 31 TYR A 27 0.09 SIDE CHAIN
REMARK 500 31 TYR A 30 0.10 SIDE CHAIN
REMARK 500 32 HIS A 63 0.19 SIDE CHAIN
REMARK 500 34 ARG A 68 0.08 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 HEM A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 201 NA 89.4
REMARK 620 3 HEM A 201 NB 93.5 91.4
REMARK 620 4 HEM A 201 NC 91.2 179.3 88.7
REMARK 620 5 HEM A 201 ND 87.7 91.7 176.6 88.1
REMARK 620 6 HIS A 63 NE2 175.6 89.9 90.9 89.4 87.9
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F03 RELATED DB: PDB
DBREF 1F04 A 3 84 UNP P00171 CYB5_BOVIN 7 88
SEQADV 1F04 ALA A 44 UNP P00171 GLU 48 ENGINEERED MUTATION
SEQADV 1F04 ALA A 48 UNP P00171 GLU 52 ENGINEERED MUTATION
SEQADV 1F04 ALA A 56 UNP P00171 GLU 60 ENGINEERED MUTATION
SEQADV 1F04 ALA A 60 UNP P00171 ASP 64 ENGINEERED MUTATION
SEQRES 1 A 82 ALA VAL LYS TYR TYR THR LEU GLU GLU ILE GLN LYS HIS
SEQRES 2 A 82 ASN ASN SER LYS SER THR TRP LEU ILE LEU HIS TYR LYS
SEQRES 3 A 82 VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS PRO GLY
SEQRES 4 A 82 GLY GLU ALA VAL LEU ARG ALA GLN ALA GLY GLY ASP ALA
SEQRES 5 A 82 THR ALA ASN PHE GLU ALA VAL GLY HIS SER THR ASP ALA
SEQRES 6 A 82 ARG GLU LEU SER LYS THR PHE ILE ILE GLY GLU LEU HIS
SEQRES 7 A 82 PRO ASP ASP ARG
HET HEM A 201 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 THR A 8 LYS A 14 1 7
HELIX 2 2 LEU A 32 LEU A 36 5 5
HELIX 3 3 ALA A 44 ALA A 50 1 7
HELIX 4 4 ALA A 54 GLY A 62 1 9
HELIX 5 5 SER A 64 PHE A 74 1 11
SHEET 1 A 2 LYS A 28 TYR A 30 0
SHEET 2 A 2 ILE A 75 GLU A 78 -1 N ILE A 76 O VAL A 29
LINK NE2 HIS A 39 FE HEM A 201 1555 1555 2.01
LINK NE2 HIS A 63 FE HEM A 201 1555 1555 2.00
SITE 1 AC1 13 LEU A 25 LEU A 32 HIS A 39 PRO A 40
SITE 2 AC1 13 VAL A 45 LEU A 46 GLN A 49 PHE A 58
SITE 3 AC1 13 VAL A 61 HIS A 63 SER A 64 LEU A 70
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
MODEL 1
Complete list - v 3 2 Bytes