Header list of 1axx.pdb file
Complete list - r 23 2 Bytes
HEADER ELECTRON TRANSPORT 22-OCT-97 1AXX
TITLE THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR,
TITLE 2 19 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: FROM RAT MICROSOMAL MEMBRANE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 ORGANELLE: MICROSOME;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: NM522;
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PUC 13
KEYWDS CYTOCHROME B5, PROTEIN RECOGNITION, ELECTRON TRANSPORT, SOLUTION
KEYWDS 2 STRUCTURE, PARAMAGNETIC NMR
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,I.C.FELLI
REVDAT 3 23-MAR-22 1AXX 1 REMARK LINK
REVDAT 2 24-FEB-09 1AXX 1 VERSN
REVDAT 1 04-MAR-98 1AXX 0
JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,I.C.FELLI
JRNL TITL THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME
JRNL TITL 2 B5.
JRNL REF BIOCHEMISTRY V. 37 173 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9425037
JRNL DOI 10.1021/BI971896W
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PSEUDOREM (BANCI,BERTINI, GORI
REMARK 3 SAVELLINI,ROMAGNOLI,TURANO,CREMONINI,LUCHINAT, GRAY) ALSO WAS
REMARK 3 USED.
REMARK 4
REMARK 4 1AXX 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_1000171391.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 1 MM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; 1D NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE 800 MHZ
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, PSEUDYANA, AMBER
REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR DYNAMICS
REMARK 210 SIMULATED ANNEALING, RESTRAINED
REMARK 210 ENERGY MINIMIZATION;
REMARK 210 PSEUDOCONTACT SHIFTS WERE USED
REMARK 210 IN THE CALCULATION AND IN THE
REMARK 210 MINIMIZATION AS FURTHER NON-
REMARK 210 CLASSICAL CONSTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : FAMILY OF MINIMIZED STRUCTURES
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 4 ASP A 1 N - CA - CB ANGL. DEV. = 21.9 DEGREES
REMARK 500 9 ASP A 1 CB - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 9 ASP A 1 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 9 ASP A 1 N - CA - C ANGL. DEV. = -18.5 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 ASP A 3 177.57 -58.81
REMARK 500 1 VAL A 4 -125.18 -74.17
REMARK 500 1 LYS A 16 49.16 -152.28
REMARK 500 1 SER A 18 -83.06 56.50
REMARK 500 1 LYS A 19 42.39 -159.54
REMARK 500 1 HIS A 26 -163.30 58.70
REMARK 500 1 PRO A 40 78.00 -69.12
REMARK 500 1 GLN A 49 -68.90 -96.23
REMARK 500 1 ALA A 50 153.90 59.20
REMARK 500 1 HIS A 63 150.07 65.22
REMARK 500 1 ASP A 83 34.51 -82.43
REMARK 500 2 VAL A 4 -152.84 -101.77
REMARK 500 2 LYS A 16 44.84 -154.58
REMARK 500 2 SER A 18 -77.04 68.70
REMARK 500 2 LYS A 19 65.72 -172.42
REMARK 500 2 GLN A 49 -69.25 -94.21
REMARK 500 2 ALA A 50 154.48 56.58
REMARK 500 2 ASP A 53 72.64 -64.44
REMARK 500 2 LYS A 86 46.62 -83.14
REMARK 500 3 LYS A 2 -71.47 -78.15
REMARK 500 3 ASP A 3 -145.29 51.93
REMARK 500 3 VAL A 4 -100.20 -87.84
REMARK 500 3 LYS A 5 37.28 -150.11
REMARK 500 3 TYR A 6 114.07 -37.06
REMARK 500 3 SER A 18 -150.39 53.21
REMARK 500 3 GLN A 49 -63.88 -103.36
REMARK 500 3 ALA A 50 165.77 58.91
REMARK 500 3 ASP A 53 83.00 -63.88
REMARK 500 3 HIS A 63 155.24 -47.08
REMARK 500 3 ASP A 82 -56.91 -29.70
REMARK 500 4 LYS A 2 161.12 66.86
REMARK 500 4 ASP A 3 -167.58 61.46
REMARK 500 4 VAL A 4 -117.45 -92.05
REMARK 500 4 LYS A 16 58.12 -143.53
REMARK 500 4 SER A 18 70.12 -67.77
REMARK 500 4 LYS A 19 -46.48 -171.34
REMARK 500 4 HIS A 26 -83.40 58.27
REMARK 500 4 HIS A 27 31.78 -147.64
REMARK 500 4 ALA A 50 150.98 -41.19
REMARK 500 4 ASP A 53 94.81 -68.26
REMARK 500 4 LYS A 86 55.83 -146.32
REMARK 500 4 GLU A 92 -158.49 41.82
REMARK 500 5 ASP A 3 -142.74 47.43
REMARK 500 5 VAL A 4 -101.96 -75.77
REMARK 500 5 LYS A 5 43.67 -143.73
REMARK 500 5 LYS A 16 -45.70 -154.90
REMARK 500 5 SER A 18 -61.38 71.67
REMARK 500 5 LYS A 19 -26.65 171.49
REMARK 500 5 SER A 20 71.58 -66.68
REMARK 500 5 PRO A 40 79.16 -69.93
REMARK 500
REMARK 500 THIS ENTRY HAS 227 RAMACHANDRAN OUTLIERS.
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 1 TYR A 30 0.12 SIDE CHAIN
REMARK 500 1 TYR A 74 0.10 SIDE CHAIN
REMARK 500 2 TYR A 74 0.08 SIDE CHAIN
REMARK 500 3 TYR A 74 0.09 SIDE CHAIN
REMARK 500 4 TYR A 6 0.07 SIDE CHAIN
REMARK 500 6 TYR A 74 0.10 SIDE CHAIN
REMARK 500 7 TYR A 30 0.07 SIDE CHAIN
REMARK 500 7 TYR A 74 0.09 SIDE CHAIN
REMARK 500 8 TYR A 74 0.09 SIDE CHAIN
REMARK 500 9 TYR A 6 0.10 SIDE CHAIN
REMARK 500 9 TYR A 74 0.09 SIDE CHAIN
REMARK 500 10 TYR A 6 0.10 SIDE CHAIN
REMARK 500 11 TYR A 30 0.11 SIDE CHAIN
REMARK 500 11 TYR A 74 0.09 SIDE CHAIN
REMARK 500 12 TYR A 30 0.08 SIDE CHAIN
REMARK 500 13 TYR A 6 0.09 SIDE CHAIN
REMARK 500 14 TYR A 6 0.09 SIDE CHAIN
REMARK 500 14 TYR A 74 0.08 SIDE CHAIN
REMARK 500 15 TYR A 30 0.07 SIDE CHAIN
REMARK 500 16 TYR A 74 0.08 SIDE CHAIN
REMARK 500 17 TYR A 7 0.07 SIDE CHAIN
REMARK 500 17 TYR A 30 0.08 SIDE CHAIN
REMARK 500 17 TYR A 74 0.09 SIDE CHAIN
REMARK 500 18 TYR A 30 0.06 SIDE CHAIN
REMARK 500 19 TYR A 74 0.07 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 96 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 96 NA 90.7
REMARK 620 3 HEM A 96 NB 91.7 88.8
REMARK 620 4 HEM A 96 NC 89.5 179.5 90.7
REMARK 620 5 HEM A 96 ND 88.2 91.2 179.9 89.3
REMARK 620 6 HIS A 63 NE2 175.2 92.2 92.2 87.6 87.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEME SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 96
DBREF 1AXX 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 96 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 THR A 33 HIS A 39 5 7
HELIX 3 3 GLY A 42 ALA A 50 1 9
HELIX 4 4 ALA A 54 GLY A 62 1 9
HELIX 5 5 SER A 64 TYR A 74 1 11
HELIX 6 6 PRO A 81 ILE A 87 1 7
SHEET 1 A 4 THR A 21 LEU A 25 0
SHEET 2 A 4 LYS A 28 LEU A 32 -1 N TYR A 30 O VAL A 23
SHEET 3 A 4 ILE A 75 GLU A 78 -1 N GLY A 77 O VAL A 29
SHEET 4 A 4 LYS A 5 TYR A 7 1 N TYR A 7 O GLU A 78
LINK NE2 HIS A 39 FE HEM A 96 1555 1555 1.99
LINK NE2 HIS A 63 FE HEM A 96 1555 1555 2.00
SITE 1 NUL 2 HIS A 39 HIS A 63
SITE 1 AC1 13 LEU A 25 LEU A 32 PHE A 35 HIS A 39
SITE 2 AC1 13 PRO A 40 GLY A 41 VAL A 45 LEU A 46
SITE 3 AC1 13 ASN A 57 HIS A 63 SER A 64 ALA A 67
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 - r 23 2 Bytes