Header list of 1ayg.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 04-NOV-97 1AYG
TITLE SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-552;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: C-TYPE CYTOCHROME (REDUCED FORM)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYDROGENOBACTER THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 940;
SOURCE 4 STRAIN: TK-6;
SOURCE 5 CELLULAR_LOCATION: PERIPLASM
KEYWDS CYTOCHROME C, ELECTRON TRANSPORT, PORPHYRIN, FERROUS IRON
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.HASEGAWA,T.YOSHIDA,T.YAMAZAKI,Y.SAMBONGI,Y.YU,Y.IGARASHI,T.KODAMA,
AUTHOR 2 K.YAMAZAKI,H.HAKUSUI,Y.KYOGOKU,Y.KOBAYASHI
REVDAT 4 16-FEB-22 1AYG 1 REMARK LINK
REVDAT 3 24-FEB-09 1AYG 1 VERSN
REVDAT 2 13-JAN-99 1AYG 1 HET SOURCE REMARK TITLE
REVDAT 2 2 1 HEADER
REVDAT 1 25-NOV-98 1AYG 0
JRNL AUTH J.HASEGAWA,T.YOSHIDA,T.YAMAZAKI,Y.SAMBONGI,Y.YU,Y.IGARASHI,
JRNL AUTH 2 T.KODAMA,K.YAMAZAKI,Y.KYOGOKU,Y.KOBAYASHI
JRNL TITL SOLUTION STRUCTURE OF THERMOSTABLE CYTOCHROME C-552 FROM
JRNL TITL 2 HYDROGENOBACTER THERMOPHILUS DETERMINED BY 1H-NMR
JRNL TITL 3 SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 37 9641 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9657676
JRNL DOI 10.1021/BI9803067
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING REFINEMENT FOR NMR
REMARK 3 STRUCTURE DETERMINATION.
REMARK 4
REMARK 4 1AYG 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_1000171409.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : 120MM ACETATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O, OR 99.98% D2O
REMARK 210 CONTAINING 120MM DEUTERATED
REMARK 210 ACETATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; E.COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : ARX500; AMX500 & DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWER ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-NMR SPECTROSCOPY ON
REMARK 210 CYTOCHROME C-552
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: 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 GLU A 2 -41.75 -157.07
REMARK 500 1 ASP A 15 148.74 163.63
REMARK 500 1 LEU A 16 -75.68 -50.39
REMARK 500 1 ALA A 18 67.58 -118.39
REMARK 500 1 LYS A 20 -95.72 -128.96
REMARK 500 1 VAL A 21 -72.81 -94.27
REMARK 500 1 ALA A 33 109.91 163.59
REMARK 500 1 LEU A 42 -70.87 -56.78
REMARK 500 1 LYS A 48 -59.97 -129.79
REMARK 500 1 SER A 51 167.65 179.50
REMARK 500 1 ASN A 63 78.07 -104.09
REMARK 500 2 GLU A 2 -40.08 -178.69
REMARK 500 2 ASP A 15 136.12 161.07
REMARK 500 2 LYS A 20 -56.46 -140.39
REMARK 500 2 TYR A 32 -132.57 -109.94
REMARK 500 2 ALA A 33 107.67 78.50
REMARK 500 2 ASP A 37 39.08 -94.27
REMARK 500 2 LEU A 42 -70.09 -65.14
REMARK 500 2 SER A 51 56.50 169.49
REMARK 500 2 VAL A 57 106.98 -50.01
REMARK 500 3 GLN A 3 -42.62 173.06
REMARK 500 3 HIS A 14 -169.38 -108.39
REMARK 500 3 ASP A 15 135.95 162.69
REMARK 500 3 TYR A 32 -115.57 -96.61
REMARK 500 3 ALA A 33 106.97 76.66
REMARK 500 3 ASN A 63 57.22 -104.57
REMARK 500 4 GLN A 3 -43.29 82.73
REMARK 500 4 HIS A 14 -171.39 -69.87
REMARK 500 4 ASP A 15 132.28 169.98
REMARK 500 4 LEU A 16 -70.05 -42.65
REMARK 500 4 ALA A 18 59.46 -153.70
REMARK 500 4 LYS A 19 101.79 -48.92
REMARK 500 4 ALA A 33 -32.81 170.47
REMARK 500 4 VAL A 57 104.60 -46.17
REMARK 500 4 ASN A 63 55.15 -96.32
REMARK 500 5 GLN A 3 -75.29 168.65
REMARK 500 5 ASP A 15 23.27 -160.44
REMARK 500 5 LEU A 16 -59.32 81.36
REMARK 500 5 LYS A 19 97.09 -51.17
REMARK 500 5 LYS A 20 -89.37 -113.16
REMARK 500 5 ILE A 46 -60.03 -102.20
REMARK 500 5 SER A 51 150.76 179.81
REMARK 500 5 VAL A 57 107.61 -43.66
REMARK 500 5 GLN A 62 -162.79 -100.46
REMARK 500 5 ASN A 63 65.84 -117.69
REMARK 500 5 ILE A 79 100.05 -47.85
REMARK 500 6 GLU A 2 -44.20 -176.41
REMARK 500 6 LYS A 6 -73.75 -88.92
REMARK 500 6 ASP A 15 139.66 -178.94
REMARK 500 6 ALA A 18 109.01 53.86
REMARK 500
REMARK 500 THIS ENTRY HAS 197 RAMACHANDRAN OUTLIERS.
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 81 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 14 NE2
REMARK 620 2 HEC A 81 NA 72.8
REMARK 620 3 HEC A 81 NB 105.3 90.0
REMARK 620 4 HEC A 81 NC 105.8 178.5 90.0
REMARK 620 5 HEC A 81 ND 74.4 90.2 179.7 89.9
REMARK 620 N 1 2 3 4
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 81
DBREF 1AYG A 1 80 UNP P15452 CY552_HYDTH 19 98
SEQRES 1 A 80 ASN GLU GLN LEU ALA LYS GLN LYS GLY CYS MET ALA CYS
SEQRES 2 A 80 HIS ASP LEU LYS ALA LYS LYS VAL GLY PRO ALA TYR ALA
SEQRES 3 A 80 ASP VAL ALA LYS LYS TYR ALA GLY ARG LYS ASP ALA VAL
SEQRES 4 A 80 ASP TYR LEU ALA GLY LYS ILE LYS LYS GLY GLY SER GLY
SEQRES 5 A 80 VAL TRP GLY SER VAL PRO MET PRO PRO GLN ASN VAL THR
SEQRES 6 A 80 ASP ALA GLU ALA LYS GLN LEU ALA GLN TRP ILE LEU SER
SEQRES 7 A 80 ILE LYS
HET HEC A 81 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 GLN A 3 GLN A 7 1 5
HELIX 2 2 TYR A 25 TYR A 32 1 8
HELIX 3 3 ALA A 38 LYS A 47 1 10
HELIX 4 4 ALA A 67 SER A 78 1 12
LINK SG CYS A 10 CAB HEC A 81 1555 1555 1.81
LINK SG CYS A 13 CAC HEC A 81 1555 1555 1.81
LINK NE2 HIS A 14 FE HEC A 81 1555 1555 2.98
SITE 1 AC1 14 GLY A 9 CYS A 10 CYS A 13 HIS A 14
SITE 2 AC1 14 PRO A 23 TYR A 32 ILE A 46 GLY A 52
SITE 3 AC1 14 TRP A 54 GLY A 55 VAL A 57 MET A 59
SITE 4 AC1 14 GLN A 62 LEU A 72
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 - b 16 2 Bytes