Header list of 1s05.pdb file
Complete list - 3 20 Bytes
HEADER ELECTRON TRANSPORT 30-DEC-03 1S05
TITLE NMR-VALIDATED STRUCTURAL MODEL FOR OXIDIZED R.PALUSTRIS CYTOCHROME
TITLE 2 C556
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-556;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C556;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEE-PET, PEC86
KEYWDS THIS IS A MODEL OBTAINED BY NMR-RESTRAINED MODELING AND
KEYWDS 2 MINIMIZATION., ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR I.BERTINI,J.FARAONE-MENNELLA,H.B.GRAY,C.LUCHINAT,G.PARIGI,J.R.WINKLER
REVDAT 4 03-MAR-21 1S05 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 HETSYN FORMUL LINK ATOM
REVDAT 3 24-FEB-09 1S05 1 VERSN
REVDAT 2 09-MAR-04 1S05 1 JRNL
REVDAT 1 20-JAN-04 1S05 0
JRNL AUTH I.BERTINI,J.FARAONE-MENNELLA,H.B.GRAY,C.LUCHINAT,G.PARIGI,
JRNL AUTH 2 J.R.WINKLER
JRNL TITL NMR-VALIDATED STRUCTURAL MODEL FOR OXIDIZED RHODOPSEUDOMONAS
JRNL TITL 2 PALUSTRIS CYTOCHROME C(556).
JRNL REF J.BIOL.INORG.CHEM. V. 9 224 2004
JRNL REFN ISSN 0949-8257
JRNL PMID 14735333
JRNL DOI 10.1007/S00775-003-0511-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PARAMAGNETIC DYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021199.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 294
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : 0.5 M PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3 MM CYTTOCROME C556 15N, 0.5M
REMARK 210 PHOSPHATE BUFFER,
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D 15N HSQC TOCSY; 3D
REMARK 210 15N HSQC NOESY; 1D NOE; 1J
REMARK 210 MODULATED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MODELLER 4.0, PARAMAGNETIC DYANA
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 : 1
REMARK 210
REMARK 210 REMARK: THIS IS A MODEL STRUCTURE VALIDATED BY NMR CONSTRAINTS
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 78 H PHE A 82 1.38
REMARK 500 O ALA A 24 H GLY A 28 1.54
REMARK 500 O PRO A 112 H LYS A 115 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 LEU A 4 -50.59 -124.12
REMARK 500 LYS A 30 145.43 55.92
REMARK 500 PRO A 31 49.78 -75.06
REMARK 500 TYR A 32 163.38 54.70
REMARK 500 ASP A 33 -59.53 -131.00
REMARK 500 GLN A 34 -52.95 89.76
REMARK 500 LYS A 53 -40.82 -166.99
REMARK 500 VAL A 59 56.81 -141.10
REMARK 500 LYS A 60 -84.40 -122.18
REMARK 500 LEU A 62 9.83 93.33
REMARK 500 LYS A 63 -51.06 162.08
REMARK 500 LYS A 68 -52.44 -165.56
REMARK 500 TYR A 69 166.29 -49.26
REMARK 500 ARG A 79 -39.46 -36.53
REMARK 500 ILE A 100 147.26 -39.27
REMARK 500 LYS A 101 -40.25 -171.50
REMARK 500 ARG A 125 87.09 177.91
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 130 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 12 SD
REMARK 620 2 HEC A 130 NA 103.3
REMARK 620 3 HEC A 130 NB 102.1 93.1
REMARK 620 4 HEC A 130 NC 81.3 172.6 91.5
REMARK 620 5 HEC A 130 ND 79.7 85.8 178.0 89.5
REMARK 620 6 HIS A 121 NE2 171.3 68.1 77.5 107.4 100.6
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 130
DBREF 1S05 A 1 129 UNP P00150 C556_RHOPA 1 129
SEQRES 1 A 129 GLN GLN ASP LEU VAL ASP LYS THR GLN LYS LEU MET LYS
SEQRES 2 A 129 ASP ASN GLY ARG ASN MET MET VAL LEU GLY ALA ILE ALA
SEQRES 3 A 129 LYS GLY GLU LYS PRO TYR ASP GLN ALA ALA VAL ASP ALA
SEQRES 4 A 129 ALA LEU LYS GLN PHE ASP GLU THR ALA LYS ASP LEU PRO
SEQRES 5 A 129 LYS LEU PHE PRO ASP SER VAL LYS GLY LEU LYS PRO PHE
SEQRES 6 A 129 ASP SER LYS TYR SER SER SER PRO LYS ILE TRP ALA GLU
SEQRES 7 A 129 ARG ALA LYS PHE ASP THR GLU ILE ALA ASP PHE ALA LYS
SEQRES 8 A 129 ALA VAL ASP GLY ALA LYS GLY LYS ILE LYS ASP VAL ASP
SEQRES 9 A 129 THR LEU LYS ALA ALA MET GLN PRO ILE GLY LYS ALA CYS
SEQRES 10 A 129 GLY ASN CYS HIS GLU ASN PHE ARG ASP LYS GLU GLY
HET HEC A 130 55
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 LEU A 4 GLY A 28 1 25
HELIX 2 2 GLN A 34 THR A 47 1 14
HELIX 3 3 ALA A 48 ASP A 50 5 3
HELIX 4 4 PRO A 73 GLU A 78 1 6
HELIX 5 5 GLU A 78 ILE A 100 1 23
HELIX 6 6 ASP A 102 MET A 110 1 9
HELIX 7 7 GLY A 114 PHE A 124 1 11
LINK SG CYS A 117 CAB HEC A 130 1555 1555 1.92
LINK SG CYS A 120 CAC HEC A 130 1555 1555 1.92
LINK SD MET A 12 FE HEC A 130 1555 1555 2.43
LINK NE2 HIS A 121 FE HEC A 130 1555 1555 2.44
SITE 1 AC1 12 MET A 12 PHE A 44 SER A 70 SER A 71
SITE 2 AC1 12 ILE A 86 PHE A 89 ALA A 116 CYS A 117
SITE 3 AC1 12 CYS A 120 HIS A 121 PHE A 124 ARG A 125
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 - 3 20 Bytes