Header list of 1dvv.pdb file
Complete list - r 14 2 Bytes
HEADER ELECTRON TRANSPORT 22-JAN-00 1DVV
TITLE SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C551;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PKK223-3
KEYWDS CYTOCHROME C, STABILITY, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.HASEGAWA,S.UCHIYAMA,Y.TANIMOTO,M.MIZUTANI,Y.KOBAYASHI,Y.SAMBONGI,
AUTHOR 2 Y.IGARASHI
REVDAT 3 14-MAR-18 1DVV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1DVV 1 VERSN
REVDAT 1 29-NOV-00 1DVV 0
JRNL AUTH J.HASEGAWA,S.UCHIYAMA,Y.TANIMOTO,M.MIZUTANI,Y.KOBAYASHI,
JRNL AUTH 2 Y.SAMBONGI,Y.IGARASHI
JRNL TITL SELECTED MUTATIONS IN A MESOPHILIC CYTOCHROME C CONFER THE
JRNL TITL 2 STABILITY OF A THERMOPHILIC COUNTERPART.
JRNL REF J.BIOL.CHEM. V. 275 37824 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10918067
JRNL DOI 10.1074/JBC.M005861200
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: NULL
REMARK 4
REMARK 4 1DVV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010419.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM CYTOCHROME
REMARK 210 C551(F7A/V13M/F34Y/E43Y/V78I)
REMARK 210 REDUCED WITH DITHIONITE; 1MM
REMARK 210 CYTOCHROME C551(F7A/V13M/F34Y/
REMARK 210 E43Y/V78I) REDUCED WITH
REMARK 210 DITHIONITE; 1MM CYTOCHROME
REMARK 210 C551(F7A/V13M/F34Y/E43Y/V78I) U-
REMARK 210 15N REDUCED WITH DITHIONITE; 1MM
REMARK 210 CYTOCHROME C551(F7A/V13M/F34Y/
REMARK 210 E43Y/V78I) U-15N,13C REDUCED
REMARK 210 WITH DITHIONITE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 3D_13C,15N_SIMULTANOUSLY_SEPARATED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
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 : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 SG CYS A 12 CAB HEM A 83 1.81
REMARK 500 SG CYS A 15 CAC HEM A 83 1.82
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 2 159.97 -48.68
REMARK 500 1 ILE A 18 -27.75 -37.79
REMARK 500 1 ASP A 19 -32.78 -155.24
REMARK 500 1 MET A 22 -117.79 -123.02
REMARK 500 1 ALA A 26 156.17 -42.28
REMARK 500 1 SER A 52 167.98 163.87
REMARK 500 1 GLN A 53 -161.14 -101.90
REMARK 500 1 VAL A 55 -62.92 -104.54
REMARK 500 1 PRO A 58 6.83 -68.94
REMARK 500 1 ALA A 65 35.72 -89.26
REMARK 500 1 SER A 67 172.82 -46.39
REMARK 500 1 GLN A 81 179.04 -50.51
REMARK 500 2 ILE A 18 -27.31 -38.66
REMARK 500 2 ASP A 19 -35.90 -148.65
REMARK 500 2 THR A 20 -179.29 -69.05
REMARK 500 2 MET A 22 -100.89 -78.82
REMARK 500 2 ALA A 26 151.24 -46.11
REMARK 500 2 ALA A 35 90.13 -51.27
REMARK 500 2 ALA A 38 39.46 -90.02
REMARK 500 2 SER A 52 168.13 164.02
REMARK 500 2 VAL A 55 -69.13 -98.28
REMARK 500 2 ALA A 65 36.37 -90.50
REMARK 500 2 SER A 67 152.84 -42.22
REMARK 500 2 GLN A 81 -155.47 37.83
REMARK 500 3 ASP A 19 -35.68 -152.21
REMARK 500 3 MET A 22 -95.22 -85.49
REMARK 500 3 ALA A 35 88.96 -54.86
REMARK 500 3 GLN A 37 157.63 -42.24
REMARK 500 3 PRO A 58 6.87 -69.44
REMARK 500 3 ALA A 65 30.32 -91.66
REMARK 500 3 SER A 67 179.69 -48.85
REMARK 500 4 ILE A 18 -27.96 -37.45
REMARK 500 4 ASP A 19 -34.46 -155.68
REMARK 500 4 MET A 22 -98.03 -124.73
REMARK 500 4 ALA A 26 150.97 -42.43
REMARK 500 4 ALA A 38 41.12 -89.42
REMARK 500 4 SER A 52 158.72 167.42
REMARK 500 4 GLN A 53 -164.82 -106.15
REMARK 500 4 VAL A 55 -69.25 -94.72
REMARK 500 4 SER A 67 157.22 -43.61
REMARK 500 5 ASP A 19 19.35 -162.22
REMARK 500 5 THR A 20 -166.40 -114.93
REMARK 500 5 MET A 22 -98.43 -97.89
REMARK 500 5 ALA A 26 163.23 -41.42
REMARK 500 5 ALA A 35 89.77 -62.21
REMARK 500 5 ALA A 38 40.29 -90.15
REMARK 500 5 SER A 52 167.07 166.28
REMARK 500 5 VAL A 55 -67.60 -91.58
REMARK 500 5 ALA A 65 30.68 -89.87
REMARK 500 5 SER A 67 -176.07 -50.99
REMARK 500
REMARK 500 THIS ENTRY HAS 192 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 HEM A 83 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 HEM A 83 NA 72.9
REMARK 620 3 HEM A 83 NB 101.7 89.0
REMARK 620 4 HEM A 83 NC 110.0 177.1 90.8
REMARK 620 5 HEM A 83 ND 77.5 90.8 179.2 89.4
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 HEM A 83
DBREF 1DVV A 1 82 UNP P00099 CY551_PSEAE 23 104
SEQADV 1DVV ALA A 7 UNP P00099 PHE 29 ENGINEERED MUTATION
SEQADV 1DVV MET A 13 UNP P00099 VAL 35 ENGINEERED MUTATION
SEQADV 1DVV TYR A 34 UNP P00099 PHE 56 ENGINEERED MUTATION
SEQADV 1DVV TYR A 43 UNP P00099 GLU 65 ENGINEERED MUTATION
SEQADV 1DVV ILE A 78 UNP P00099 VAL 100 ENGINEERED MUTATION
SEQRES 1 A 82 GLU ASP PRO GLU VAL LEU ALA LYS ASN LYS GLY CYS MET
SEQRES 2 A 82 ALA CYS HIS ALA ILE ASP THR LYS MET VAL GLY PRO ALA
SEQRES 3 A 82 TYR LYS ASP VAL ALA ALA LYS TYR ALA GLY GLN ALA GLY
SEQRES 4 A 82 ALA GLU ALA TYR LEU ALA GLN ARG ILE LYS ASN GLY SER
SEQRES 5 A 82 GLN GLY VAL TRP GLY PRO ILE PRO MET PRO PRO ASN ALA
SEQRES 6 A 82 VAL SER ASP ASP GLU ALA GLN THR LEU ALA LYS TRP ILE
SEQRES 7 A 82 LEU SER GLN LYS
HET HEM A 83 74
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 ASP A 2 LYS A 10 1 9
HELIX 2 2 GLY A 11 HIS A 16 1 6
HELIX 3 3 ALA A 26 ALA A 35 1 10
HELIX 4 4 GLY A 39 LYS A 49 1 11
HELIX 5 5 SER A 67 GLN A 81 1 15
LINK NE2 HIS A 16 FE HEM A 83 1555 1555 2.51
SITE 1 AC1 22 LYS A 10 GLY A 11 CYS A 12 CYS A 15
SITE 2 AC1 22 HIS A 16 VAL A 23 PRO A 25 LEU A 44
SITE 3 AC1 22 ARG A 47 ILE A 48 SER A 52 GLN A 53
SITE 4 AC1 22 VAL A 55 TRP A 56 GLY A 57 ILE A 59
SITE 5 AC1 22 PRO A 60 MET A 61 PRO A 62 ASN A 64
SITE 6 AC1 22 LEU A 74 ILE A 78
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 14 2 Bytes