Header list of 1bfy.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 23-MAY-98 1BFY
TITLE SOLUTION STRUCTURE OF REDUCED CLOSTRIDIUM PASTEURIANUM RUBREDOXIN,
TITLE 2 NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.18.1.1;
COMPND 5 OTHER_DETAILS: REDUCED CLOSTRIDIUM PASTEURIANUM RUBREDOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PASTEURIANUM;
SOURCE 3 ORGANISM_TAXID: 1501
KEYWDS ELECTRON TRANSPORT, RUBREDOXIN, SOLUTION STRUCTURE, PARAMAGNETISM,
KEYWDS 2 NUCLEAR RELAXATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.BERTINI,D.M.KURTZ JUNIOR,M.K.EIDSNESS,G.LIU,C.LUCHINAT,A.ROSATO,
AUTHOR 2 R.A.SCOTT
REVDAT 3 16-FEB-22 1BFY 1 REMARK LINK
REVDAT 2 24-FEB-09 1BFY 1 VERSN
REVDAT 1 25-MAY-99 1BFY 0
JRNL AUTH I.BERTINI,D.M.KURTZ JUNIOR,M.K.EIDSNESS,G.LIU,C.LUCHINAT,
JRNL AUTH 2 A.ROSATO,R.A.SCOTT
JRNL TITL SOLUTION STRUCTURE OF REDUCED CLOSTRIDIUM PASTEURIANUM
JRNL TITL 2 RUBREDOXIN
JRNL REF J.BIOL.INORG.CHEM. V. 3 401 1998
JRNL REFN ISSN 0949-8257
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BFY 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_1000171708.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1 M
REMARK 210 PRESSURE : NORMAL
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; IR-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE800; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER XWINNMR XWINNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D NMR 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: 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 9 CYS A 42 CB - CA - C ANGL. DEV. = 8.3 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 LYS A 2 167.41 58.72
REMARK 500 1 CYS A 6 -97.56 -68.77
REMARK 500 1 THR A 7 -41.65 -172.95
REMARK 500 1 VAL A 8 -38.62 -147.79
REMARK 500 1 VAL A 44 -51.85 -145.46
REMARK 500 2 CYS A 6 -112.08 -74.84
REMARK 500 2 THR A 7 -158.20 -160.18
REMARK 500 2 CYS A 9 -55.85 -153.19
REMARK 500 2 CYS A 39 148.55 -34.57
REMARK 500 2 ASP A 47 -68.53 54.67
REMARK 500 3 CYS A 6 94.72 -58.91
REMARK 500 3 TYR A 11 66.13 -150.82
REMARK 500 3 ILE A 12 125.19 -37.79
REMARK 500 3 CYS A 39 144.02 -39.65
REMARK 500 3 LEU A 41 35.87 -149.32
REMARK 500 3 CYS A 42 -47.41 -131.19
REMARK 500 3 ASP A 47 85.83 21.11
REMARK 500 3 GLN A 48 150.66 75.20
REMARK 500 3 PHE A 49 109.44 -171.02
REMARK 500 4 LYS A 2 162.00 62.54
REMARK 500 4 CYS A 6 47.45 -77.56
REMARK 500 4 THR A 7 -124.27 43.39
REMARK 500 4 CYS A 9 -70.04 -133.00
REMARK 500 4 TYR A 11 -57.63 -131.91
REMARK 500 4 ILE A 12 119.15 75.17
REMARK 500 4 VAL A 44 -149.39 48.07
REMARK 500 4 ASP A 47 -63.59 -158.43
REMARK 500 5 LYS A 2 168.36 60.15
REMARK 500 5 VAL A 8 -65.15 -123.34
REMARK 500 5 CYS A 9 -60.53 -94.56
REMARK 500 5 VAL A 44 123.35 78.84
REMARK 500 5 LYS A 46 74.05 53.87
REMARK 500 5 ASP A 47 -69.67 -152.59
REMARK 500 6 THR A 7 81.02 -69.28
REMARK 500 6 VAL A 8 -74.88 66.98
REMARK 500 6 CYS A 9 -122.68 43.05
REMARK 500 6 ASP A 19 63.94 -151.87
REMARK 500 6 CYS A 42 -68.19 -142.67
REMARK 500 6 LYS A 46 33.89 -148.55
REMARK 500 7 LYS A 2 171.60 62.18
REMARK 500 7 VAL A 8 24.22 -140.50
REMARK 500 7 TYR A 11 65.27 21.00
REMARK 500 7 LEU A 41 -62.31 68.80
REMARK 500 8 LYS A 2 173.38 54.64
REMARK 500 8 VAL A 8 16.20 -148.57
REMARK 500 8 ILE A 12 128.06 71.32
REMARK 500 8 LYS A 46 -88.02 62.38
REMARK 500 8 ASP A 47 -72.48 46.83
REMARK 500 9 LYS A 2 167.82 64.04
REMARK 500 9 THR A 7 -94.41 53.84
REMARK 500
REMARK 500 THIS ENTRY HAS 116 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 GLU A 53 GLU A 54 6 149.72
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 4 0.09 SIDE CHAIN
REMARK 500 1 TYR A 13 0.08 SIDE CHAIN
REMARK 500 2 TYR A 11 0.10 SIDE CHAIN
REMARK 500 2 TYR A 13 0.07 SIDE CHAIN
REMARK 500 3 TYR A 4 0.08 SIDE CHAIN
REMARK 500 3 TYR A 13 0.07 SIDE CHAIN
REMARK 500 4 TYR A 4 0.09 SIDE CHAIN
REMARK 500 4 TYR A 13 0.08 SIDE CHAIN
REMARK 500 5 TYR A 13 0.08 SIDE CHAIN
REMARK 500 6 TYR A 13 0.08 SIDE CHAIN
REMARK 500 7 TYR A 4 0.12 SIDE CHAIN
REMARK 500 7 TYR A 13 0.08 SIDE CHAIN
REMARK 500 10 TYR A 13 0.09 SIDE CHAIN
REMARK 500 11 TYR A 4 0.09 SIDE CHAIN
REMARK 500 12 TYR A 13 0.09 SIDE CHAIN
REMARK 500 12 PHE A 30 0.09 SIDE CHAIN
REMARK 500 13 TYR A 4 0.12 SIDE CHAIN
REMARK 500 14 TYR A 13 0.07 SIDE CHAIN
REMARK 500 16 TYR A 4 0.10 SIDE CHAIN
REMARK 500 16 TYR A 13 0.08 SIDE CHAIN
REMARK 500 16 PHE A 30 0.08 SIDE CHAIN
REMARK 500 17 TYR A 4 0.11 SIDE CHAIN
REMARK 500 17 TYR A 13 0.08 SIDE CHAIN
REMARK 500 18 TYR A 4 0.10 SIDE CHAIN
REMARK 500 18 TYR A 13 0.09 SIDE CHAIN
REMARK 500 19 TYR A 13 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 FE A 55 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 CYS A 9 SG 92.5
REMARK 620 3 CYS A 39 SG 100.5 121.0
REMARK 620 4 CYS A 42 SG 125.0 106.2 111.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FEB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: IRON BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 55
DBREF 1BFY A 1 54 UNP P00268 RUBR_CLOPA 1 54
SEQRES 1 A 54 MET LYS LYS TYR THR CYS THR VAL CYS GLY TYR ILE TYR
SEQRES 2 A 54 ASN PRO GLU ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO
SEQRES 3 A 54 GLY THR ASP PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS
SEQRES 4 A 54 PRO LEU CYS GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL
SEQRES 5 A 54 GLU GLU
HET FE A 55 1
HETNAM FE FE (III) ION
FORMUL 2 FE FE 3+
SHEET 1 A 2 LYS A 3 TYR A 4 0
SHEET 2 A 2 GLU A 51 VAL A 52 -1 N VAL A 52 O LYS A 3
LINK SG CYS A 6 FE FE A 55 1555 1555 2.30
LINK SG CYS A 9 FE FE A 55 1555 1555 2.23
LINK SG CYS A 39 FE FE A 55 1555 1555 2.25
LINK SG CYS A 42 FE FE A 55 1555 1555 2.25
SITE 1 FEB 4 CYS A 6 CYS A 9 CYS A 39 CYS A 42
SITE 1 AC1 4 CYS A 6 CYS A 9 CYS A 39 CYS A 42
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