Header list of 1axj.pdb file
Complete list - b 16 2 Bytes
HEADER BINDING PROTEIN 16-OCT-97 1AXJ
TITLE FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS (MIYAZAKI F), NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FMN-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS STR. 'MIYAZAKI F';
SOURCE 3 ORGANISM_TAXID: 883;
SOURCE 4 STRAIN: MIYAZAKI F;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMKBT-100
KEYWDS FMN-BINDING PROTEIN, BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.LIEPINSH,G.OTTING
REVDAT 3 16-FEB-22 1AXJ 1 REMARK
REVDAT 2 24-FEB-09 1AXJ 1 VERSN
REVDAT 1 14-JAN-98 1AXJ 0
JRNL AUTH E.LIEPINSH,M.KITAMURA,T.MURAKAMI,T.NAKAYA,G.OTTING
JRNL TITL PATHWAY OF CHYMOTRYPSIN EVOLUTION SUGGESTED BY THE STRUCTURE
JRNL TITL 2 OF THE FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS
JRNL TITL 3 (MIYAZAKI F)
JRNL REF NAT.STRUCT.BIOL. V. 4 975 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9406543
JRNL DOI 10.1038/NSB1297-975
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. OPAL (LUGINBUHL ET AL.) ALSO WAS USED.
REMARK 4
REMARK 4 1AXJ 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_1000171377.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 309
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; NOESY-15N-HSQC; NOESY-13C
REMARK 210 -HSQC; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, OPAL
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 : LEAST RESTRAINT VIOLATIONS
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: 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
REMARK 500 REMARK: NULL
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 1 ARG A 92 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 3 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 10 ARG A 60 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 17 ARG A 92 CD - NE - CZ ANGL. DEV. = 9.8 DEGREES
REMARK 500 17 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 19 ARG A 63 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 20 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 3.1 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 GLU A 23 -61.68 -164.16
REMARK 500 1 MET A 51 71.41 -107.88
REMARK 500 1 VAL A 116 -54.99 -127.50
REMARK 500 1 THR A 121 -81.04 -134.83
REMARK 500 2 GLU A 23 -48.86 -161.42
REMARK 500 2 ASP A 24 40.63 -78.44
REMARK 500 2 ARG A 76 -78.63 -91.81
REMARK 500 2 PHE A 104 -179.00 -61.02
REMARK 500 2 VAL A 116 -54.77 -130.15
REMARK 500 2 THR A 121 -81.91 -135.37
REMARK 500 3 GLU A 23 -48.75 -168.98
REMARK 500 3 ASP A 24 38.68 -78.18
REMARK 500 3 SER A 34 -8.71 -58.48
REMARK 500 3 MET A 51 71.50 -103.39
REMARK 500 3 HIS A 52 -70.53 -67.28
REMARK 500 3 THR A 121 -58.82 -132.98
REMARK 500 4 GLU A 23 -60.33 -158.89
REMARK 500 4 ASP A 24 38.84 -78.61
REMARK 500 4 SER A 34 -8.66 -59.31
REMARK 500 4 ASN A 42 13.23 53.82
REMARK 500 4 MET A 51 71.74 -109.75
REMARK 500 4 PHE A 104 -174.74 -65.55
REMARK 500 4 THR A 121 -58.55 -152.84
REMARK 500 5 GLU A 23 -48.24 -158.23
REMARK 500 5 ASP A 24 38.48 -78.18
REMARK 500 5 SER A 34 -8.81 -59.24
REMARK 500 5 ASN A 42 13.00 53.79
REMARK 500 5 MET A 51 50.16 -109.23
REMARK 500 5 LYS A 105 -0.98 -140.89
REMARK 500 5 VAL A 116 -57.14 -129.22
REMARK 500 5 THR A 121 -58.49 -138.69
REMARK 500 6 GLU A 23 -48.59 -158.32
REMARK 500 6 ASP A 24 37.74 -78.61
REMARK 500 6 ASN A 42 13.06 54.08
REMARK 500 6 LYS A 105 -0.78 -141.64
REMARK 500 6 THR A 121 -58.00 -130.17
REMARK 500 7 GLU A 23 -48.71 -158.66
REMARK 500 7 ASP A 24 38.06 -78.77
REMARK 500 7 MET A 51 71.48 -112.11
REMARK 500 7 THR A 121 -58.41 -129.42
REMARK 500 8 GLU A 23 -61.27 -159.63
REMARK 500 8 ASP A 24 38.72 -81.55
REMARK 500 8 ASN A 42 12.88 53.84
REMARK 500 8 MET A 51 71.23 -108.78
REMARK 500 8 PRO A 79 89.73 -69.49
REMARK 500 8 LYS A 105 -0.56 -141.44
REMARK 500 8 VAL A 116 -56.88 -128.57
REMARK 500 8 THR A 121 -77.61 -136.86
REMARK 500 9 GLU A 23 -59.33 -159.20
REMARK 500 9 ASP A 24 39.21 -78.83
REMARK 500
REMARK 500 THIS ENTRY HAS 112 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 2 ARG A 108 0.09 SIDE CHAIN
REMARK 500 3 ARG A 60 0.22 SIDE CHAIN
REMARK 500 3 ARG A 103 0.08 SIDE CHAIN
REMARK 500 4 ARG A 60 0.13 SIDE CHAIN
REMARK 500 4 ARG A 63 0.09 SIDE CHAIN
REMARK 500 4 ARG A 108 0.11 SIDE CHAIN
REMARK 500 5 ARG A 60 0.16 SIDE CHAIN
REMARK 500 5 ARG A 63 0.09 SIDE CHAIN
REMARK 500 6 ARG A 60 0.14 SIDE CHAIN
REMARK 500 6 ARG A 63 0.10 SIDE CHAIN
REMARK 500 6 ARG A 92 0.17 SIDE CHAIN
REMARK 500 7 ARG A 76 0.08 SIDE CHAIN
REMARK 500 8 ARG A 60 0.10 SIDE CHAIN
REMARK 500 8 ARG A 76 0.09 SIDE CHAIN
REMARK 500 8 ARG A 108 0.09 SIDE CHAIN
REMARK 500 9 ARG A 60 0.12 SIDE CHAIN
REMARK 500 9 ARG A 108 0.14 SIDE CHAIN
REMARK 500 10 ARG A 60 0.17 SIDE CHAIN
REMARK 500 11 ARG A 60 0.22 SIDE CHAIN
REMARK 500 11 ARG A 108 0.09 SIDE CHAIN
REMARK 500 14 ARG A 60 0.13 SIDE CHAIN
REMARK 500 14 ARG A 92 0.24 SIDE CHAIN
REMARK 500 15 ARG A 43 0.09 SIDE CHAIN
REMARK 500 15 ARG A 60 0.13 SIDE CHAIN
REMARK 500 15 ARG A 71 0.14 SIDE CHAIN
REMARK 500 15 ARG A 108 0.09 SIDE CHAIN
REMARK 500 16 ARG A 60 0.14 SIDE CHAIN
REMARK 500 16 ARG A 63 0.09 SIDE CHAIN
REMARK 500 17 HIS A 52 0.13 SIDE CHAIN
REMARK 500 17 ARG A 60 0.14 SIDE CHAIN
REMARK 500 17 ARG A 86 0.09 SIDE CHAIN
REMARK 500 17 ARG A 92 0.08 SIDE CHAIN
REMARK 500 17 ARG A 108 0.11 SIDE CHAIN
REMARK 500 18 ARG A 71 0.24 SIDE CHAIN
REMARK 500 19 ARG A 60 0.12 SIDE CHAIN
REMARK 500 19 ARG A 92 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FMN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FMN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 123
DBREF 1AXJ A 1 122 UNP Q46604 FMNB_DESVM 1 122
SEQRES 1 A 122 MET LEU PRO GLY THR PHE PHE GLU VAL LEU LYS ASN GLU
SEQRES 2 A 122 GLY VAL VAL ALA ILE ALA THR GLN GLY GLU ASP GLY PRO
SEQRES 3 A 122 HIS LEU VAL ASN THR TRP ASN SER TYR LEU LYS VAL LEU
SEQRES 4 A 122 ASP GLY ASN ARG ILE VAL VAL PRO VAL GLY GLY MET HIS
SEQRES 5 A 122 LYS THR GLU ALA ASN VAL ALA ARG ASP GLU ARG VAL LEU
SEQRES 6 A 122 MET THR LEU GLY SER ARG LYS VAL ALA GLY ARG ASN GLY
SEQRES 7 A 122 PRO GLY THR GLY PHE LEU ILE ARG GLY SER ALA ALA PHE
SEQRES 8 A 122 ARG THR ASP GLY PRO GLU PHE GLU ALA ILE ALA ARG PHE
SEQRES 9 A 122 LYS TRP ALA ARG ALA ALA LEU VAL ILE THR VAL VAL SER
SEQRES 10 A 122 ALA GLU GLN THR LEU
HET FMN A 123 50
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
HELIX 1 1 GLY A 4 LEU A 10 1 7
HELIX 2 2 ASN A 33 TYR A 35 5 3
HELIX 3 3 HIS A 52 ARG A 60 1 9
HELIX 4 4 GLY A 95 ALA A 102 1 8
SHEET 1 A 6 HIS A 27 TRP A 32 0
SHEET 2 A 6 VAL A 15 THR A 20 -1 N THR A 20 O HIS A 27
SHEET 3 A 6 ARG A 63 SER A 70 -1 N THR A 67 O ALA A 17
SHEET 4 A 6 THR A 81 ARG A 92 -1 N GLY A 87 O VAL A 64
SHEET 5 A 6 ALA A 109 GLN A 120 -1 N GLU A 119 O LEU A 84
SHEET 6 A 6 ARG A 43 VAL A 48 -1 N VAL A 48 O ALA A 109
SHEET 1 B 1 LYS A 37 VAL A 38 0
SITE 1 FMN 8 TRP A 32 THR A 31 ASN A 30 TRP A 106
SITE 2 FMN 8 PRO A 47 VAL A 48 GLY A 50 LYS A 53
SITE 1 AC1 15 HIS A 27 VAL A 29 ASN A 30 THR A 31
SITE 2 AC1 15 TRP A 32 TYR A 35 PRO A 47 VAL A 48
SITE 3 AC1 15 GLY A 49 GLY A 50 MET A 51 HIS A 52
SITE 4 AC1 15 LYS A 53 THR A 54 TRP A 106
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