Header list of 2f40.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-NOV-05 2F40
TITLE STRUCTURE OF A NOVEL PROTEIN FROM BACKBONE-CENTERED NMR DATA AND NMR-
TITLE 2 ASSISTED STRUCTURE PREDICTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PF1455;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 186497;
SOURCE 4 STRAIN: DSM 3638;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10, BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRIL
KEYWDS PROTEIN STRUCTURE PREDICTION, RESIDUAL DIPOLAR COUPLINGS, PYROCOCCUS
KEYWDS 2 FURIOUS, SIMULATED ANNEALING, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, SOUTHEAST COLLABORATORY FOR STRUCTURAL
KEYWDS 4 GENOMICS, SECSG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.BANSAL,J.H.PRESTEGARD,SOUTHEAST COLLABORATORY FOR STRUCTURAL
AUTHOR 2 GENOMICS (SECSG)
REVDAT 4 13-JUL-11 2F40 1 VERSN
REVDAT 3 24-FEB-09 2F40 1 VERSN
REVDAT 2 07-NOV-06 2F40 1 JRNL
REVDAT 1 20-DEC-05 2F40 0
JRNL AUTH K.L.MAYER,Y.QU,S.BANSAL,P.D.LEBLOND,F.E.JENNEY,P.S.BRERETON,
JRNL AUTH 2 M.W.ADAMS,Y.XU,J.H.PRESTEGARD
JRNL TITL STRUCTURE DETERMINATION OF A NEW PROTEIN FROM
JRNL TITL 2 BACKBONE-CENTERED NMR DATA AND NMR-ASSISTED STRUCTURE
JRNL TITL 3 PREDICTION.
JRNL REF PROTEINS V. 65 480 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16927360
JRNL DOI 10.1002/PROT.21119
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: LIMITED AMOUNTS OF STRUCTURAL DATA ARE
REMARK 3 USED TO IMPROVE AN INITIAL HOMOLOGY SEARCH AND THE DATA ARE
REMARK 3 SUBSEQUENTLY USED TO PRODUCE A STRUCTURE BY DATA-CONSTRAINED
REMARK 3 REFINEMENT OF AN IDENTIFIED STRUCTURAL TEMPLATE
REMARK 4
REMARK 4 2F40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035424.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 70MM NACL; 40MM NACL; 70MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PF1455 U-15N, 20MM TRIS,
REMARK 210 70MM NACL, PH 7.0, 90% H20, 10%
REMARK 210 D20; 1.14MM PF1455 U-15N/16%13C,
REMARK 210 11MM TRIS, 40MM NACL, 10MG/ML
REMARK 210 PHAGE, PHAGE IN 90% H2O, 10% D2O;
REMARK 210 1.2MM PF1455 U-15N/16%13C, 20MM
REMARK 210 TRIS, 70MM NACL, 3% C12E5/
REMARK 210 HEXANOL, PH 7.0, C12E5 IN 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N IPAP HSQC; 3D_15N-SEPARATED_
REMARK 210 NOESY; HNCA-ECOSY; HNCAHA; 3D
REMARK 210 TOCSY
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 : NMRPIPE, REDCAT 1.0
REMARK 210 METHOD USED : RDC DIRECTED FRAGMENT ASSEMBLY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ALA A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 GLU A 75
REMARK 465 GLY A 76
REMARK 465 SER A 77
REMARK 465 LEU A 78
REMARK 465 SER A 79
REMARK 465 TRP A 80
REMARK 465 ASN A 81
REMARK 465 ASN A 82
REMARK 465 VAL A 83
REMARK 465 LEU A 84
REMARK 465 ARG A 85
REMARK 465 SER A 86
REMARK 465 LYS A 87
REMARK 465 ALA A 88
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 HG2 GLN A 71 H GLU A 72 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 10 GLY A 60 N GLY A 60 CA 0.096
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 LEU A 70 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 1 LEU A 70 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 2 LEU A 70 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 2 LEU A 70 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 3 LEU A 70 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 3 LEU A 70 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 9 GLU A 61 N - CA - CB ANGL. DEV. = 11.2 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 5 -156.19 -94.57
REMARK 500 1 PHE A 6 -158.71 176.27
REMARK 500 1 ASN A 9 -77.20 -163.60
REMARK 500 1 GLU A 13 -49.27 -148.84
REMARK 500 1 GLU A 14 0.37 -62.07
REMARK 500 1 ARG A 25 -79.36 -29.91
REMARK 500 1 ASP A 26 22.29 -70.88
REMARK 500 1 GLU A 27 -40.70 -150.68
REMARK 500 1 TYR A 29 -111.51 -128.97
REMARK 500 1 TYR A 36 -30.76 -160.90
REMARK 500 1 ALA A 40 67.47 62.78
REMARK 500 1 ASP A 46 123.07 -170.76
REMARK 500 1 LYS A 48 -70.71 -101.86
REMARK 500 1 VAL A 49 -44.33 177.53
REMARK 500 1 ASN A 50 -4.64 99.23
REMARK 500 1 GLU A 61 -7.18 58.69
REMARK 500 1 GLU A 65 -73.79 -111.76
REMARK 500 1 GLU A 67 72.06 -108.11
REMARK 500 1 ILE A 68 77.90 -103.95
REMARK 500 1 THR A 69 44.31 -87.34
REMARK 500 1 GLN A 71 -114.10 26.70
REMARK 500 1 LEU A 73 -95.49 -37.76
REMARK 500 2 LYS A 5 -156.19 -94.57
REMARK 500 2 PHE A 6 -158.71 176.27
REMARK 500 2 ASN A 9 -77.20 -163.60
REMARK 500 2 GLU A 13 -49.27 -148.84
REMARK 500 2 GLU A 14 0.37 -62.07
REMARK 500 2 ARG A 25 -79.36 -29.91
REMARK 500 2 ASP A 26 22.29 -70.88
REMARK 500 2 GLU A 27 -40.70 -150.68
REMARK 500 2 TYR A 29 -111.51 -128.97
REMARK 500 2 TYR A 36 -30.76 -160.90
REMARK 500 2 ALA A 40 67.47 62.78
REMARK 500 2 ASP A 46 123.07 -170.76
REMARK 500 2 LYS A 48 -70.71 -101.86
REMARK 500 2 VAL A 49 -44.33 177.53
REMARK 500 2 ASN A 50 -4.64 99.23
REMARK 500 2 GLU A 61 -7.18 58.69
REMARK 500 2 GLU A 65 -73.79 -111.76
REMARK 500 2 GLU A 67 72.06 -108.11
REMARK 500 2 ILE A 68 77.90 -103.95
REMARK 500 2 THR A 69 44.31 -87.34
REMARK 500 2 GLN A 71 -114.10 26.70
REMARK 500 2 LEU A 73 -95.49 -37.76
REMARK 500 3 LYS A 5 -156.19 -94.57
REMARK 500 3 PHE A 6 -158.71 176.27
REMARK 500 3 ASN A 9 -77.20 -163.60
REMARK 500 3 GLU A 13 -49.27 -148.84
REMARK 500 3 GLU A 14 0.37 -62.07
REMARK 500 3 ARG A 25 -79.36 -29.91
REMARK 500
REMARK 500 THIS ENTRY HAS 236 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 GLN A 71 GLU A 72 10 147.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 1 LYS A 59 24.6 L L OUTSIDE RANGE
REMARK 500 2 LYS A 59 24.6 L L OUTSIDE RANGE
REMARK 500 3 LYS A 59 24.6 L L OUTSIDE RANGE
REMARK 500 4 VAL A 42 24.3 L L OUTSIDE RANGE
REMARK 500 4 GLU A 52 24.4 L L OUTSIDE RANGE
REMARK 500 5 GLN A 19 23.4 L L OUTSIDE RANGE
REMARK 500 5 GLU A 65 24.3 L L OUTSIDE RANGE
REMARK 500 6 LEU A 22 24.8 L L OUTSIDE RANGE
REMARK 500 6 PHE A 32 24.0 L L OUTSIDE RANGE
REMARK 500 6 ASP A 46 22.4 L L OUTSIDE RANGE
REMARK 500 7 ILE A 68 23.6 L L OUTSIDE RANGE
REMARK 500 8 GLU A 21 11.2 L L OUTSIDE RANGE
REMARK 500 8 SER A 47 24.3 L L OUTSIDE RANGE
REMARK 500 9 LYS A 57 24.0 L L OUTSIDE RANGE
REMARK 500 9 GLU A 61 11.3 L L OUTSIDE RANGE
REMARK 500 10 PHE A 28 22.1 L L OUTSIDE RANGE
REMARK 500 10 GLU A 56 7.7 L L EXPECTING SP3
REMARK 500 10 GLU A 61 18.6 L L OUTSIDE RANGE
REMARK 500 10 ILE A 68 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFU-1362288-001 RELATED DB: TARGETDB
DBREF 2F40 A 2 88 GB 18977827 NP_579184 2 88
SEQADV 2F40 ALA A -7 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -6 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -5 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -4 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -3 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -2 GB 18977827 EXPRESSION TAG
SEQADV 2F40 HIS A -1 GB 18977827 EXPRESSION TAG
SEQADV 2F40 GLY A 0 GB 18977827 EXPRESSION TAG
SEQADV 2F40 SER A 1 GB 18977827 EXPRESSION TAG
SEQRES 1 A 96 ALA HIS HIS HIS HIS HIS HIS GLY SER LYS TRP ILE LYS
SEQRES 2 A 96 PHE THR THR ASN LEU THR PRO GLU GLU ALA LYS ILE VAL
SEQRES 3 A 96 GLN TYR GLU LEU SER THR ARG ASP GLU PHE TYR ARG VAL
SEQRES 4 A 96 PHE ILE ASN PRO TYR ALA LYS VAL ALA GLU VAL VAL ILE
SEQRES 5 A 96 ASP ASP SER LYS VAL ASN ILE GLU GLU LEU LYS GLU LYS
SEQRES 6 A 96 LEU LYS GLY GLU VAL ILE GLU GLU LYS GLU ILE THR LEU
SEQRES 7 A 96 GLN GLU LEU ILE GLU GLY SER LEU SER TRP ASN ASN VAL
SEQRES 8 A 96 LEU ARG SER LYS ALA
HELIX 1 1 ALA A 15 GLU A 21 1 7
HELIX 2 2 ASN A 50 LEU A 58 1 9
SHEET 1 A 2 TRP A 3 LYS A 5 0
SHEET 2 A 2 GLU A 41 VAL A 43 -1 O VAL A 42 N ILE A 4
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 25 2 Bytes