Header list of 1fw7.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 22-SEP-00 1FW7
TITLE NMR STRUCTURE OF 15N-LABELED BARNASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BARNASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RIBONUCLEASE;
COMPND 5 EC: 3.1.27.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;
SOURCE 3 ORGANISM_TAXID: 1390;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PRBA
KEYWDS RIBONUCLEASE, ALPHA-BETA PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.Y.REIBARKH,L.I.VASILIEVA,A.A.SCHULGA,M.P.KIRPICHNIKOV,A.S.ARSENIEV
REVDAT 3 23-FEB-22 1FW7 1 REMARK
REVDAT 2 24-FEB-09 1FW7 1 VERSN
REVDAT 1 10-JUN-03 1FW7 0
JRNL AUTH M.Y.REIBARKH,L.I.VASILIEVA,A.A.SCHULGA,M.P.KIRPICHNIKOV,
JRNL AUTH 2 A.S.ARSENIEV
JRNL TITL REFINED SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF
JRNL TITL 2 15N-LABELED BARNASE STUDIED BY NMR.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, FANTOM 4.0
REMARK 3 AUTHORS : VARIAN (VNMR), SCHAUMANN ET AL. (FANTOM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FW7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011955.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.04
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 15N-LABELED BARNASE, 1MM; 15N
REMARK 210 -LABELED BARNASE, 1MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HMQC; 2D
REMARK 210 NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY 1.2.11, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA).
REMARK 210 NEWTON-RAPHSON MINIMIZATION OF
REMARK 210 CONFORMATIONAL ENERGY WITH
REMARK 210 EXPERIMENTAL CONSTRAINTS (FANTOM)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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: 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 ASN A 5 43.68 -160.05
REMARK 500 1 THR A 16 -77.03 -72.03
REMARK 500 1 ASP A 22 48.94 -81.46
REMARK 500 1 ALA A 46 73.62 -154.32
REMARK 500 1 ASP A 54 172.06 -57.90
REMARK 500 1 SER A 57 86.56 58.55
REMARK 500 1 LYS A 66 -71.23 -132.34
REMARK 500 1 SER A 67 -49.83 -173.94
REMARK 500 1 THR A 79 -73.96 -117.54
REMARK 500 1 ASN A 84 -163.32 -109.83
REMARK 500 1 TRP A 94 49.56 74.47
REMARK 500 1 ASP A 101 30.09 -141.47
REMARK 500 2 ASN A 5 28.90 -147.46
REMARK 500 2 THR A 16 -71.92 -72.41
REMARK 500 2 ASP A 22 47.63 -81.47
REMARK 500 2 ALA A 46 76.21 -155.49
REMARK 500 2 ASP A 54 171.75 -56.76
REMARK 500 2 SER A 57 2.33 84.24
REMARK 500 2 SER A 67 96.41 -60.51
REMARK 500 2 THR A 79 -73.54 -116.42
REMARK 500 2 ASN A 84 -161.83 -109.40
REMARK 500 2 TRP A 94 54.10 75.16
REMARK 500 2 HIS A 102 65.73 61.42
REMARK 500 3 ASN A 5 29.17 -147.08
REMARK 500 3 THR A 16 -76.68 -72.23
REMARK 500 3 ALA A 46 73.85 -155.16
REMARK 500 3 SER A 67 93.35 -62.53
REMARK 500 3 THR A 79 -74.41 -115.99
REMARK 500 3 ASN A 84 -158.17 -119.35
REMARK 500 3 TRP A 94 50.34 73.25
REMARK 500 4 GLN A 2 44.28 -157.08
REMARK 500 4 ASN A 5 55.58 -159.36
REMARK 500 4 ALA A 46 75.04 -155.18
REMARK 500 4 ASP A 54 172.03 -57.28
REMARK 500 4 SER A 57 -9.89 91.00
REMARK 500 4 LYS A 66 -76.06 -132.89
REMARK 500 4 SER A 67 -53.52 -168.82
REMARK 500 4 THR A 79 -73.40 -108.94
REMARK 500 4 ASN A 84 -161.33 -113.55
REMARK 500 4 TRP A 94 45.92 77.77
REMARK 500 4 HIS A 102 67.51 64.09
REMARK 500 4 GLN A 104 -61.30 -100.19
REMARK 500 5 THR A 16 -73.65 -75.74
REMARK 500 5 ALA A 46 74.54 -154.98
REMARK 500 5 ASP A 54 173.99 -58.83
REMARK 500 5 SER A 57 112.81 70.58
REMARK 500 5 THR A 79 -73.72 -111.93
REMARK 500 5 ASN A 84 -163.52 -109.80
REMARK 500 5 TRP A 94 48.14 77.04
REMARK 500 5 ASP A 101 39.28 -156.47
REMARK 500
REMARK 500 THIS ENTRY HAS 209 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 GLY A 40 ASN A 41 1 -148.30
REMARK 500 TRP A 94 LEU A 95 1 142.96
REMARK 500 GLY A 40 ASN A 41 2 -142.56
REMARK 500 TRP A 94 LEU A 95 2 140.61
REMARK 500 GLY A 40 ASN A 41 3 -143.69
REMARK 500 TRP A 94 LEU A 95 3 141.95
REMARK 500 GLY A 40 ASN A 41 4 -149.22
REMARK 500 TRP A 94 LEU A 95 4 146.83
REMARK 500 TRP A 94 LEU A 95 5 144.38
REMARK 500 TRP A 94 LEU A 95 6 144.10
REMARK 500 GLY A 40 ASN A 41 7 -146.84
REMARK 500 TRP A 94 LEU A 95 7 140.15
REMARK 500 TRP A 94 LEU A 95 8 146.82
REMARK 500 GLY A 40 ASN A 41 9 -148.66
REMARK 500 TRP A 94 LEU A 95 9 149.54
REMARK 500 GLY A 40 ASN A 41 10 -144.73
REMARK 500 TRP A 94 LEU A 95 10 142.75
REMARK 500 GLY A 40 ASN A 41 11 -146.20
REMARK 500 ASN A 58 ARG A 59 11 144.21
REMARK 500 TRP A 94 LEU A 95 11 145.15
REMARK 500 TRP A 94 LEU A 95 12 148.09
REMARK 500 GLY A 40 ASN A 41 13 -148.51
REMARK 500 TRP A 94 LEU A 95 13 148.01
REMARK 500 TRP A 94 LEU A 95 14 145.55
REMARK 500 GLY A 40 ASN A 41 15 -145.58
REMARK 500 TRP A 94 LEU A 95 15 149.38
REMARK 500 GLY A 40 ASN A 41 16 -149.03
REMARK 500 TRP A 94 LEU A 95 16 143.11
REMARK 500 GLY A 40 ASN A 41 17 -145.35
REMARK 500 TRP A 94 LEU A 95 17 140.37
REMARK 500 GLY A 40 ASN A 41 18 -147.09
REMARK 500 ARG A 59 GLU A 60 18 149.41
REMARK 500 TRP A 94 LEU A 95 18 146.83
REMARK 500 GLY A 40 ASN A 41 19 -144.22
REMARK 500 TRP A 94 LEU A 95 19 141.26
REMARK 500 LEU A 20 PRO A 21 20 149.63
REMARK 500 TRP A 94 LEU A 95 20 147.04
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 87 0.09 SIDE CHAIN
REMARK 500 3 ARG A 87 0.09 SIDE CHAIN
REMARK 500 4 ARG A 69 0.14 SIDE CHAIN
REMARK 500 4 ARG A 83 0.11 SIDE CHAIN
REMARK 500 5 ARG A 69 0.15 SIDE CHAIN
REMARK 500 5 ARG A 110 0.14 SIDE CHAIN
REMARK 500 6 ARG A 69 0.14 SIDE CHAIN
REMARK 500 6 ARG A 87 0.09 SIDE CHAIN
REMARK 500 7 ARG A 69 0.09 SIDE CHAIN
REMARK 500 8 ARG A 69 0.09 SIDE CHAIN
REMARK 500 8 ARG A 110 0.13 SIDE CHAIN
REMARK 500 9 ARG A 69 0.08 SIDE CHAIN
REMARK 500 10 ARG A 59 0.09 SIDE CHAIN
REMARK 500 10 ARG A 69 0.14 SIDE CHAIN
REMARK 500 10 ARG A 110 0.13 SIDE CHAIN
REMARK 500 11 ARG A 83 0.10 SIDE CHAIN
REMARK 500 12 ARG A 69 0.10 SIDE CHAIN
REMARK 500 12 ARG A 110 0.12 SIDE CHAIN
REMARK 500 13 ARG A 69 0.09 SIDE CHAIN
REMARK 500 13 ARG A 87 0.10 SIDE CHAIN
REMARK 500 14 ARG A 59 0.11 SIDE CHAIN
REMARK 500 14 ARG A 87 0.10 SIDE CHAIN
REMARK 500 14 ARG A 110 0.09 SIDE CHAIN
REMARK 500 15 ARG A 83 0.08 SIDE CHAIN
REMARK 500 15 ARG A 110 0.14 SIDE CHAIN
REMARK 500 16 ARG A 69 0.14 SIDE CHAIN
REMARK 500 17 ARG A 110 0.14 SIDE CHAIN
REMARK 500 18 ARG A 69 0.10 SIDE CHAIN
REMARK 500 18 ARG A 110 0.13 SIDE CHAIN
REMARK 500 19 ARG A 69 0.12 SIDE CHAIN
REMARK 500 19 ARG A 110 0.14 SIDE CHAIN
REMARK 500 20 ARG A 110 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FW7 A 1 110 UNP P00648 RNBR_BACAM 48 157
SEQRES 1 A 110 ALA GLN VAL ILE ASN THR PHE ASP GLY VAL ALA ASP TYR
SEQRES 2 A 110 LEU GLN THR TYR HIS LYS LEU PRO ASP ASN TYR ILE THR
SEQRES 3 A 110 LYS SER GLU ALA GLN ALA LEU GLY TRP VAL ALA SER LYS
SEQRES 4 A 110 GLY ASN LEU ALA ASP VAL ALA PRO GLY LYS SER ILE GLY
SEQRES 5 A 110 GLY ASP ILE PHE SER ASN ARG GLU GLY LYS LEU PRO GLY
SEQRES 6 A 110 LYS SER GLY ARG THR TRP ARG GLU ALA ASP ILE ASN TYR
SEQRES 7 A 110 THR SER GLY PHE ARG ASN SER ASP ARG ILE LEU TYR SER
SEQRES 8 A 110 SER ASP TRP LEU ILE TYR LYS THR THR ASP HIS TYR GLN
SEQRES 9 A 110 THR PHE THR LYS ILE ARG
HELIX 1 1 THR A 6 HIS A 18 1 13
HELIX 2 2 THR A 26 GLY A 34 1 9
HELIX 3 3 ASN A 41 ALA A 46 1 6
SHEET 1 A 6 TYR A 24 ILE A 25 0
SHEET 2 A 6 SER A 50 ILE A 55 1 O SER A 50 N ILE A 25
SHEET 3 A 6 TRP A 71 ASP A 75 -1 O GLU A 73 N GLY A 53
SHEET 4 A 6 ARG A 87 SER A 91 -1 N ILE A 88 O ALA A 74
SHEET 5 A 6 ILE A 96 THR A 99 -1 O TYR A 97 N LEU A 89
SHEET 6 A 6 THR A 107 ARG A 110 -1 O THR A 107 N LYS A 98
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 23 2 Bytes