Header list of 1ab7.pdb file
Complete list - v 3 2 Bytes
HEADER RIBONUCLEASE INHIBITOR 04-FEB-97 1AB7
TITLE NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL
TITLE 2 EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BARSTAR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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
KEYWDS RIBONUCLEASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR K.B.WONG,A.R.FERSHT,S.M.V.FREUND
REVDAT 3 03-NOV-21 1AB7 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1AB7 1 VERSN
REVDAT 1 04-SEP-97 1AB7 0
JRNL AUTH K.B.WONG,A.R.FERSHT,S.M.FREUND
JRNL TITL NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL SLOW
JRNL TITL 2 CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A.
JRNL REF J.MOL.BIOL. V. 268 494 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9159486
JRNL DOI 10.1006/JMBI.1997.0989
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.W.HARTLEY
REMARK 1 TITL BARNASE AND BARSTAR: TWO SMALL PROTEINS TO FOLD AND FIT
REMARK 1 TITL 2 TOGETHER
REMARK 1 REF TRENDS BIOCHEM.SCI. V. 14 450 1989
REMARK 1 REFN ISSN 0968-0004
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 1AB7 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_1000170613.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500; AMX2 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY - SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 ON THE 13C, 15N-LABELED BARSTAR MUTANT C40A,C82A
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 ALA A 25 51.88 71.97
REMARK 500 1 PRO A 27 -166.63 -78.06
REMARK 500 1 TYR A 30 115.43 -31.79
REMARK 500 1 ALA A 40 -71.28 -81.51
REMARK 500 1 THR A 42 45.65 -82.97
REMARK 500 1 TRP A 44 -55.62 -165.24
REMARK 500 1 GLU A 52 84.62 -66.46
REMARK 500 1 ARG A 54 -138.77 -61.68
REMARK 500 1 GLN A 55 102.16 -43.03
REMARK 500 1 SER A 59 -31.86 83.45
REMARK 500 1 THR A 63 -143.16 -135.81
REMARK 500 1 ASN A 65 38.67 179.92
REMARK 500 1 ALA A 79 -70.87 -90.21
REMARK 500 1 ALA A 82 149.87 -39.65
REMARK 500 1 ASP A 83 61.15 -106.46
REMARK 500 1 LEU A 88 -39.05 -147.36
REMARK 500 2 ALA A 25 50.83 75.41
REMARK 500 2 TYR A 30 117.44 -35.39
REMARK 500 2 ALA A 40 -70.83 -81.67
REMARK 500 2 TRP A 44 -46.15 -172.95
REMARK 500 2 GLU A 52 85.67 -61.23
REMARK 500 2 ARG A 54 -93.01 -52.85
REMARK 500 2 GLU A 57 -71.48 -48.54
REMARK 500 2 SER A 59 -42.05 83.15
REMARK 500 2 LEU A 62 -31.36 -33.13
REMARK 500 2 THR A 63 -133.50 -101.77
REMARK 500 2 GLU A 64 -47.03 -138.97
REMARK 500 2 ASN A 65 20.50 -156.60
REMARK 500 2 ALA A 82 160.81 -40.99
REMARK 500 2 ASP A 83 54.81 -115.79
REMARK 500 3 TYR A 30 114.06 -34.65
REMARK 500 3 TRP A 44 -46.82 -174.80
REMARK 500 3 GLU A 52 86.41 -62.51
REMARK 500 3 GLN A 55 -161.54 49.16
REMARK 500 3 PHE A 56 -71.14 173.11
REMARK 500 3 LEU A 62 -25.10 -38.81
REMARK 500 3 THR A 63 -134.23 -89.53
REMARK 500 3 GLU A 64 59.05 -163.50
REMARK 500 3 ASN A 65 16.87 83.61
REMARK 500 3 ALA A 79 -70.47 -93.88
REMARK 500 3 ALA A 82 155.87 -39.59
REMARK 500 3 ASP A 83 54.26 -109.73
REMARK 500 4 ALA A 25 51.42 77.22
REMARK 500 4 TYR A 30 110.51 -36.21
REMARK 500 4 ASN A 33 -168.08 -161.91
REMARK 500 4 ALA A 40 -71.35 -81.10
REMARK 500 4 THR A 42 41.58 -81.11
REMARK 500 4 TRP A 44 -66.44 -174.79
REMARK 500 4 VAL A 45 -29.21 -38.44
REMARK 500 4 GLU A 46 128.00 73.16
REMARK 500
REMARK 500 THIS ENTRY HAS 481 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 1 ARG A 11 0.17 SIDE CHAIN
REMARK 500 1 ARG A 54 0.24 SIDE CHAIN
REMARK 500 1 ARG A 75 0.30 SIDE CHAIN
REMARK 500 2 ARG A 11 0.10 SIDE CHAIN
REMARK 500 2 ARG A 54 0.24 SIDE CHAIN
REMARK 500 2 ARG A 75 0.08 SIDE CHAIN
REMARK 500 3 ARG A 11 0.32 SIDE CHAIN
REMARK 500 3 ARG A 54 0.32 SIDE CHAIN
REMARK 500 3 ARG A 75 0.18 SIDE CHAIN
REMARK 500 4 ARG A 11 0.29 SIDE CHAIN
REMARK 500 4 ARG A 75 0.30 SIDE CHAIN
REMARK 500 5 ARG A 11 0.28 SIDE CHAIN
REMARK 500 5 ARG A 54 0.27 SIDE CHAIN
REMARK 500 5 ARG A 75 0.26 SIDE CHAIN
REMARK 500 6 ARG A 11 0.22 SIDE CHAIN
REMARK 500 6 ARG A 54 0.18 SIDE CHAIN
REMARK 500 6 ARG A 75 0.32 SIDE CHAIN
REMARK 500 7 ARG A 11 0.31 SIDE CHAIN
REMARK 500 7 ARG A 54 0.29 SIDE CHAIN
REMARK 500 7 ARG A 75 0.19 SIDE CHAIN
REMARK 500 8 ARG A 11 0.30 SIDE CHAIN
REMARK 500 8 ARG A 54 0.30 SIDE CHAIN
REMARK 500 8 ARG A 75 0.18 SIDE CHAIN
REMARK 500 9 ARG A 11 0.31 SIDE CHAIN
REMARK 500 9 ARG A 54 0.24 SIDE CHAIN
REMARK 500 9 ARG A 75 0.22 SIDE CHAIN
REMARK 500 10 ARG A 11 0.31 SIDE CHAIN
REMARK 500 10 ARG A 54 0.30 SIDE CHAIN
REMARK 500 10 ARG A 75 0.21 SIDE CHAIN
REMARK 500 11 ARG A 11 0.21 SIDE CHAIN
REMARK 500 11 ARG A 54 0.11 SIDE CHAIN
REMARK 500 11 ARG A 75 0.30 SIDE CHAIN
REMARK 500 12 ARG A 11 0.14 SIDE CHAIN
REMARK 500 12 ARG A 54 0.19 SIDE CHAIN
REMARK 500 12 ARG A 75 0.09 SIDE CHAIN
REMARK 500 13 ARG A 11 0.13 SIDE CHAIN
REMARK 500 13 ARG A 54 0.30 SIDE CHAIN
REMARK 500 13 ARG A 75 0.26 SIDE CHAIN
REMARK 500 14 ARG A 11 0.31 SIDE CHAIN
REMARK 500 14 ARG A 54 0.31 SIDE CHAIN
REMARK 500 14 ARG A 75 0.22 SIDE CHAIN
REMARK 500 15 ARG A 11 0.27 SIDE CHAIN
REMARK 500 15 ARG A 54 0.32 SIDE CHAIN
REMARK 500 15 ARG A 75 0.12 SIDE CHAIN
REMARK 500 16 ARG A 11 0.23 SIDE CHAIN
REMARK 500 16 ARG A 54 0.24 SIDE CHAIN
REMARK 500 16 ARG A 75 0.32 SIDE CHAIN
REMARK 500 17 ARG A 11 0.24 SIDE CHAIN
REMARK 500 17 ARG A 54 0.18 SIDE CHAIN
REMARK 500 17 ARG A 75 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 87 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RESIDUE 26 - 44 IS THE REGION THAT BINDS TO THE
REMARK 800 ACTIVE SITE OF THE RIBONUCLEASE BARNASE AND INHIBITS THE ENZYME.
DBREF 1AB7 A 1 89 UNP P11540 BARS_BACAM 1 89
SEQADV 1AB7 ALA A 40 UNP P11540 CYS 40 ENGINEERED MUTATION
SEQADV 1AB7 ALA A 82 UNP P11540 CYS 82 ENGINEERED MUTATION
SEQRES 1 A 89 LYS LYS ALA VAL ILE ASN GLY GLU GLN ILE ARG SER ILE
SEQRES 2 A 89 SER ASP LEU HIS GLN THR LEU LYS LYS GLU LEU ALA LEU
SEQRES 3 A 89 PRO GLU TYR TYR GLY GLU ASN LEU ASP ALA LEU TRP ASP
SEQRES 4 A 89 ALA LEU THR GLY TRP VAL GLU TYR PRO LEU VAL LEU GLU
SEQRES 5 A 89 TRP ARG GLN PHE GLU GLN SER LYS GLN LEU THR GLU ASN
SEQRES 6 A 89 GLY ALA GLU SER VAL LEU GLN VAL PHE ARG GLU ALA LYS
SEQRES 7 A 89 ALA GLU GLY ALA ASP ILE THR ILE ILE LEU SER
HELIX 1 H2 ASN A 33 GLY A 43 1 11
HELIX 2 H3 PHE A 56 THR A 63 1 8
HELIX 3 H4 GLU A 68 GLY A 81 1 14
SHEET 1 S1 2 LEU A 49 ARG A 54 0
SHEET 2 S1 2 ASP A 83 SER A 89 1
CISPEP 1 TYR A 47 PRO A 48 1 1.81
CISPEP 2 TYR A 47 PRO A 48 2 1.91
CISPEP 3 TYR A 47 PRO A 48 3 2.28
CISPEP 4 TYR A 47 PRO A 48 4 1.64
CISPEP 5 TYR A 47 PRO A 48 5 1.47
CISPEP 6 TYR A 47 PRO A 48 6 1.46
CISPEP 7 TYR A 47 PRO A 48 7 2.06
CISPEP 8 TYR A 47 PRO A 48 8 2.18
CISPEP 9 TYR A 47 PRO A 48 9 1.88
CISPEP 10 TYR A 47 PRO A 48 10 1.91
CISPEP 11 TYR A 47 PRO A 48 11 1.40
CISPEP 12 TYR A 47 PRO A 48 12 1.62
CISPEP 13 TYR A 47 PRO A 48 13 1.80
CISPEP 14 TYR A 47 PRO A 48 14 1.79
CISPEP 15 TYR A 47 PRO A 48 15 1.86
CISPEP 16 TYR A 47 PRO A 48 16 2.06
CISPEP 17 TYR A 47 PRO A 48 17 2.05
CISPEP 18 TYR A 47 PRO A 48 18 1.83
CISPEP 19 TYR A 47 PRO A 48 19 2.11
CISPEP 20 TYR A 47 PRO A 48 20 1.82
CISPEP 21 TYR A 47 PRO A 48 21 2.79
CISPEP 22 TYR A 47 PRO A 48 22 1.86
CISPEP 23 TYR A 47 PRO A 48 23 2.31
CISPEP 24 TYR A 47 PRO A 48 24 2.12
CISPEP 25 TYR A 47 PRO A 48 25 1.46
CISPEP 26 TYR A 47 PRO A 48 26 1.81
CISPEP 27 TYR A 47 PRO A 48 27 1.89
CISPEP 28 TYR A 47 PRO A 48 28 1.37
CISPEP 29 TYR A 47 PRO A 48 29 1.81
CISPEP 30 TYR A 47 PRO A 48 30 1.80
SITE 1 BNB 19 LEU A 26 PRO A 27 GLU A 28 TYR A 29
SITE 2 BNB 19 TYR A 30 GLY A 31 GLU A 32 ASN A 33
SITE 3 BNB 19 LEU A 34 ASP A 35 ALA A 36 LEU A 37
SITE 4 BNB 19 TRP A 38 ASP A 39 ALA A 40 LEU A 41
SITE 5 BNB 19 THR A 42 GLY A 43 TRP A 44
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 - v 3 2 Bytes