Header list of 1awo.pdb file
Complete list - b 16 2 Bytes
HEADER KINASE 03-OCT-97 1AWO
TITLE THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2 IN
TITLE 2 THE SH(32) CONSTRUCT, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABL TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SRC-HOMOLOGY 3 (SH3) DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NB42;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX;
SOURCE 9 OTHER_DETAILS: EXPRESSED AS GST FUSIONS AND CLEAVED
KEYWDS KINASE, SH3 DOMAIN, TRANSFERASE, PHOSPHOTRANSFERASE, PROTO-ONCOGENE,
KEYWDS 2 MULTIPLE DOMAIN, LEUKEMIA
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.COWBURN
REVDAT 3 16-FEB-22 1AWO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1AWO 1 VERSN
REVDAT 1 28-JAN-98 1AWO 0
JRNL AUTH Y.Q.GOSSER,J.ZHENG,M.OVERDUIN,B.J.MAYER,D.COWBURN
JRNL TITL THE SOLUTION STRUCTURE OF ABL SH3, AND ITS RELATIONSHIP TO
JRNL TITL 2 SH2 IN THE SH(32) CONSTRUCT.
JRNL REF STRUCTURE V. 3 1075 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8590002
JRNL DOI 10.1016/S0969-2126(01)00243-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.J.MAYER,D.BALTIMORE
REMARK 1 TITL MUTAGENIC ANALYSIS OF THE ROLES OF SH2 AND SH3 DOMAINS IN
REMARK 1 TITL 2 REGULATION OF THE ABL TYROSINE KINASE
REMARK 1 REF MOL.CELL.BIOL. V. 14 2883 1994
REMARK 1 REFN ISSN 0270-7306
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.MUSACCHIO,M.SARASTE,M.WILMANNS
REMARK 1 TITL HIGH-RESOLUTION CRYSTAL STRUCTURES OF TYROSINE KINASE SH3
REMARK 1 TITL 2 DOMAINS COMPLEXED WITH PROLINE-RICH PEPTIDES
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 546 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.REN,B.J.MAYER,P.CICCHETTI,D.BALTIMORE
REMARK 1 TITL IDENTIFICATION OF A TEN-AMINO ACID PROLINE-RICH SH3 BINDING
REMARK 1 TITL 2 SITE
REMARK 1 REF SCIENCE V. 259 1157 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.E.NOBLE,A.MUSACCHIO,M.SARASTE,S.A.COURTNEIDGE,R.K.WIERENGA
REMARK 1 TITL CRYSTAL STRUCTURE OF THE SH3 DOMAIN IN HUMAN FYN; COMPARISON
REMARK 1 TITL 2 OF THE THREE-DIMENSIONAL STRUCTURES OF SH3 DOMAINS IN
REMARK 1 TITL 3 TYROSINE KINASES AND SPECTRIN
REMARK 1 REF EMBO J. V. 12 2617 1993
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.OVERDUIN,C.B.RIOS,B.J.MAYER,D.BALTIMORE,D.COWBURN
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2
REMARK 1 TITL 2 DOMAIN OF C-ABL
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 70 697 1992
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 6
REMARK 1 AUTH A.MUSACCHIO,M.NOBLE,R.PAUPTIT,R.WIERENGA,M.SARASTE
REMARK 1 TITL CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN
REMARK 1 REF NATURE V. 359 851 1992
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 2.1
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED REDAC STRATEGY
REMARK 4
REMARK 4 1AWO 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_1000171347.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQX; HTQC; H/13C HSQC; 1H-13C
REMARK 210 HQQC; NOESY; NOESY-HMQC; J-HMQC;
REMARK 210 EXCHANGE; 15N{1H NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : GE OMEGA 400; DMX-600
REMARK 210 SPECTROMETER MANUFACTURER : GE; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : RUNMR, UXNMR, DIANA (REDAC)
REMARK 210 (REDAC)
REMARK 210 METHOD USED : VARIABLE TARGET FUNCTION TORSION
REMARK 210 ANGLE SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 59
REMARK 465 SER A 60
REMARK 465 PRO A 61
REMARK 465 GLY A 62
REMARK 465 GLY A 63
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: 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 LEU A 69 -79.30 -113.13
REMARK 500 1 SER A 75 -57.95 -149.10
REMARK 500 1 ASN A 78 -43.45 -163.47
REMARK 500 1 ASN A 96 -175.38 -176.99
REMARK 500 1 GLU A 98 -66.90 -120.31
REMARK 500 2 LEU A 69 -81.66 -101.62
REMARK 500 2 ASP A 77 170.27 -46.04
REMARK 500 2 ASN A 78 110.74 -39.30
REMARK 500 2 LYS A 84 -177.36 -68.39
REMARK 500 2 LYS A 87 70.30 -69.29
REMARK 500 2 ASN A 94 -74.82 -69.63
REMARK 500 2 HIS A 95 -67.26 165.69
REMARK 500 3 ALA A 74 94.26 -48.07
REMARK 500 3 ASP A 77 52.01 -112.80
REMARK 500 3 ASN A 78 41.86 168.01
REMARK 500 3 LYS A 84 -175.30 -58.07
REMARK 500 3 LYS A 87 80.83 -69.11
REMARK 500 3 HIS A 95 -80.44 -38.35
REMARK 500 4 LEU A 69 -76.41 -83.35
REMARK 500 4 VAL A 73 -151.91 -105.25
REMARK 500 4 ALA A 74 164.03 -44.82
REMARK 500 4 ASP A 77 -165.28 66.78
REMARK 500 4 LYS A 84 178.56 -57.96
REMARK 500 4 HIS A 95 170.23 154.13
REMARK 500 4 ASN A 96 28.92 41.12
REMARK 500 4 GLU A 98 -63.16 -102.66
REMARK 500 5 ALA A 74 100.19 -55.25
REMARK 500 5 ASN A 78 -0.47 79.12
REMARK 500 5 LYS A 87 90.07 -69.81
REMARK 500 5 HIS A 95 41.40 37.51
REMARK 500 5 ASN A 96 169.15 177.65
REMARK 500 6 LEU A 69 -80.80 -90.74
REMARK 500 6 SER A 75 -67.41 -149.73
REMARK 500 6 VAL A 119 -111.28 -77.80
REMARK 500 7 ASP A 77 -68.71 -106.69
REMARK 500 7 LYS A 87 81.48 -69.32
REMARK 500 7 ASN A 94 -151.55 -71.16
REMARK 500 7 ASN A 96 45.20 -84.72
REMARK 500 7 VAL A 119 -103.41 -69.05
REMARK 500 8 LEU A 69 -77.66 -77.80
REMARK 500 8 ASP A 77 85.47 -166.86
REMARK 500 8 ASN A 78 68.29 38.99
REMARK 500 8 LYS A 84 -176.22 -62.25
REMARK 500 8 HIS A 95 41.73 -91.21
REMARK 500 8 ASN A 96 -53.39 -168.80
REMARK 500 8 ASN A 106 58.71 -150.16
REMARK 500 9 LEU A 65 64.47 -110.64
REMARK 500 9 ASP A 77 -167.02 -64.14
REMARK 500 9 ASN A 78 101.84 -43.06
REMARK 500 9 LYS A 84 -177.81 -65.36
REMARK 500
REMARK 500 THIS ENTRY HAS 121 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AWO A 65 119 UNP P00519 ABL1_HUMAN 65 119
SEQADV 1AWO GLY A 59 UNP P00519 SER 59 CONFLICT
SEQADV 1AWO SER A 60 UNP P00519 GLU 60 CONFLICT
SEQADV 1AWO PRO A 61 UNP P00519 ASN 61 CONFLICT
SEQADV 1AWO GLY A 62 UNP P00519 ASP 62 CONFLICT
SEQADV 1AWO GLY A 63 UNP P00519 PRO 63 CONFLICT
SEQADV 1AWO SER A 64 UNP P00519 ASN 64 CONFLICT
SEQADV 1AWO SER A 120 UNP P00519 ASN 120 CONFLICT
SEQRES 1 A 62 GLY SER PRO GLY GLY SER LEU PHE VAL ALA LEU TYR ASP
SEQRES 2 A 62 PHE VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS
SEQRES 3 A 62 GLY GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY
SEQRES 4 A 62 GLU TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP
SEQRES 5 A 62 VAL PRO SER ASN TYR ILE THR PRO VAL SER
SHEET 1 A 2 PHE A 66 ALA A 68 0
SHEET 2 A 2 ILE A 116 PRO A 118 -1 N THR A 117 O VAL A 67
SHEET 1 B 3 GLN A 108 PRO A 112 0
SHEET 2 B 3 TRP A 99 GLN A 103 -1 N ALA A 102 O GLY A 109
SHEET 3 B 3 VAL A 90 TYR A 93 -1 N GLY A 92 O GLU A 101
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