Header list of 1ab2.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 19-JUL-93 1AB2
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF
TITLE 2 C-ABL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-ABL TYROSINE KINASE SH2 DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.112;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRANSFERASE(PHOSPHOTRANSFERASE)
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.OVERDUIN,C.B.RIOS,B.J.MAYER,D.BALTIMORE,D.COWBURN
REVDAT 3 16-FEB-22 1AB2 1 REMARK
REVDAT 2 24-FEB-09 1AB2 1 VERSN
REVDAT 1 31-JAN-94 1AB2 0
JRNL AUTH M.OVERDUIN,C.B.RIOS,B.J.MAYER,D.BALTIMORE,D.COWBURN
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2
JRNL TITL 2 DOMAIN OF C-ABL.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 70 697 1992
JRNL REFN ISSN 0092-8674
JRNL PMID 1505033
JRNL DOI 10.1016/0092-8674(92)90437-H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.OVERDUIN,B.MAYER,C.B.RIOS,D.BALTIMORE,D.COWBURN
REMARK 1 TITL SECONDARY STRUCTURE OF SRC HOMOLOGY 2 DOMAIN OF C-ABL BY
REMARK 1 TITL 2 HETERONUCLEAR NMR SPECTROSCOPY IN SOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 11673 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AB2 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_1000170608.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 O LEU A 34 HG SER A 48 1.38
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 SER A 5 171.80 54.96
REMARK 500 1 LYS A 8 -104.31 -57.63
REMARK 500 1 LEU A 24 -70.95 -55.84
REMARK 500 1 LEU A 25 106.24 -56.76
REMARK 500 1 SER A 27 122.94 61.76
REMARK 500 1 GLU A 37 -165.93 -123.90
REMARK 500 1 TYR A 51 -156.26 -93.42
REMARK 500 1 GLU A 52 22.15 -73.65
REMARK 500 1 ARG A 59 164.18 -42.00
REMARK 500 1 ASN A 61 124.10 71.60
REMARK 500 1 SER A 64 34.27 -91.28
REMARK 500 1 ASP A 65 -54.92 -149.85
REMARK 500 1 LYS A 67 152.54 -43.54
REMARK 500 1 SER A 71 -68.50 -94.44
REMARK 500 1 SER A 72 -26.87 154.52
REMARK 500 1 ASN A 77 -42.76 -134.97
REMARK 500 1 ILE A 94 -84.73 -44.44
REMARK 500 1 LEU A 97 119.92 -36.99
REMARK 500 1 HIS A 98 -79.49 -102.02
REMARK 500 1 HIS A 107 129.96 169.04
REMARK 500 1 ARG A 108 71.87 177.84
REMARK 500 2 SER A 2 -66.63 66.16
REMARK 500 2 ASN A 4 -54.37 -152.13
REMARK 500 2 SER A 5 44.21 -103.46
REMARK 500 2 LEU A 6 144.44 63.00
REMARK 500 2 LYS A 8 -98.81 -48.03
REMARK 500 2 SER A 10 30.33 -82.95
REMARK 500 2 LEU A 25 86.06 -52.71
REMARK 500 2 SER A 26 -107.53 28.39
REMARK 500 2 SER A 27 35.02 175.85
REMARK 500 2 SER A 40 -36.37 -35.78
REMARK 500 2 TYR A 51 -144.69 -109.26
REMARK 500 2 GLU A 52 -80.37 -60.03
REMARK 500 2 ILE A 60 -121.95 -70.14
REMARK 500 2 ASN A 61 119.90 167.91
REMARK 500 2 SER A 64 32.63 36.90
REMARK 500 2 ASP A 65 -56.23 -138.53
REMARK 500 2 SER A 71 -84.82 -116.05
REMARK 500 2 SER A 72 -50.61 176.48
REMARK 500 2 HIS A 86 9.42 -68.01
REMARK 500 2 ALA A 90 72.01 -67.69
REMARK 500 2 ILE A 94 -87.24 -54.74
REMARK 500 2 THR A 95 -148.67 -78.65
REMARK 500 2 LEU A 97 132.54 -23.32
REMARK 500 2 HIS A 98 26.57 -140.24
REMARK 500 2 TYR A 99 46.59 -153.98
REMARK 500 2 ILE A 106 -63.10 -94.13
REMARK 500 2 HIS A 107 59.07 -175.48
REMARK 500 3 ASN A 4 -93.69 39.90
REMARK 500 3 LYS A 8 -94.24 -48.17
REMARK 500
REMARK 500 THIS ENTRY HAS 419 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AB2 A 4 104 UNP P00519 ABL1_HUMAN 120 220
SEQRES 1 A 109 GLY SER GLY ASN SER LEU GLU LYS HIS SER TRP TYR HIS
SEQRES 2 A 109 GLY PRO VAL SER ARG ASN ALA ALA GLU TYR LEU LEU SER
SEQRES 3 A 109 SER GLY ILE ASN GLY SER PHE LEU VAL ARG GLU SER GLU
SEQRES 4 A 109 SER SER PRO GLY GLN ARG SER ILE SER LEU ARG TYR GLU
SEQRES 5 A 109 GLY ARG VAL TYR HIS TYR ARG ILE ASN THR ALA SER ASP
SEQRES 6 A 109 GLY LYS LEU TYR VAL SER SER GLU SER ARG PHE ASN THR
SEQRES 7 A 109 LEU ALA GLU LEU VAL HIS HIS HIS SER THR VAL ALA ASP
SEQRES 8 A 109 GLY LEU ILE THR THR LEU HIS TYR PRO ALA PRO LYS ARG
SEQRES 9 A 109 GLY ILE HIS ARG ASP
HELIX 1 A ARG A 18 LEU A 25 1 8
HELIX 2 B THR A 78 VAL A 89 1 12
SHEET 1 S1 1 TRP A 11 HIS A 13 0
SHEET 1 S2 3 SER A 32 SER A 38 0
SHEET 2 S2 3 GLN A 44 TYR A 51 -1 O ARG A 50 N SER A 32
SHEET 3 S2 3 VAL A 55 ILE A 60 -1 O VAL A 55 N TYR A 51
SHEET 1 S3 3 ASN A 61 ALA A 63 0
SHEET 2 S3 3 LYS A 67 TYR A 69 -1 N TYR A 69 O ASN A 61
SHEET 3 S3 3 ARG A 75 PHE A 76 -1 O PHE A 76 N LEU A 68
SHEET 1 S4 1 LEU A 93 THR A 96 0
SHEET 1 S5 1 ALA A 101 ARG A 104 0
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