Header list of 1z3k.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-MAR-05 1Z3K
TITLE STRUCTURAL INSIGHT INTO THE BINDING DIVERSITY BETWEEN THE TYR-
TITLE 2 PHOSPHORYLATED HUMAN EPHRINBS AND NCK2 SH2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: NCK ADAPTOR PROTEIN 2, SH2/SH3 ADAPTOR PROTEIN NCK-BETA,
COMPND 6 NCK-2;
COMPND 7 ENGINEERED: 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
KEYWDS NCK2, SH2 DOMAIN, EPH RECEPTOR-EPHRIN MEDIATED SIGNALING, STRUCTURAL
KEYWDS 2 GENOMICS, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR X.RAN,J.SONG
REVDAT 4 02-MAR-22 1Z3K 1 REMARK
REVDAT 3 24-FEB-09 1Z3K 1 VERSN
REVDAT 2 21-JUN-05 1Z3K 1 JRNL
REVDAT 1 29-MAR-05 1Z3K 0
JRNL AUTH X.RAN,J.SONG
JRNL TITL STRUCTURAL INSIGHT INTO THE BINDING DIVERSITY BETWEEN THE
JRNL TITL 2 TYR-PHOSPHORYLATED HUMAN EPHRINBS AND NCK2 SH2 DOMAIN.
JRNL REF J.BIOL.CHEM. V. 280 19205 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15764601
JRNL DOI 10.1074/JBC.M500330200
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 1Z3K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032253.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM NCK2 SH2 DOMAIN U-15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER NA; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES ACCEPTED BY CNS
REMARK 210 PROGRAM WITH THE LOWEST ENERGY
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 17 H ARG A 20 1.56
REMARK 500 O THR A 9 H HIS A 11 1.58
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 THR A 9 169.13 177.53
REMARK 500 1 ARG A 10 -55.16 68.82
REMARK 500 1 GLU A 19 -33.51 -39.50
REMARK 500 1 ARG A 20 70.25 85.55
REMARK 500 1 GLU A 23 -173.99 47.76
REMARK 500 1 SER A 45 81.15 -60.96
REMARK 500 1 ASP A 57 57.64 32.33
REMARK 500 1 GLN A 64 43.88 -140.17
REMARK 500 1 MET A 70 -77.65 -121.89
REMARK 500 1 TYR A 77 52.11 34.57
REMARK 500 1 LYS A 78 -125.09 -62.20
REMARK 500 1 PRO A 81 11.85 -54.34
REMARK 500 1 GLU A 89 -178.00 70.77
REMARK 500 1 VAL A 94 -107.95 -105.66
REMARK 500 1 LEU A 97 -174.91 47.95
REMARK 500 2 GLU A 2 26.73 46.18
REMARK 500 2 TYR A 5 -33.54 168.26
REMARK 500 2 THR A 9 -177.91 57.45
REMARK 500 2 ARG A 10 -56.26 72.75
REMARK 500 2 ARG A 20 90.10 118.40
REMARK 500 2 GLU A 23 -136.96 39.09
REMARK 500 2 SER A 45 80.55 -67.66
REMARK 500 2 ASP A 57 61.61 34.49
REMARK 500 2 HIS A 68 42.67 -86.69
REMARK 500 2 MET A 70 -110.39 -122.83
REMARK 500 2 HIS A 76 16.03 -154.81
REMARK 500 2 TYR A 77 73.36 42.16
REMARK 500 2 LYS A 78 -72.29 -49.49
REMARK 500 2 VAL A 94 -99.75 -49.66
REMARK 500 2 LEU A 97 117.28 68.57
REMARK 500 3 TRP A 3 -132.35 -121.12
REMARK 500 3 THR A 9 147.13 117.48
REMARK 500 3 ARG A 10 -44.64 31.90
REMARK 500 3 GLU A 19 -67.72 177.64
REMARK 500 3 ARG A 20 -19.78 147.00
REMARK 500 3 GLU A 23 -91.18 45.20
REMARK 500 3 SER A 36 33.74 -158.54
REMARK 500 3 SER A 45 80.91 -63.31
REMARK 500 3 ASP A 57 51.69 32.35
REMARK 500 3 HIS A 68 30.29 -82.31
REMARK 500 3 MET A 70 -79.58 -133.12
REMARK 500 3 HIS A 76 27.95 -156.10
REMARK 500 3 LYS A 78 -125.71 -68.80
REMARK 500 3 PRO A 81 8.69 -68.59
REMARK 500 3 VAL A 94 -100.39 -53.87
REMARK 500 4 GLU A 2 -80.03 62.85
REMARK 500 4 TYR A 5 -81.12 -179.62
REMARK 500 4 VAL A 8 -98.19 -101.06
REMARK 500 4 THR A 9 179.81 -46.77
REMARK 500 4 ARG A 10 -54.15 74.09
REMARK 500
REMARK 500 THIS ENTRY HAS 173 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z3K A 1 98 UNP O43639 NCK2_HUMAN 283 380
SEQRES 1 A 98 ARG GLU TRP TYR TYR GLY ASN VAL THR ARG HIS GLN ALA
SEQRES 2 A 98 GLU CYS ALA LEU ASN GLU ARG GLY VAL GLU GLY ASP PHE
SEQRES 3 A 98 LEU ILE ARG ASP SER GLU SER SER PRO SER ASP PHE SER
SEQRES 4 A 98 VAL SER LEU LYS ALA SER GLY LYS ASN LYS HIS PHE LYS
SEQRES 5 A 98 VAL GLN LEU VAL ASP ASN VAL TYR CYS ILE GLY GLN ARG
SEQRES 6 A 98 ARG PHE HIS THR MET ASP GLU LEU VAL GLU HIS TYR LYS
SEQRES 7 A 98 LYS ALA PRO ILE PHE THR SER GLU HIS GLY GLU LYS LEU
SEQRES 8 A 98 TYR LEU VAL ARG ALA LEU GLN
HELIX 1 1 HIS A 11 ASN A 18 1 8
HELIX 2 2 GLU A 72 TYR A 77 1 6
SHEET 1 A 4 PHE A 26 ASP A 30 0
SHEET 2 A 4 ASP A 37 LYS A 43 -1 O SER A 39 N ARG A 29
SHEET 3 A 4 ASN A 48 VAL A 56 -1 O VAL A 53 N PHE A 38
SHEET 4 A 4 VAL A 59 ILE A 62 -1 O CYS A 61 N GLN A 54
SHEET 1 B 2 THR A 84 SER A 85 0
SHEET 2 B 2 GLU A 89 LYS A 90 -1 O GLU A 89 N SER A 85
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 2 2 Bytes