Header list of 1zsg.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 24-MAY-05 1ZSG
TITLE BETA PIX-SH3 COMPLEXED WITH AN ATYPICAL PEPTIDE FROM ALPHA-PAK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 179-243;
COMPND 5 SYNONYM: PAK-INTERACTING EXCHANGE FACTOR BETA, BETA-PIX, COOL-1, P85,
COMPND 6 PIX-SH3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SEQUENCE DATABASE RESIDUES 183-204;
COMPND 12 SYNONYM: P21-ACTIVATED KINASE 1, PAK-1, P65-PAK, ALPHA-PAK, PAK
COMPND 13 PEPTIDE;
COMPND 14 EC: 2.7.1.37;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ARHGEF7, COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET16B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 13 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS SH3-PEPTIDE COMPLEX, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR H.R.MOTT,D.NIETLISPACH,K.A.EVETTS,D.OWEN
REVDAT 3 02-MAR-22 1ZSG 1 REMARK
REVDAT 2 24-FEB-09 1ZSG 1 VERSN
REVDAT 1 30-AUG-05 1ZSG 0
JRNL AUTH H.R.MOTT,D.NIETLISPACH,K.A.EVETTS,D.OWEN
JRNL TITL STRUCTURAL ANALYSIS OF THE SH3 DOMAIN OF BETA-PIX AND ITS
JRNL TITL 2 INTERACTION WITH ALPHA-P21 ACTIVATED KINASE (PAK)
JRNL REF BIOCHEMISTRY V. 44 10977 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16101281
JRNL DOI 10.1021/BI050374A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TOTAL OF 1788 UNAMBIGUOUS AND 761
REMARK 3 AMBIGUOUS NOE DERIEVED DISTANCE RESTRAINTS, 33 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1ZSG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000033063.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.3; 7.3
REMARK 210 IONIC STRENGTH : 100 MM NA2SO4; 100 MM NA2SO4
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM 15N LABELLED PIX-SH3
REMARK 210 COMPLEXED WITH 1.2 MM PEPTIDE IN
REMARK 210 20 MM NA2HPO4/NAH2PO4, PH 7.3,
REMARK 210 100MM NA2SO4, 0.05% NAN3, 90%
REMARK 210 H2O, 10% D2O; 1MM 15N,13C
REMARK 210 LABELLED PIX-SH3 COMPLEXED WITH
REMARK 210 1.2 MM PEPTIDE IN 20 MM NA2HPO4/
REMARK 210 NAH2PO4, PH 7.3, 100MM NA2SO4,
REMARK 210 0.05% NAN3, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 13C,15N-
REMARK 210 FILTERED, 13C-SEPARATED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.7, ANSIG 3.3, ARIA 1.2,
REMARK 210 CNS 1.1
REMARK 210 METHOD USED : SIMLUATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS FOLLOWED BY
REMARK 210 CARTESIAN DYNAMICS COOLING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 7 123.93 65.34
REMARK 500 1 LYS A 14 -67.59 -97.65
REMARK 500 1 LYS A 29 100.73 -45.18
REMARK 500 1 ILE B 190 142.74 64.70
REMARK 500 1 PRO B 194 -172.70 -68.35
REMARK 500 1 THR B 197 -79.98 63.23
REMARK 500 1 LYS B 198 -165.48 -69.09
REMARK 500 1 SER B 199 112.46 57.51
REMARK 500 1 THR B 202 132.56 67.24
REMARK 500 2 SER A 5 -9.30 -155.64
REMARK 500 2 ASN A 7 14.34 -149.00
REMARK 500 2 GLU A 24 -153.70 -97.21
REMARK 500 2 LYS A 29 104.27 -43.48
REMARK 500 2 ASN A 49 108.05 -54.76
REMARK 500 2 LYS A 64 110.62 62.58
REMARK 500 2 ILE B 190 153.87 63.52
REMARK 500 2 ARG B 193 100.61 -164.84
REMARK 500 2 LYS B 198 -85.29 61.92
REMARK 500 2 SER B 199 96.79 -169.94
REMARK 500 2 VAL B 200 -154.08 -142.88
REMARK 500 2 TYR B 201 -164.10 -69.53
REMARK 500 3 LYS A 14 -61.70 -98.42
REMARK 500 3 LYS A 29 99.40 -44.54
REMARK 500 3 GLU A 39 -151.74 -98.58
REMARK 500 3 ASN A 49 106.56 -55.36
REMARK 500 3 VAL B 189 -157.15 -114.87
REMARK 500 3 PRO B 194 -74.81 -86.43
REMARK 500 3 GLU B 195 -31.27 -150.45
REMARK 500 3 THR B 197 105.82 62.97
REMARK 500 3 TYR B 201 102.34 60.59
REMARK 500 3 THR B 202 -172.61 53.48
REMARK 500 4 ASP A 3 24.94 -159.52
REMARK 500 4 ASN A 4 -17.88 -153.50
REMARK 500 4 SER A 5 -82.94 61.51
REMARK 500 4 ASN A 6 171.39 61.96
REMARK 500 4 LYS A 14 -65.76 -96.44
REMARK 500 4 LYS A 29 104.45 -43.38
REMARK 500 4 ASN A 49 101.18 -52.58
REMARK 500 4 LYS A 64 89.07 59.91
REMARK 500 4 ILE B 190 139.21 63.51
REMARK 500 4 PRO B 194 -166.00 -71.80
REMARK 500 4 HIS B 196 -176.91 61.15
REMARK 500 4 THR B 197 -84.75 61.61
REMARK 500 4 LYS B 198 -87.40 58.08
REMARK 500 4 VAL B 200 -151.85 -101.03
REMARK 500 5 SER A 5 -159.74 51.10
REMARK 500 5 ASN A 7 84.33 -150.99
REMARK 500 5 LYS A 29 98.58 -45.45
REMARK 500 5 ASN A 49 108.27 -52.39
REMARK 500 5 ILE B 190 143.29 64.45
REMARK 500
REMARK 500 THIS ENTRY HAS 311 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZSG A 1 65 UNP Q14155 ARHG7_HUMAN 179 243
DBREF 1ZSG B 183 204 UNP Q13153 PAK1_HUMAN 183 204
SEQRES 1 A 65 MET THR ASP ASN SER ASN ASN GLN LEU VAL VAL ARG ALA
SEQRES 2 A 65 LYS PHE ASN PHE GLN GLN THR ASN GLU ASP GLU LEU SER
SEQRES 3 A 65 PHE SER LYS GLY ASP VAL ILE HIS VAL THR ARG VAL GLU
SEQRES 4 A 65 GLU GLY GLY TRP TRP GLU GLY THR LEU ASN GLY ARG THR
SEQRES 5 A 65 GLY TRP PHE PRO SER ASN TYR VAL ARG GLU VAL LYS ALA
SEQRES 1 B 22 ASP ALA THR PRO PRO PRO VAL ILE ALA PRO ARG PRO GLU
SEQRES 2 B 22 HIS THR LYS SER VAL TYR THR ARG SER
SHEET 1 A 5 ARG A 51 PRO A 56 0
SHEET 2 A 5 TRP A 43 LEU A 48 -1 N TRP A 44 O PHE A 55
SHEET 3 A 5 VAL A 32 ARG A 37 -1 N THR A 36 O GLU A 45
SHEET 4 A 5 VAL A 10 ALA A 13 -1 N VAL A 11 O ILE A 33
SHEET 5 A 5 VAL A 60 GLU A 62 -1 O ARG A 61 N ARG A 12
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