Header list of 1mw4.pdb file
Complete list - y 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR/TRANSFERASE 27-SEP-02 1MW4
TITLE SOLUTION STRUCTURE OF THE HUMAN GRB7-SH2 DOMAIN IN COMPLEX WITH A 10
TITLE 2 AMINO ACID PEPTIDE PY1139
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: GRB7 ADAPTER PROTEIN, EPIDERMAL GROWTH FACTOR RECEPTOR GRB-
COMPND 6 7, B47;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RECEPTOR PROTEIN-TYROSINE KINASE ERBB-2;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SH2 DOMAIN BINDING SITE;
COMPND 12 SYNONYM: PY1139, NEU PROTO-ONCOGENE, C-ERBB-2, TYROSINE KINASE-TYPE
COMPND 13 CELL SURFACE RECEPTOR HER2, MLN 19;
COMPND 14 EC: 2.7.10.1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX2T;
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 SH2 DOMAIN IN COMPLEX WITH A LIGAND, HORMONE-GROWTH FACTOR-
KEYWDS 2 TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.IVANCIC,B.A.LYONS
REVDAT 3 02-MAY-12 1MW4 1 COMPND VERSN
REVDAT 2 24-FEB-09 1MW4 1 VERSN
REVDAT 1 09-SEP-03 1MW4 0
JRNL AUTH M.IVANCIC,R.J.DALY,B.A.LYONS
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN GRB7-SH2 DOMAIN/ERBB2
JRNL TITL 2 PEPTIDE COMPLEX AND STRUCTURAL BASIS FOR GRB7 BINDING TO
JRNL TITL 3 ERBB2
JRNL REF J.BIOMOL.NMR V. 27 205 2003
JRNL REFN ISSN 0925-2738
JRNL PMID 12975581
JRNL DOI 10.1023/A:1025498409113
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.J.BRESCIA,M.IVANCIC,B.A.LYONS
REMARK 1 TITL ASSIGNMENT OF BACKBONE 1H, 13C, AND 15N RESONANCES OF HUMAN
REMARK 1 TITL 2 GRB7-SH2 DOMAIN IN COMPLEX WITH A PHOSPHORYLATED PEPTIDE
REMARK 1 TITL 3 LIGAND
REMARK 1 REF J.BIOMOL.NMR V. 23 77 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1015345302576
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON A TOTAL OF 1904 RESTRAINTS: 1660
REMARK 3 ARE NOE DERIVED, 120 ARE DIHEDRAL RESTRAINTS AND 124 ARE
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1MW4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-02.
REMARK 100 THE RCSB ID CODE IS RCSB017238.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1ATM
REMARK 210 SAMPLE CONTENTS : 0.7MM GRB7 SH2 U-15N, 13C, 50MM
REMARK 210 ACETATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.6, ANSIG 3.3, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON-
REMARK 210 BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 ASP A 92 H LEU A 96 1.42
REMARK 500 O VAL A 39 H GLY A 41 1.45
REMARK 500 OE1 GLU A 47 H SER A 48 1.49
REMARK 500 O THR A 88 H PHE A 90 1.58
REMARK 500 O THR A 88 N PHE A 90 2.15
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 2 -64.78 -150.21
REMARK 500 1 PRO A 3 107.58 -58.93
REMARK 500 1 ALA A 4 -47.96 -149.59
REMARK 500 1 THR A 7 -74.81 -135.57
REMARK 500 1 ALA A 12 78.28 -150.05
REMARK 500 1 THR A 16 -147.04 -141.10
REMARK 500 1 GLN A 17 31.88 -99.34
REMARK 500 1 SER A 25 88.93 -41.68
REMARK 500 1 ASP A 40 54.29 -68.59
REMARK 500 1 GLU A 47 -116.39 -142.33
REMARK 500 1 GLN A 53 65.04 -111.26
REMARK 500 1 LEU A 62 39.61 -94.00
REMARK 500 1 GLN A 63 -40.26 -152.80
REMARK 500 1 LYS A 64 -158.83 -154.03
REMARK 500 1 ILE A 70 -38.93 -143.10
REMARK 500 1 SER A 73 99.05 -62.94
REMARK 500 1 ARG A 78 -111.15 -135.05
REMARK 500 1 SER A 82 -115.12 -150.15
REMARK 500 1 ASP A 85 38.88 -140.41
REMARK 500 1 ARG A 89 64.60 -39.66
REMARK 500 1 PHE A 90 -156.77 -141.49
REMARK 500 1 THR A 91 165.26 -46.93
REMARK 500 1 ASP A 92 -69.41 -150.19
REMARK 500 1 LEU A 93 -72.28 -39.73
REMARK 500 1 ASN A 103 -159.25 -105.56
REMARK 500 1 LEU A 107 -100.71 -29.79
REMARK 500 1 PRO A 108 50.00 -105.53
REMARK 500 1 LEU A 110 92.78 -44.70
REMARK 500 1 CYS A 114 -85.33 -140.27
REMARK 500 1 VAL A 118 -69.06 -140.93
REMARK 500 1 ALA A 119 -84.29 -80.05
REMARK 500 1 GLN B1136 -52.35 -157.42
REMARK 500 1 PRO B1137 -146.87 -69.70
REMARK 500 1 GLU B1138 -68.82 -147.67
REMARK 500 1 PTR B1139 -141.22 15.93
REMARK 500 1 ASN B1141 -29.94 89.92
REMARK 500 1 GLN B1142 172.55 176.88
REMARK 500 1 PRO B1143 -6.11 -57.21
REMARK 500 2 SER A 2 -64.74 -150.14
REMARK 500 2 PRO A 3 87.17 -58.55
REMARK 500 2 THR A 16 -86.22 -141.06
REMARK 500 2 GLN A 17 21.66 -150.36
REMARK 500 2 TRP A 19 57.70 -140.05
REMARK 500 2 ARG A 23 99.63 -67.83
REMARK 500 2 SER A 25 93.75 -34.81
REMARK 500 2 LEU A 32 -64.21 -103.29
REMARK 500 2 ASP A 40 54.26 -62.21
REMARK 500 2 PRO A 52 -34.21 -39.57
REMARK 500 2 LEU A 62 35.76 -93.85
REMARK 500 2 GLN A 63 -32.95 -152.98
REMARK 500
REMARK 500 THIS ENTRY HAS 332 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5288 RELATED DB: BMRB
REMARK 900 BACKBONE N, HN, CA AND CB ASSIGNMENTS FOR HGRB7-SH2 DOMAIN
DBREF 1MW4 A 3 120 UNP Q14451 GRB7_HUMAN 415 532
DBREF 1MW4 B 1135 1144 UNP P04626 ERBB2_HUMAN 1135 1144
SEQADV 1MW4 GLY A 1 UNP Q14451 CLONING ARTIFACT
SEQADV 1MW4 SER A 2 UNP Q14451 CLONING ARTIFACT
SEQADV 1MW4 PTR B 1139 UNP P04626 TYR 1139 MODIFIED RESIDUE
SEQRES 1 A 120 GLY SER PRO ALA SER GLY THR SER LEU SER ALA ALA ILE
SEQRES 2 A 120 HIS ARG THR GLN LEU TRP PHE HIS GLY ARG ILE SER ARG
SEQRES 3 A 120 GLU GLU SER GLN ARG LEU ILE GLY GLN GLN GLY LEU VAL
SEQRES 4 A 120 ASP GLY LEU PHE LEU VAL ARG GLU SER GLN ARG ASN PRO
SEQRES 5 A 120 GLN GLY PHE VAL LEU SER LEU CYS HIS LEU GLN LYS VAL
SEQRES 6 A 120 LYS HIS TYR LEU ILE LEU PRO SER GLU GLU GLU GLY ARG
SEQRES 7 A 120 LEU TYR PHE SER MET ASP ASP GLY GLN THR ARG PHE THR
SEQRES 8 A 120 ASP LEU LEU GLN LEU VAL GLU PHE HIS GLN LEU ASN ARG
SEQRES 9 A 120 GLY ILE LEU PRO CYS LEU LEU ARG HIS CYS CYS THR ARG
SEQRES 10 A 120 VAL ALA LEU
SEQRES 1 B 10 PRO GLN PRO GLU PTR VAL ASN GLN PRO ASP
MODRES 1MW4 PTR B 1139 TYR O-PHOSPHOTYROSINE
HET PTR B1139 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 SER A 25 ILE A 33 1 9
HELIX 2 2 GLY A 34 GLN A 36 5 3
HELIX 3 3 ASP A 92 HIS A 100 1 9
SHEET 1 A 4 PHE A 20 HIS A 21 0
SHEET 2 A 4 LEU A 44 GLU A 47 1 O GLU A 47 N HIS A 21
SHEET 3 A 4 PHE A 55 CYS A 60 -1 O SER A 58 N LEU A 44
SHEET 4 A 4 VAL A 65 LEU A 69 -1 O TYR A 68 N LEU A 57
LINK C GLU B1138 N PTR B1139 1555 1555 1.33
LINK C PTR B1139 N VAL B1140 1555 1555 1.33
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 - y 9 2 Bytes