Header list of 1mke.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 29-AUG-02 1MKE
TITLE STRUCTURE OF THE N-WASP EVH1 DOMAIN-WIP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUSION PROTEIN CONSISTING OF WISKOTT-ALDRICH SYNDROME
COMPND 3 PROTEIN INTERACTING PROTEIN (WIP), GSGSG LINKER, AND NEURAL WISKOTT-
COMPND 4 ALDRICH SYNDROME PROTEIN (N-WASP);
COMPND 5 CHAIN: A;
COMPND 6 FRAGMENT: WIP PEPTIDE AND N-WASP EVH1 DOMAIN;
COMPND 7 SYNONYM: WIP - N-WASP;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: FUSION PROTEIN COMPRISES RESIDUES 461-485 OF WIP, A
COMPND 10 GSGSG LINKER SEQUENCE, AND RESIDUES 26-147 (EVH1 DOMAIN) OF N-WASP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT, HUMAN;
SOURCE 4 ORGANISM_TAXID: 10116,9606;
SOURCE 5 STRAIN: ,;
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: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBH4
KEYWDS POLYPROLINE, PROTEIN-PROTEIN COMPLEX, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR B.F.VOLKMAN,K.E.PREHODA,J.A.SCOTT,F.C.PETERSON,W.A.LIM
REVDAT 3 23-FEB-22 1MKE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1MKE 1 VERSN
REVDAT 1 04-DEC-02 1MKE 0
JRNL AUTH B.F.VOLKMAN,K.E.PREHODA,J.A.SCOTT,F.C.PETERSON,W.A.LIM
JRNL TITL STRUCTURE OF THE N-WASP EVH1 DOMAIN-WIP COMPLEX. INSIGHT
JRNL TITL 2 INTO THE MOLECULAR BASIS OF WISKOTT-ALDRICH SYNDROME.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 111 565 2002
JRNL REFN ISSN 0092-8674
JRNL PMID 12437929
JRNL DOI 10.1016/S0092-8674(02)01076-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT, P. (DYANA), GUENTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FINAL STRUCTURES WERE DERIVED FROM A
REMARK 3 TOTAL OF 1884 NON-TRIVIAL NOE DISTANCE CONSTRAINTS, INCLUDING
REMARK 3 135 RESTRAINTS BETWEEN RESIDUES OF THE WIP PEPTIDE AND THE EVH1
REMARK 3 DOMAIN. 143 PHI AND PSI TORSION ANGLE CONSTRAINTS WERE GENERATED
REMARK 3 FROM CHEMICAL SHIFT DATABASE SEARCHING USING THE PROGRAM TALOS
REMARK 4
REMARK 4 1MKE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000016979.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N PROTEIN 20 MM PO4 BUFFER 1
REMARK 210 MM DITHIOTHREITOL; U-13C/15N
REMARK 210 PROTEIN 20 MM PO4 BUFFER 1 MM
REMARK 210 DITHIOTHREITOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, XEASY 1.3, NMRPIPE
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: REPRESENTATIVE CONFORMER (MODEL 1) IS MINIMIZED
REMARK 210 AVERAGE STRUCTURE.
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 1-21
REMARK 465 RES C SSSEQI
REMARK 465 ARG A 145
REMARK 465 LYS A 146
REMARK 465 SER A 147
REMARK 465 GLU A 148
REMARK 465 LYS A 149
REMARK 465 ARG A 150
REMARK 465 ARG A 151
REMARK 465 ASP A 152
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 H ASP A 72 O SER A 77 1.46
REMARK 500 O VAL A 41 H LYS A 71 1.52
REMARK 500 H ALA A 46 O ALA A 67 1.55
REMARK 500 O THR A 137 H GLY A 141 1.56
REMARK 500 H GLN A 49 O ASN A 122 1.57
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 11 -91.69 -148.59
REMARK 500 1 GLU A 23 141.33 65.54
REMARK 500 1 SER A 24 176.38 -49.06
REMARK 500 1 ARG A 25 74.86 67.11
REMARK 500 1 SER A 27 103.03 -167.16
REMARK 500 1 SER A 29 175.58 159.81
REMARK 500 1 PHE A 33 -82.37 -40.32
REMARK 500 1 SER A 34 -161.40 170.14
REMARK 500 1 PHE A 35 -62.14 -157.97
REMARK 500 1 LYS A 39 89.51 -150.28
REMARK 500 1 MET A 43 -71.07 -109.41
REMARK 500 1 ALA A 53 83.27 -61.81
REMARK 500 1 ARG A 55 177.32 -52.30
REMARK 500 1 CYS A 57 82.40 49.17
REMARK 500 1 MET A 58 104.69 -160.73
REMARK 500 1 CYS A 63 128.39 -179.36
REMARK 500 1 ASN A 98 157.51 -40.19
REMARK 500 1 SER A 104 69.00 -156.77
REMARK 500 1 TYR A 108 42.76 -143.03
REMARK 500 1 ARG A 143 -161.00 41.01
REMARK 500 2 THR A 11 -52.59 -144.77
REMARK 500 2 THR A 12 -64.02 -173.81
REMARK 500 2 LYS A 13 149.20 61.67
REMARK 500 2 LYS A 18 56.87 -153.12
REMARK 500 2 ARG A 21 91.66 -163.40
REMARK 500 2 ASN A 22 -61.63 -108.62
REMARK 500 2 GLU A 23 68.45 -156.29
REMARK 500 2 SER A 29 84.86 -168.99
REMARK 500 2 SER A 31 -57.77 -130.40
REMARK 500 2 LEU A 32 -62.59 -154.08
REMARK 500 2 LEU A 36 55.41 -162.11
REMARK 500 2 LYS A 38 173.39 73.36
REMARK 500 2 LYS A 39 70.68 76.44
REMARK 500 2 SER A 44 145.36 -171.20
REMARK 500 2 ASP A 54 166.21 -44.12
REMARK 500 2 CYS A 63 99.21 171.92
REMARK 500 2 ARG A 76 54.14 35.33
REMARK 500 2 GLU A 95 74.94 -102.96
REMARK 500 2 LEU A 96 146.56 -34.35
REMARK 500 2 ASN A 99 61.56 60.64
REMARK 500 2 SER A 104 64.91 -174.64
REMARK 500 2 ASP A 115 -88.67 57.20
REMARK 500 2 ARG A 143 43.04 38.95
REMARK 500 3 GLN A 10 125.40 -39.53
REMARK 500 3 LYS A 18 57.11 -148.93
REMARK 500 3 ASN A 22 75.20 176.03
REMARK 500 3 GLU A 23 -61.32 -170.71
REMARK 500 3 ARG A 25 -57.54 -129.76
REMARK 500 3 SER A 27 119.48 175.94
REMARK 500 3 SER A 31 112.10 58.73
REMARK 500
REMARK 500 THIS ENTRY HAS 440 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MKE A 1 25 UNP O43516 WAIP_HUMAN 461 485
DBREF 1MKE A 31 152 UNP O08816 WASL_RAT 26 147
SEQADV 1MKE GLY A 26 UNP O43516 LINKER
SEQADV 1MKE SER A 27 UNP O43516 LINKER
SEQADV 1MKE GLY A 28 UNP O43516 LINKER
SEQADV 1MKE SER A 29 UNP O43516 LINKER
SEQADV 1MKE GLY A 30 UNP O43516 LINKER
SEQRES 1 A 152 ASP LEU PRO PRO PRO GLU PRO TYR VAL GLN THR THR LYS
SEQRES 2 A 152 SER TYR PRO SER LYS LEU ALA ARG ASN GLU SER ARG GLY
SEQRES 3 A 152 SER GLY SER GLY SER LEU PHE SER PHE LEU GLY LYS LYS
SEQRES 4 A 152 CYS VAL THR MET SER SER ALA VAL VAL GLN LEU TYR ALA
SEQRES 5 A 152 ALA ASP ARG ASN CYS MET TRP SER LYS LYS CYS SER GLY
SEQRES 6 A 152 VAL ALA CYS LEU VAL LYS ASP ASN PRO GLN ARG SER TYR
SEQRES 7 A 152 PHE LEU ARG ILE PHE ASP ILE LYS ASP GLY LYS LEU LEU
SEQRES 8 A 152 TRP GLU GLN GLU LEU TYR ASN ASN PHE VAL TYR ASN SER
SEQRES 9 A 152 PRO ARG GLY TYR PHE HIS THR PHE ALA GLY ASP THR CYS
SEQRES 10 A 152 GLN VAL ALA LEU ASN PHE ALA ASN GLU GLU GLU ALA LYS
SEQRES 11 A 152 LYS PHE ARG LYS ALA VAL THR ASP LEU LEU GLY ARG ARG
SEQRES 12 A 152 GLN ARG LYS SER GLU LYS ARG ARG ASP
HELIX 1 1 ASN A 125 ARG A 143 1 19
SHEET 1 A 6 LEU A 90 GLU A 95 0
SHEET 2 A 6 SER A 77 PHE A 83 -1 N LEU A 80 O GLN A 94
SHEET 3 A 6 MET A 58 ASP A 72 -1 N ASP A 72 O SER A 77
SHEET 4 A 6 VAL A 41 ASP A 54 -1 N VAL A 41 O LYS A 71
SHEET 5 A 6 GLN A 118 PHE A 123 -1 O ASN A 122 N GLN A 49
SHEET 6 A 6 PHE A 109 ALA A 113 -1 N HIS A 110 O LEU A 121
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 23 2 Bytes