Header list of 1cee.pdb file
Complete list - b 16 2 Bytes
HEADER STRUCTURAL PROTEIN REGULATION 08-MAR-99 1CEE
TITLE SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN
TITLE 2 OF WASP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING RHO-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CDC42;
COMPND 5 SYNONYM: CELL DIVISION CYCLE 42, PCDC42;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: WISKOTT-ALDRICH SYNDROME PROTEIN WASP;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: GTPASE BINDING DOMAIN OF WASP;
COMPND 11 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS CDC42 ACTIN REGULATOR GTPASE AND THE GTPASE BINDING DOMAIN OF ITS
KEYWDS 2 EFFECTOR WASP, STRUCTURAL PROTEIN REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.ABDUL-MANAN,B.AGHAZADEH,G.A.LIU,A.MAJUMDAR,O.OUERFELLI,M.K.ROSEN
REVDAT 4 16-FEB-22 1CEE 1 REMARK LINK
REVDAT 3 24-FEB-09 1CEE 1 VERSN
REVDAT 2 01-APR-03 1CEE 1 JRNL
REVDAT 1 30-JUN-99 1CEE 0
JRNL AUTH N.ABDUL-MANAN,B.AGHAZADEH,G.A.LIU,A.MAJUMDAR,O.OUERFELLI,
JRNL AUTH 2 K.A.SIMINOVITCH,M.K.ROSEN
JRNL TITL STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE-BINDING DOMAIN
JRNL TITL 2 OF THE 'WISKOTT-ALDRICH SYNDROME' PROTEIN.
JRNL REF NATURE V. 399 379 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10360578
JRNL DOI 10.1038/20726
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3, X-PLOR 3.1
REMARK 3 AUTHORS : A.BRUNGER, M.NILGES (CNS), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: X-PLOR 3.851 WAS USED IN COMBINATION
REMARK 3 WITH ARIA (REF. M. NILGES)
REMARK 4
REMARK 4 1CEE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000595.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY TOCSY 2D AND 3D THROUGH
REMARK 210 BOND TRANSFER EXPERIMENTS; 13C/
REMARK 210 15N PURGED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, ARIA, X-PLOR,
REMARK 210 CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING A COMBINATION OF TRIPLE
REMARK 210 - AND QUADRUPLE- RESONANCE NMR EXPERIMENTS ON 13C/ 15N AND
REMARK 210 PARTIALLY OR FULLY DEUTERATED SAMPLES WITH SELECTIVE METHYL
REMARK 210 LABELING AT VALINE,LUECINE AND ISOLEUCINES.
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 SER A 89 H VAL A 93 1.56
REMARK 500 O PRO A 69 H TYR A 72 1.58
REMARK 500 O SER B 5 H ASP B 8 1.58
REMARK 500 O LEU B 38 H PHE B 42 1.60
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 LYS A 5 70.46 -112.48
REMARK 500 1 PRO A 29 -167.75 -62.01
REMARK 500 1 SER A 30 -47.50 -146.04
REMARK 500 1 VAL A 33 60.70 170.22
REMARK 500 1 VAL A 36 -70.71 -159.82
REMARK 500 1 PHE A 37 125.49 -173.93
REMARK 500 1 PRO A 50 89.64 -69.40
REMARK 500 1 ASP A 76 -55.61 -121.47
REMARK 500 1 VAL A 85 34.49 -93.70
REMARK 500 1 LYS A 96 -51.06 169.99
REMARK 500 1 GLN A 116 50.66 79.27
REMARK 500 1 ASP A 122 77.31 -110.88
REMARK 500 1 LYS A 133 -29.02 170.11
REMARK 500 1 LYS A 135 143.40 -172.77
REMARK 500 1 ALA A 159 -49.21 -139.44
REMARK 500 1 LYS A 163 101.95 -56.52
REMARK 500 1 LEU A 165 -79.87 -54.74
REMARK 500 1 ILE B 9 96.81 -53.61
REMARK 500 1 PRO B 12 163.96 -49.42
REMARK 500 1 SER B 13 79.90 170.19
REMARK 500 1 HIS B 17 85.48 -67.28
REMARK 500 1 PHE B 29 126.69 60.60
REMARK 500 1 ASN B 33 34.47 -173.73
REMARK 500 1 ALA B 45 -99.04 -90.70
REMARK 500 1 ILE B 47 34.50 -98.52
REMARK 500 1 ALA B 50 137.71 172.18
REMARK 500 1 ASP B 54 99.02 -49.07
REMARK 500 1 ALA B 55 126.14 65.89
REMARK 500 2 ALA A 13 35.83 -177.67
REMARK 500 2 VAL A 36 -78.03 -50.16
REMARK 500 2 ALA A 59 -176.99 -67.83
REMARK 500 2 GLU A 62 -1.74 65.40
REMARK 500 2 THR A 75 132.59 -39.67
REMARK 500 2 LYS A 96 -59.36 178.64
REMARK 500 2 CYS A 105 83.44 -150.08
REMARK 500 2 GLN A 116 44.75 80.17
REMARK 500 2 ALA A 130 -29.37 -39.76
REMARK 500 2 LYS A 133 -25.09 165.94
REMARK 500 2 LYS A 135 144.18 -176.96
REMARK 500 2 LYS A 153 -163.34 177.44
REMARK 500 2 GLN A 162 30.96 73.98
REMARK 500 2 LEU A 165 -76.77 -47.34
REMARK 500 2 LEU A 177 -89.63 -53.36
REMARK 500 2 GLU A 178 159.23 101.59
REMARK 500 2 LYS B 2 28.41 -146.15
REMARK 500 2 ILE B 9 97.14 -48.14
REMARK 500 2 SER B 13 165.05 168.07
REMARK 500 2 HIS B 20 117.16 -163.52
REMARK 500 2 ASP B 30 53.58 -145.60
REMARK 500 2 ASN B 33 83.45 -154.30
REMARK 500
REMARK 500 THIS ENTRY HAS 505 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 180 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 THR A 35 OG1 104.1
REMARK 620 3 GCP A 181 O2B 82.8 137.8
REMARK 620 4 GCP A 181 O2G 158.3 68.2 90.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP A 181
DBREF 1CEE A 1 179 UNP P60953 CDC42_HUMAN 1 179
DBREF 1CEE B 1 59 UNP P42768 WASP_HUMAN 230 288
SEQRES 1 A 179 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 179 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 179 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 179 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 179 LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 179 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 179 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 179 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 179 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 179 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 179 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 179 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 179 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 179 ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO
SEQRES 1 B 59 LYS LYS LYS ILE SER LYS ALA ASP ILE GLY ALA PRO SER
SEQRES 2 B 59 GLY PHE LYS HIS VAL SER HIS VAL GLY TRP ASP PRO GLN
SEQRES 3 B 59 ASN GLY PHE ASP VAL ASN ASN LEU ASP PRO ASP LEU ARG
SEQRES 4 B 59 SER LEU PHE SER ARG ALA GLY ILE SER GLU ALA GLN LEU
SEQRES 5 B 59 THR ASP ALA GLU THR SER LYS
HET MG A 180 1
HET GCP A 181 46
HETNAM MG MAGNESIUM ION
HETNAM GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
FORMUL 3 MG MG 2+
FORMUL 4 GCP C11 H18 N5 O13 P3
HELIX 1 1 LYS A 16 THR A 25 1 10
HELIX 2 2 PRO A 69 SER A 71 5 3
HELIX 3 3 PRO A 87 LYS A 94 1 8
HELIX 4 4 PRO A 99 CYS A 105 1 7
HELIX 5 5 ILE A 117 ARG A 120 1 4
HELIX 6 6 PRO A 123 ALA A 130 1 8
HELIX 7 7 PRO A 139 ASP A 148 1 10
HELIX 8 8 LEU A 165 ALA A 176 1 12
HELIX 9 9 PRO B 36 PHE B 42 1 7
SHEET 1 A 4 VAL A 77 VAL A 80 0
SHEET 2 A 4 THR A 3 VAL A 9 1 N VAL A 7 O VAL A 77
SHEET 3 A 4 GLU A 49 ASP A 57 1 N THR A 52 O ILE A 4
SHEET 4 A 4 ASP A 38 ILE A 46 -1 N ILE A 46 O GLU A 49
SHEET 1 B 2 LEU A 111 GLY A 114 0
SHEET 2 B 2 LYS A 153 GLU A 156 1 N LYS A 153 O LEU A 112
LINK OG1 THR A 17 MG MG A 180 1555 1555 2.39
LINK OG1 THR A 35 MG MG A 180 1555 1555 2.38
LINK MG MG A 180 O2B GCP A 181 1555 1555 2.26
LINK MG MG A 180 O2G GCP A 181 1555 1555 2.20
SITE 1 AC1 3 THR A 17 THR A 35 GCP A 181
SITE 1 AC2 14 GLY A 12 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC2 14 LYS A 16 THR A 17 CYS A 18 PHE A 28
SITE 3 AC2 14 THR A 35 ASP A 118 SER A 158 ALA A 159
SITE 4 AC2 14 LEU A 160 MG A 180
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