Header list of 1cf4.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 23-MAR-99 1CF4
TITLE CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CDC42 HOMOLOG);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN (ACTIVATED P21CDC42HS KINASE);
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: GTPASE-BINDING DOMAIN;
COMPND 10 OTHER_DETAILS: COMPLEXED WITH 5'-GUANOSYL-IMIDO-TRIPHOSPHATE
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 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606
KEYWDS CDC42-ACK GTPASE COMPLEX, G PROTEIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.R.MOTT,D.OWEN,D.NIETLISPACH,P.N.LOWE,L.LIM,E.D.LAUE
REVDAT 4 16-FEB-22 1CF4 1 REMARK SEQADV SHEET LINK
REVDAT 3 24-FEB-09 1CF4 1 VERSN
REVDAT 2 27-JUN-01 1CF4 1 COMPND SOURCE DBREF SEQADV
REVDAT 2 2 1 REMARK HETATM
REVDAT 1 18-JUN-99 1CF4 0
JRNL AUTH H.R.MOTT,D.OWEN,D.NIETLISPACH,P.N.LOWE,E.MANSER,L.LIM,
JRNL AUTH 2 E.D.LAUE
JRNL TITL STRUCTURE OF THE SMALL G PROTEIN CDC42 BOUND TO THE
JRNL TITL 2 GTPASE-BINDING DOMAIN OF ACK.
JRNL REF NATURE V. 399 384 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10360579
JRNL DOI 10.1038/20732
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CF4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000710.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : [50%2H; 100%15N,13C]-LABELLED
REMARK 210 CDC42, UNLABELLED F-ACK, 90% H2O/
REMARK 210 10%; [U-15N] F-ACK, CDC42, 90%
REMARK 210 H2O/10%; [U-13C; U-15N] F-ACK,
REMARK 210 CDC42, 90% H2O/10% D2O; [U-13C;
REMARK 210 U-15N] CDC42, 90% H2O/10% D2O;
REMARK 210 [U-100% 15N] CDC42, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCA; 3D HNCO; 3D HCCH-TOCSY;
REMARK 210 15N-EDITED NOESY; 15N-EDITED
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG, XPLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
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: 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 ILE A 21 H THR A 25 1.49
REMARK 500 O LEU A 129 H LYS A 133 1.55
REMARK 500 O VAL A 42 HG1 THR A 52 1.56
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 GLN A 2 134.04 62.25
REMARK 500 1 THR A 3 -166.50 -107.39
REMARK 500 1 VAL A 14 -87.41 44.62
REMARK 500 1 LEU A 19 -71.05 -62.83
REMARK 500 1 ILE A 21 -71.20 -58.31
REMARK 500 1 THR A 25 -162.84 -177.83
REMARK 500 1 ASN A 26 -20.87 97.60
REMARK 500 1 LYS A 27 146.67 60.06
REMARK 500 1 SER A 30 -85.53 -133.85
REMARK 500 1 VAL A 33 -61.35 -165.31
REMARK 500 1 PHE A 37 46.90 -83.02
REMARK 500 1 ASP A 38 -158.29 -63.66
REMARK 500 1 PRO A 50 105.55 -43.28
REMARK 500 1 TYR A 64 93.34 -166.80
REMARK 500 1 ARG A 68 62.82 -178.18
REMARK 500 1 SER A 71 -71.25 -48.36
REMARK 500 1 THR A 75 174.60 -50.82
REMARK 500 1 PHE A 82 -174.30 -179.63
REMARK 500 1 PRO A 87 53.28 -94.01
REMARK 500 1 SER A 88 30.07 81.12
REMARK 500 1 PRO A 106 89.25 -50.98
REMARK 500 1 LYS A 107 94.54 63.29
REMARK 500 1 THR A 115 -61.53 -153.83
REMARK 500 1 LYS A 133 -95.05 -146.20
REMARK 500 1 GLN A 134 -21.17 128.94
REMARK 500 1 ILE A 137 96.78 -62.47
REMARK 500 1 ALA A 151 -81.02 -62.26
REMARK 500 1 VAL A 152 -75.03 -159.59
REMARK 500 1 LYS A 153 146.06 170.13
REMARK 500 1 LEU A 160 -44.06 -131.57
REMARK 500 1 GLN A 162 77.78 78.05
REMARK 500 1 LYS A 163 30.23 -96.17
REMARK 500 1 LEU A 165 -73.58 66.74
REMARK 500 1 ASN A 167 -71.71 -52.31
REMARK 500 1 GLU A 178 149.30 171.24
REMARK 500 1 PRO A 179 107.71 -57.48
REMARK 500 1 PRO A 182 -165.28 -76.46
REMARK 500 1 SER B 503 -78.77 -64.14
REMARK 500 1 LEU B 505 55.12 -167.17
REMARK 500 1 ALA B 507 53.42 -175.50
REMARK 500 1 GLN B 512 179.58 -50.60
REMARK 500 1 PRO B 513 92.60 -46.12
REMARK 500 1 LEU B 514 -168.33 -62.84
REMARK 500 1 SER B 517 65.48 -100.90
REMARK 500 1 HIS B 520 103.12 72.91
REMARK 500 1 THR B 521 57.60 -143.86
REMARK 500 1 HIS B 523 -91.26 -98.68
REMARK 500 1 ASP B 525 79.22 82.07
REMARK 500 1 ASP B 527 163.61 -40.15
REMARK 500 1 CYS B 531 -160.96 44.99
REMARK 500
REMARK 500 THIS ENTRY HAS 976 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 186 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 THR A 35 OG1 81.1
REMARK 620 3 GNP A 185 O2G 168.0 88.2
REMARK 620 4 GNP A 185 N3B 132.2 131.4 53.2
REMARK 620 5 GNP A 185 O1B 134.0 136.7 58.1 49.4
REMARK 620 6 GNP A 185 O2B 88.5 167.8 101.4 53.4 55.5
REMARK 620 7 HOH A 187 O 91.4 93.6 94.7 115.3 66.0 93.0
REMARK 620 8 HOH A 188 O 78.9 94.0 96.6 66.7 114.5 77.6 166.6
REMARK 620 N 1 2 3 4 5 6 7
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 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 185
DBREF 1CF4 A 1 184 UNP P60953 CDC42_HUMAN 1 191
DBREF 1CF4 B 502 545 UNP Q07912 ACK1_HUMAN 446 489
SEQADV 1CF4 LEU A 61 UNP P60953 GLN 61 CONFLICT
SEQADV 1CF4 A UNP P60953 LYS 183 DELETION
SEQADV 1CF4 A UNP P60953 LYS 184 DELETION
SEQADV 1CF4 A UNP P60953 SER 185 DELETION
SEQADV 1CF4 A UNP P60953 ARG 186 DELETION
SEQADV 1CF4 A UNP P60953 ARG 187 DELETION
SEQADV 1CF4 A UNP P60953 CYS 188 DELETION
SEQADV 1CF4 A UNP P60953 VAL 189 DELETION
SEQADV 1CF4 GLY B 502 UNP Q07912 VAL 502 CONFLICT
SEQADV 1CF4 SER B 503 UNP Q07912 ALA 503 CONFLICT
SEQRES 1 A 184 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 184 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 184 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 184 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 184 LEU GLY LEU PHE ASP THR ALA GLY LEU GLU ASP TYR ASP
SEQRES 6 A 184 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 184 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 184 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 184 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 184 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 184 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 184 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 184 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 184 ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO PRO GLU PRO
SEQRES 15 A 184 LYS LYS
SEQRES 1 B 44 GLY SER GLY LEU SER ALA GLN ASP ILE SER GLN PRO LEU
SEQRES 2 B 44 GLN ASN SER PHE ILE HIS THR GLY HIS GLY ASP SER ASP
SEQRES 3 B 44 PRO ARG HIS CYS TRP GLY PHE PRO ASP ARG ILE ASP GLU
SEQRES 4 B 44 LEU TYR LEU GLY ASN
HET MG A 186 1
HET GNP A 185 45
HETNAM MG MAGNESIUM ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL 3 MG MG 2+
FORMUL 4 GNP C10 H17 N6 O13 P3
FORMUL 5 HOH *2(H2 O)
HELIX 1 1 LYS A 16 THR A 24 1 9
HELIX 2 2 TYR A 64 ARG A 66 1 3
HELIX 3 3 PRO A 69 TYR A 72 1 4
HELIX 4 4 SER A 89 HIS A 104 1 16
HELIX 5 5 ILE A 117 LEU A 119 1 3
HELIX 6 6 PRO A 123 ALA A 130 1 8
HELIX 7 7 PRO A 139 LEU A 149 1 11
HELIX 8 8 LEU A 165 LEU A 177 1 13
SHEET 1 A 6 THR A 3 VAL A 9 0
SHEET 2 A 6 ALA A 41 ILE A 46 0
SHEET 3 A 6 TYR A 51 LEU A 53 0
SHEET 4 A 6 PHE A 78 CYS A 81 1 N LEU A 79 O VAL A 9
SHEET 5 A 6 PHE A 110 GLY A 114 1 N LEU A 111 O PHE A 78
SHEET 6 A 6 TYR A 154 SER A 158 1 N VAL A 155 O LEU A 112
SHEET 1 B 1 SER B 517 HIS B 520 0
LINK OG1 THR A 17 MG MG A 186 1555 1555 2.33
LINK OG1 THR A 35 MG MG A 186 1555 1555 2.33
LINK O2G GNP A 185 MG MG A 186 1555 1555 2.29
LINK N3B GNP A 185 MG MG A 186 1555 1555 3.11
LINK O1B GNP A 185 MG MG A 186 1555 1555 2.97
LINK O2B GNP A 185 MG MG A 186 1555 1555 2.31
LINK MG MG A 186 O HOH A 187 1555 1555 2.45
LINK MG MG A 186 O HOH A 188 1555 1555 2.45
SITE 1 AC1 5 THR A 17 THR A 35 GNP A 185 HOH A 187
SITE 2 AC1 5 HOH A 188
SITE 1 AC2 20 GLY A 12 ALA A 13 VAL A 14 THR A 17
SITE 2 AC2 20 CYS A 18 ASN A 26 PHE A 28 GLU A 31
SITE 3 AC2 20 TYR A 32 THR A 35 CYS A 81 PHE A 82
SITE 4 AC2 20 SER A 83 VAL A 113 THR A 115 GLN A 116
SITE 5 AC2 20 MG A 186 HOH A 187 HOH A 188 ARG B 537
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