HEADER CHAPERONE 23-MAR-16 2NCA
TITLE STRUCTURAL MODEL FOR THE N-TERMINAL DOMAIN OF HUMAN CDC37
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HSP90 CO-CHAPERONE CDC37;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 1-120;
COMPND 5 SYNONYM: HSP90 CHAPERONE PROTEIN KINASE-TARGETING SUBUNIT, P50CDC37,
COMPND 6 HSP90 CO-CHAPERONE CDC37, N-TERMINALLY PROCESSED;
COMPND 7 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: CDC37, CDC37A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PDBHIS.MBP
KEYWDS CHAPERONE, COCHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.ZHANG,D.KERAMISANOU,I.GELIS
REVDAT 2 14-JUN-23 2NCA 1 REMARK SEQADV
REVDAT 1 04-MAY-16 2NCA 0
JRNL AUTH D.KERAMISANOU,A.ABOALROUB,Z.ZHANG,W.LIU,D.MARSHALL,
JRNL AUTH 2 A.DIVINEY,R.W.LARSEN,R.LANDGRAF,I.GELIS
JRNL TITL MOLECULAR MECHANISM OF PROTEIN KINASE RECOGNITION AND
JRNL TITL 2 SORTING BY THE HSP90 KINOME-SPECIFIC COCHAPERONE CDC37.
JRNL REF MOL.CELL V. 62 260 2016
JRNL REFN ISSN 1097-2765
JRNL PMID 27105117
JRNL DOI 10.1016/J.MOLCEL.2016.04.005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CYANA
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3 (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000104687.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-100% 15N] N-CDC37, 90%
REMARK 210 H2O/10% D2O; 0.5 MM U-2H; VILMA
REMARK 210 METHYL 1H/13C N-CDC37, 100% D2O;
REMARK 210 0.5 MM [U-100% 13C; U-100% 15N]
REMARK 210 N-CDC37, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HMQC;
REMARK 210 3D HNCA; 3D HN(CO)CA; 3D HNCACB;
REMARK 210 3D CBCA(CO)NH; 3D HNCO; 3D HCACO;
REMARK 210 3D H(CCO)NH; 3D HCCH-TOCSY; 3D
REMARK 210 C(CO)NH; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 13C NOESY; HMQC-NOESY-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNIFORM NMR SYSTEM
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY, TALOS, CYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 HIS A 0
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 TYR A 4 52.53 -115.22
REMARK 500 1 SER A 5 93.88 -65.87
REMARK 500 1 VAL A 6 -32.51 -176.59
REMARK 500 1 ASP A 8 -34.70 -172.28
REMARK 500 1 GLU A 11 99.31 59.83
REMARK 500 1 ASP A 15 92.29 56.00
REMARK 500 1 GLU A 16 -174.54 56.78
REMARK 500 1 HIS A 20 68.41 -179.11
REMARK 500 1 ASN A 22 70.82 -154.24
REMARK 500 1 ASP A 24 -73.75 -155.18
REMARK 500 1 THR A 25 -73.64 -127.91
REMARK 500 1 ASP A 117 -170.94 63.29
REMARK 500 1 THR A 118 68.91 64.36
REMARK 500 1 LEU A 119 -179.64 -177.86
REMARK 500 2 GLU A 11 102.48 61.59
REMARK 500 2 ASP A 15 70.05 56.17
REMARK 500 2 GLU A 16 118.88 179.79
REMARK 500 2 THR A 19 40.21 -99.33
REMARK 500 2 ASP A 24 -64.68 -172.03
REMARK 500 2 THR A 25 -73.23 -147.50
REMARK 500 2 VAL A 116 -71.51 -127.99
REMARK 500 2 LYS A 121 82.60 63.22
REMARK 500 3 VAL A 2 88.67 51.69
REMARK 500 3 TYR A 4 175.15 57.99
REMARK 500 3 SER A 5 -71.19 -162.06
REMARK 500 3 GLU A 11 103.98 62.39
REMARK 500 3 ASP A 15 76.98 53.27
REMARK 500 3 GLU A 16 143.47 179.84
REMARK 500 3 PRO A 21 -171.71 -69.74
REMARK 500 3 ASP A 24 -71.91 -151.06
REMARK 500 3 THR A 25 -73.62 -130.21
REMARK 500 3 ASP A 117 72.29 62.92
REMARK 500 3 SER A 120 -176.70 -59.38
REMARK 500 3 LYS A 121 81.66 62.95
REMARK 500 4 SER A 5 88.99 -159.05
REMARK 500 4 GLU A 11 102.22 61.24
REMARK 500 4 GLU A 16 82.53 179.64
REMARK 500 4 PRO A 21 -171.80 -69.79
REMARK 500 4 ASP A 24 -63.47 -155.23
REMARK 500 4 THR A 25 -66.20 -145.84
REMARK 500 4 ALA A 74 -75.55 -77.71
REMARK 500 4 ASN A 115 -74.27 -84.80
REMARK 500 4 LYS A 121 -170.32 57.59
REMARK 500 5 ASP A 8 -168.32 -177.14
REMARK 500 5 HIS A 9 -51.29 76.72
REMARK 500 5 GLU A 11 105.63 63.32
REMARK 500 5 GLU A 16 106.34 -51.27
REMARK 500 5 THR A 19 -33.39 178.80
REMARK 500 5 HIS A 20 73.34 58.98
REMARK 500 5 ASP A 24 -72.18 -163.24
REMARK 500
REMARK 500 THIS ENTRY HAS 253 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2N5X RELATED DB: PDB
REMARK 900 C-TERMINAL DOMAIN OF CDC37
REMARK 900 RELATED ID: 1US7 RELATED DB: PDB
REMARK 900 TWO-DOMAIN FRAGMENT OF CDC37
REMARK 900 RELATED ID: 2K5B RELATED DB: PDB
REMARK 900 HUMAN CDC37-HSP90 DOCKING MODEL
REMARK 900 RELATED ID: 26012 RELATED DB: BMRB
DBREF 2NCA A 1 126 UNP Q16543 CDC37_HUMAN 1 126
SEQADV 2NCA GLY A -1 UNP Q16543 EXPRESSION TAG
SEQADV 2NCA HIS A 0 UNP Q16543 EXPRESSION TAG
SEQRES 1 A 128 GLY HIS MET VAL ASP TYR SER VAL TRP ASP HIS ILE GLU
SEQRES 2 A 128 VAL SER ASP ASP GLU ASP GLU THR HIS PRO ASN ILE ASP
SEQRES 3 A 128 THR ALA SER LEU PHE ARG TRP ARG HIS GLN ALA ARG VAL
SEQRES 4 A 128 GLU ARG MET GLU GLN PHE GLN LYS GLU LYS GLU GLU LEU
SEQRES 5 A 128 ASP ARG GLY CYS ARG GLU CYS LYS ARG LYS VAL ALA GLU
SEQRES 6 A 128 CYS GLN ARG LYS LEU LYS GLU LEU GLU VAL ALA GLU GLY
SEQRES 7 A 128 GLY LYS ALA GLU LEU GLU ARG LEU GLN ALA GLU ALA GLN
SEQRES 8 A 128 GLN LEU ARG LYS GLU GLU ARG SER TRP GLU GLN LYS LEU
SEQRES 9 A 128 GLU GLU MET ARG LYS LYS GLU LYS SER MET PRO TRP ASN
SEQRES 10 A 128 VAL ASP THR LEU SER LYS ASP GLY PHE SER LYS
HELIX 1 1 ALA A 26 VAL A 73 1 48
HELIX 2 2 LYS A 78 LYS A 110 1 33
HELIX 3 3 MET A 112 ASP A 117 1 6
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
(ATOM LINES ARE NOT SHOWN.)
END
