Header list of 2dk9.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 07-APR-06 2DK9
TITLE SOLUTION STRUCTURE OF CALPONIN HOMOLOGY DOMAIN OF HUMAN MICAL-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEDD9-INTERACTING PROTEIN WITH CALPONIN HOMOLOGY AND LIM
COMPND 3 DOMAINS;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CALPONIN HOMOLOGY DOMAIN;
COMPND 6 SYNONYM: MOLECULE INTERACTING WITH CASL PROTEIN 1, MICAL-1;
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: MICAL1, MICAL, NICAL;
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: P28
KEYWDS HELIX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.SUN,H.DAI,J.ZHANG,S.XIONG,J.WU,Y.SHI
REVDAT 4 09-MAR-22 2DK9 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2DK9 1 VERSN
REVDAT 2 05-DEC-06 2DK9 1 JRNL
REVDAT 1 19-SEP-06 2DK9 0
JRNL AUTH H.SUN,H.DAI,J.ZHANG,X.JIN,S.XIONG,J.XU,J.WU,Y.SHI
JRNL TITL SOLUTION STRUCTURE OF CALPONIN HOMOLOGY DOMAIN OF HUMAN
JRNL TITL 2 MICAL-1
JRNL REF J.BIOMOL.NMR V. 36 295 2006
JRNL REFN ISSN 0925-2738
JRNL PMID 17043746
JRNL DOI 10.1007/S10858-006-9062-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2042 RESTRAINTS, 1746 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 140
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,82 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS,74 RESIDUAL DIPOLAR COUPLINGS RESTRAINTS.
REMARK 4
REMARK 4 2DK9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025514.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER, 50MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM MICAL_1 CH U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM NACL; 90%
REMARK 210 H2O, 10% D2O; 1.5MM MICAL_1 CH U-
REMARK 210 15N; 50MM PHOSPHATE BUFFER, 50MM
REMARK 210 NACL; 90% H2O, 10% D2O; 1.5MM
REMARK 210 MICAL_1 CH U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM NACL; 100%
REMARK 210 D2O; 1.5MM MICAL_1 CH U-15N;
REMARK 210 50MM PHOSPHATE BUFFER, 50MM NACL;
REMARK 210 17 MG/ML PF1 FILAMENTOUS PHAGE;
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO,
REMARK 210 HN(CA)CO, CBCA(CO)NH, CBCANH,
REMARK 210 C(CO)NH-TOCSY, H(CCO)NH-TOCSY,
REMARK 210 HBHA(CBCACO)NH,3D 15N-SEPARTED
REMARK 210 NOESY; 3D HCCH-TOCSY, HCCH-COSY,
REMARK 210 13C-SEPARTED NOESY; 1H-COUPLED
REMARK 210 IPAP {15N, 1H}-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, CNS 1.1, MOLMOL
REMARK 210 2K.2
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HOMONUCLEAR TECHNIQUES AND RESIDUAL DIPOLAR COUPLINGS DATA
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 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
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 HIS A -5 -55.50 -154.50
REMARK 500 1 HIS A -4 -62.70 -171.61
REMARK 500 1 HIS A -2 -47.46 -148.57
REMARK 500 1 HIS A -1 -59.88 -132.09
REMARK 500 1 SER A 26 21.40 -148.62
REMARK 500 1 LEU A 28 37.81 -96.36
REMARK 500 1 SER A 29 -74.60 -164.49
REMARK 500 1 ASP A 91 70.42 -157.67
REMARK 500 1 SER A 108 -60.82 -109.45
REMARK 500 2 HIS A -4 -48.50 -176.19
REMARK 500 2 HIS A -3 -45.16 -160.21
REMARK 500 2 PRO A 21 62.76 -69.21
REMARK 500 2 HIS A 24 38.61 -144.08
REMARK 500 2 VAL A 25 97.57 -66.24
REMARK 500 2 SER A 26 20.84 -146.16
REMARK 500 2 LEU A 28 39.38 -99.66
REMARK 500 2 SER A 29 -80.35 -169.58
REMARK 500 2 ASP A 91 70.76 -159.83
REMARK 500 3 HIS A -3 69.98 -104.39
REMARK 500 3 HIS A -1 95.74 63.22
REMARK 500 3 SER A 26 21.03 -151.73
REMARK 500 3 LEU A 28 35.95 -94.35
REMARK 500 3 SER A 29 -69.32 -163.78
REMARK 500 3 GLU A 51 46.75 -148.21
REMARK 500 4 PRO A 21 68.38 -65.81
REMARK 500 4 SER A 26 18.96 -146.15
REMARK 500 4 LEU A 28 37.23 -95.98
REMARK 500 4 SER A 29 -78.94 -159.66
REMARK 500 4 GLU A 51 63.06 -163.48
REMARK 500 4 SER A 90 42.87 -107.54
REMARK 500 4 ASP A 91 70.24 -158.20
REMARK 500 5 PRO A 21 63.15 -66.22
REMARK 500 5 SER A 26 22.37 -150.21
REMARK 500 5 LEU A 28 38.51 -98.52
REMARK 500 5 SER A 29 -80.81 -173.90
REMARK 500 5 GLU A 51 49.40 -156.99
REMARK 500 5 SER A 90 31.10 -98.54
REMARK 500 5 ASP A 91 71.35 -161.55
REMARK 500 6 HIS A -5 97.21 57.78
REMARK 500 6 HIS A -1 85.59 -155.89
REMARK 500 6 MET A 0 106.05 59.87
REMARK 500 6 SER A 26 19.97 -152.66
REMARK 500 6 LEU A 28 36.74 -94.27
REMARK 500 6 SER A 29 -70.01 -163.50
REMARK 500 6 GLU A 51 61.21 -154.06
REMARK 500 6 ASP A 91 63.54 -159.39
REMARK 500 7 HIS A -5 -80.42 62.47
REMARK 500 7 HIS A -4 -170.52 58.27
REMARK 500 7 HIS A -3 165.57 60.02
REMARK 500 7 MET A 0 92.53 -176.02
REMARK 500
REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2DK9 A 1 109 UNP Q8TDZ2 MICA1_HUMAN 506 614
SEQADV 2DK9 MET A -8 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 GLY A -7 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -6 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -5 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -4 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -3 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -2 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 HIS A -1 UNP Q8TDZ2 EXPRESSION TAG
SEQADV 2DK9 MET A 0 UNP Q8TDZ2 EXPRESSION TAG
SEQRES 1 A 118 MET GLY HIS HIS HIS HIS HIS HIS MET GLY SER ALA GLY
SEQRES 2 A 118 THR GLN GLU GLU LEU LEU ARG TRP CYS GLN GLU GLN THR
SEQRES 3 A 118 ALA GLY TYR PRO GLY VAL HIS VAL SER ASP LEU SER SER
SEQRES 4 A 118 SER TRP ALA ASP GLY LEU ALA LEU CYS ALA LEU VAL TYR
SEQRES 5 A 118 ARG LEU GLN PRO GLY LEU LEU GLU PRO SER GLU LEU GLN
SEQRES 6 A 118 GLY LEU GLY ALA LEU GLU ALA THR ALA TRP ALA LEU LYS
SEQRES 7 A 118 VAL ALA GLU ASN GLU LEU GLY ILE THR PRO VAL VAL SER
SEQRES 8 A 118 ALA GLN ALA VAL VAL ALA GLY SER ASP PRO LEU GLY LEU
SEQRES 9 A 118 ILE ALA TYR LEU SER HIS PHE HIS SER ALA PHE LYS SER
SEQRES 10 A 118 MET
HELIX 1 1 GLY A 1 THR A 17 1 17
HELIX 2 2 SER A 29 ALA A 33 5 5
HELIX 3 3 GLY A 35 GLN A 46 1 12
HELIX 4 4 PRO A 47 LEU A 50 5 4
HELIX 5 5 GLU A 51 GLY A 59 1 9
HELIX 6 6 GLY A 59 LEU A 75 1 17
HELIX 7 7 SER A 82 GLY A 89 1 8
HELIX 8 8 ASP A 91 MET A 109 1 19
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 - r 9 2 Bytes