HEADER BLOOD CLOTTING 25-NOV-99 1DGU
TITLE HOMOLOGY-BASED MODEL OF CALCIUM-SATURATED CIB (CALCIUM-AND INTEGRIN-
TITLE 2 BINDING PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-SATURATED CIB;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HELICAL, EF-HANDS, BLOOD CLOTTING
EXPDTA SOLUTION NMR
AUTHOR P.M.HWANG,H.J.VOGEL
REVDAT 5 16-FEB-22 1DGU 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1DGU 1 VERSN
REVDAT 3 01-APR-03 1DGU 1 JRNL
REVDAT 2 30-AUG-00 1DGU 1 JRNL
REVDAT 1 08-DEC-99 1DGU 0
JRNL AUTH P.M.HWANG,H.J.VOGEL
JRNL TITL STRUCTURES OF THE PLATELET CALCIUM- AND INTEGRIN-BINDING
JRNL TITL 2 PROTEIN AND THE ALPHAIIB-INTEGRIN CYTOPLASMIC DOMAIN SUGGEST
JRNL TITL 3 A MECHANISM FOR CALCIUM-REGULATED RECOGNITION; HOMOLOGY
JRNL TITL 4 MODELLING AND NMR STUDIES.
JRNL REF J.MOL.RECOG. V. 13 83 2000
JRNL REFN ISSN 0952-3499
JRNL PMID 10822252
JRNL DOI 10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.3.CO
JRNL DOI 2 ;2-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DGU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010077.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 GLU A 7 CD GLU A 7 OE2 0.108
REMARK 500 GLU A 18 CD GLU A 18 OE2 0.108
REMARK 500 HIS A 23 CG HIS A 23 CD2 0.056
REMARK 500 GLU A 28 CD GLU A 28 OE2 0.108
REMARK 500 GLU A 33 CD GLU A 33 OE2 0.105
REMARK 500 GLU A 38 CD GLU A 38 OE2 0.110
REMARK 500 GLU A 48 CD GLU A 48 OE2 0.108
REMARK 500 GLU A 55 CD GLU A 55 OE2 0.108
REMARK 500 GLU A 63 CD GLU A 63 OE2 0.110
REMARK 500 GLU A 81 CD GLU A 81 OE2 0.108
REMARK 500 HIS A 101 CG HIS A 101 CD2 0.054
REMARK 500 GLU A 118 CD GLU A 118 OE2 0.109
REMARK 500 GLU A 130 CD GLU A 130 OE2 0.107
REMARK 500 GLU A 132 CD GLU A 132 OE2 0.108
REMARK 500 GLU A 140 CD GLU A 140 OE2 0.107
REMARK 500 GLU A 150 CD GLU A 150 OE2 0.111
REMARK 500 GLU A 151 CD GLU A 151 OE2 0.107
REMARK 500 GLU A 164 CD GLU A 164 OE2 0.097
REMARK 500 HIS A 167 CG HIS A 167 CD2 0.055
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 10 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 10 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 HIS A 23 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 SER A 70 O - C - N ANGL. DEV. = -12.9 DEGREES
REMARK 500 SER A 72 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP A 76 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 82 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 85 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 92 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 92 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 97 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 97 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 HIS A 101 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 108 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 108 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 110 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 110 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 111 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 111 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 112 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 112 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASP A 146 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 146 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 153 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 153 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASP A 157 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 157 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 HIS A 167 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 174 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 174 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
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 LEU A 4 71.75 -105.47
REMARK 500 LEU A 5 -59.40 -146.92
REMARK 500 GLN A 32 -58.63 -133.74
REMARK 500 ALA A 43 -59.90 -169.40
REMARK 500 PRO A 54 -70.40 -26.57
REMARK 500 LEU A 56 54.04 -111.85
REMARK 500 LYS A 57 -74.71 -130.17
REMARK 500 SER A 70 -69.06 -124.35
REMARK 500 SER A 72 -101.94 75.86
REMARK 500 LYS A 75 -39.35 77.81
REMARK 500 SER A 77 -120.86 -128.39
REMARK 500 THR A 93 -32.47 94.07
REMARK 500 GLU A 130 -68.99 -127.75
REMARK 500 GLU A 132 67.10 63.36
REMARK 500 ASP A 153 38.79 -70.95
REMARK 500 ARG A 156 -27.67 105.17
REMARK 500 ASP A 157 2.37 -63.30
REMARK 500 SER A 170 60.61 -150.03
REMARK 500 PHE A 179 56.21 -140.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 44 VAL A 45 47.49
REMARK 500 SER A 70 THR A 71 -79.29
REMARK 500 ARG A 171 SER A 172 140.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 69 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 70 -11.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DGV RELATED DB: PDB
DBREF 1DGU A 1 183 UNP Q99828 KIP1_HUMAN 9 191
SEQADV 1DGU SER A 36 UNP Q99828 THR 44 CONFLICT
SEQRES 1 A 183 SER LYS GLU LEU LEU ALA GLU TYR GLN ASP LEU THR PHE
SEQRES 2 A 183 LEU THR LYS GLN GLU ILE LEU LEU ALA HIS ARG ARG PHE
SEQRES 3 A 183 CYS GLU LEU LEU PRO GLN GLU GLN ARG SER VAL GLU SER
SEQRES 4 A 183 SER LEU ARG ALA GLN VAL PRO PHE GLU GLN ILE LEU SER
SEQRES 5 A 183 LEU PRO GLU LEU LYS ALA ASN PRO PHE LYS GLU ARG ILE
SEQRES 6 A 183 CYS ARG VAL PHE SER THR SER PRO ALA LYS ASP SER LEU
SEQRES 7 A 183 SER PHE GLU ASP PHE LEU ASP LEU LEU SER VAL PHE SER
SEQRES 8 A 183 ASP THR ALA THR PRO ASP ILE LYS SER HIS TYR ALA PHE
SEQRES 9 A 183 ARG ILE PHE ASP PHE ASP ASP ASP GLY THR LEU ASN ARG
SEQRES 10 A 183 GLU ASP LEU SER ARG LEU VAL ASN CYS LEU THR GLY GLU
SEQRES 11 A 183 GLY GLU ASP THR ARG LEU SER ALA SER GLU MET LYS GLN
SEQRES 12 A 183 LEU ILE ASP ASN ILE LEU GLU GLU SER ASP ILE ASP ARG
SEQRES 13 A 183 ASP GLY THR ILE ASN LEU SER GLU PHE GLN HIS VAL ILE
SEQRES 14 A 183 SER ARG SER PRO ASP PHE ALA SER SER PHE LYS ILE VAL
SEQRES 15 A 183 LEU
HELIX 1 1 THR A 15 LEU A 30 1 16
HELIX 2 2 PRO A 46 SER A 52 1 7
HELIX 3 3 PHE A 61 SER A 70 1 10
HELIX 4 4 SER A 79 SER A 91 1 13
HELIX 5 5 THR A 95 ASP A 108 1 14
HELIX 6 6 ARG A 117 GLY A 129 1 13
HELIX 7 7 THR A 134 ASP A 153 1 20
HELIX 8 8 LEU A 162 SER A 170 1 9
HELIX 9 9 PRO A 173 SER A 178 1 6
SHEET 1 A 2 THR A 114 ASN A 116 0
SHEET 2 A 2 THR A 159 ASN A 161 -1 O ILE A 160 N LEU A 115
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
(ATOM LINES ARE NOT SHOWN.)
END