HEADER HYDROLASE 30-APR-98 1BCI
TITLE C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOSOLIC PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN;
COMPND 5 SYNONYM: CALB DOMAIN;
COMPND 6 EC: 3.1.1.4;
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 CELL_LINE: PROPRIETARY STRAIN/GI400;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: PROPRIETARY STRAIN/GI400;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHISB(INVITROGEN)
KEYWDS HYDROLASE, LIPID DEGRADATION, CYTOSOLIC PHOSPHOLIPASE A2, CALCIUM-
KEYWDS 2 DEPENDENT LIPID BINDING, C2 DOMAIN, PHOSPHOCHOLINE
EXPDTA SOLUTION NMR
AUTHOR G.Y.XU,T.MCDONAGH,H.A.YU,E.A.NALEFSKI,J.D.CLARK,D.A.CUMMING
REVDAT 5 16-FEB-22 1BCI 1 REMARK LINK
REVDAT 4 24-FEB-09 1BCI 1 VERSN
REVDAT 3 01-APR-03 1BCI 1 JRNL
REVDAT 2 13-JAN-99 1BCI 3 ATOM SOURCE COMPND REMARK
REVDAT 2 2 3 TITLE HETATM JRNL EXPDTA
REVDAT 2 3 3 KEYWDS HEADER
REVDAT 1 25-NOV-98 1BCI 0
JRNL AUTH G.Y.XU,T.MCDONAGH,H.A.YU,E.A.NALEFSKI,J.D.CLARK,D.A.CUMMING
JRNL TITL SOLUTION STRUCTURE AND MEMBRANE INTERACTIONS OF THE C2
JRNL TITL 2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2.
JRNL REF J.MOL.BIOL. V. 280 485 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9665851
JRNL DOI 10.1006/JMBI.1998.1874
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS AVERAGE-MINIMIZED STRUCTURE IS
REMARK 3 FROM 34 ENSEMBLE STRUCTURES, WHICH ARE BASED ON 2215 INTERPROTON
REMARK 3 DISTANCE RESTRAINTS DERIVED FROM NMR MEASUREMENTS INCLUDING 106
REMARK 3 HYDROGEN BOND RESTRAINTS AND 155 TORSION ANGLE RESTRAINTS. THE
REMARK 3 DETAILED ENERGETIC STATISTICS AND ATOMIC RMSD'S CAN BE FOUND IN
REMARK 3 THE J.MOL.BIOL CITATION.
REMARK 4
REMARK 4 1BCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171590.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 0.0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20 MM TRIS, 0.5MM CACL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNIT+
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, RESTRAINED MOLECULAR
REMARK 210 DYNAMICS, ETC.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : VIOLATION: NOES<0.3 A, DIHEDRAL
REMARK 210 ANGLES<3 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: N15-NOESY, HNHA-J, HNHB, CBCACONNH, HNCACB, HBHACONNH,
REMARK 210 HNHAHB, HCCH-TOCSY, LONG-RANGE-CCJ, CN-NOESY, ETC.
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 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PHE A 3
REMARK 465 ILE A 4
REMARK 465 ASP A 5
REMARK 465 PRO A 6
REMARK 465 TYR A 7
REMARK 465 GLN A 8
REMARK 465 HIS A 9
REMARK 465 ILE A 10
REMARK 465 ILE A 11
REMARK 465 VAL A 12
REMARK 465 GLU A 13
REMARK 465 HIS A 14
REMARK 465 GLN A 15
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 25 -74.81 -80.05
REMARK 500 ALA A 27 70.50 -163.89
REMARK 500 LYS A 32 -77.00 -160.43
REMARK 500 ASP A 40 176.06 175.66
REMARK 500 THR A 41 147.70 -36.05
REMARK 500 PRO A 42 154.74 -34.00
REMARK 500 TYR A 45 125.13 -175.14
REMARK 500 THR A 52 -31.44 167.80
REMARK 500 ASP A 55 73.22 -159.37
REMARK 500 HIS A 62 -109.79 -83.40
REMARK 500 ASN A 65 86.04 45.09
REMARK 500 ASP A 66 115.96 179.45
REMARK 500 ASN A 68 49.67 -143.94
REMARK 500 PHE A 77 89.44 -150.85
REMARK 500 GLN A 83 -159.03 -81.69
REMARK 500 GLU A 84 68.30 -100.33
REMARK 500 ASN A 85 90.90 -49.44
REMARK 500 LEU A 87 92.60 -59.25
REMARK 500 THR A 90 108.55 -161.27
REMARK 500 ASN A 95 -165.57 -100.71
REMARK 500 VAL A 97 -50.52 -131.86
REMARK 500 LYS A 113 58.10 -96.57
REMARK 500 ASN A 125 -87.77 62.63
REMARK 500 GLN A 126 -38.80 -161.14
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 ARG A 26 0.13 SIDE CHAIN
REMARK 500 ARG A 57 0.28 SIDE CHAIN
REMARK 500 ARG A 59 0.29 SIDE CHAIN
REMARK 500 ARG A 61 0.30 SIDE CHAIN
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 CA A 139 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 40 O
REMARK 620 2 THR A 41 O 57.2
REMARK 620 3 ASP A 43 OD1 99.4 65.7
REMARK 620 4 ASN A 65 N 113.3 57.5 64.6
REMARK 620 5 ASN A 65 OD1 128.9 99.4 111.2 53.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 140 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 43 OD2
REMARK 620 2 ASP A 93 OD2 113.6
REMARK 620 3 ALA A 94 O 70.3 98.7
REMARK 620 4 ASN A 95 OD1 149.0 75.8 79.2
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 CA A 139
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 140
DBREF 1BCI A 1 138 UNP P47712 PA24A_HUMAN 1 138
SEQRES 1 A 138 MET SER PHE ILE ASP PRO TYR GLN HIS ILE ILE VAL GLU
SEQRES 2 A 138 HIS GLN TYR SER HIS LYS PHE THR VAL VAL VAL LEU ARG
SEQRES 3 A 138 ALA THR LYS VAL THR LYS GLY ALA PHE GLY ASP MET LEU
SEQRES 4 A 138 ASP THR PRO ASP PRO TYR VAL GLU LEU PHE ILE SER THR
SEQRES 5 A 138 THR PRO ASP SER ARG LYS ARG THR ARG HIS PHE ASN ASN
SEQRES 6 A 138 ASP ILE ASN PRO VAL TRP ASN GLU THR PHE GLU PHE ILE
SEQRES 7 A 138 LEU ASP PRO ASN GLN GLU ASN VAL LEU GLU ILE THR LEU
SEQRES 8 A 138 MET ASP ALA ASN TYR VAL MET ASP GLU THR LEU GLY THR
SEQRES 9 A 138 ALA THR PHE THR VAL SER SER MET LYS VAL GLY GLU LYS
SEQRES 10 A 138 LYS GLU VAL PRO PHE ILE PHE ASN GLN VAL THR GLU MET
SEQRES 11 A 138 VAL LEU GLU MET SER LEU GLU VAL
HET CA A 139 1
HET CA A 140 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 PHE A 35 LEU A 39 5 5
SHEET 1 A 4 PRO A 69 LEU A 79 0
SHEET 2 A 4 HIS A 18 THR A 28 -1 O HIS A 18 O LEU A 79
SHEET 3 A 4 THR A 128 GLU A 137 -1 N GLU A 129 O THR A 28
SHEET 4 A 4 GLY A 115 PHE A 124 -1 O GLU A 116 N LEU A 136
SHEET 1 B 4 SER A 56 PHE A 63 0
SHEET 2 B 4 PRO A 44 PHE A 49 -1 O PRO A 44 O PHE A 63
SHEET 3 B 4 VAL A 86 ALA A 94 -1 N GLU A 88 O PHE A 49
SHEET 4 B 4 ASP A 99 VAL A 109 -1 N GLU A 100 O ASP A 93
LINK O ASP A 40 CA CA A 139 1555 1555 2.73
LINK O THR A 41 CA CA A 139 1555 1555 2.57
LINK OD1 ASP A 43 CA CA A 139 1555 1555 2.56
LINK OD2 ASP A 43 CA CA A 140 1555 1555 2.71
LINK N ASN A 65 CA CA A 139 1555 1555 3.22
LINK OD1 ASN A 65 CA CA A 139 1555 1555 2.81
LINK OD2 ASP A 93 CA CA A 140 1555 1555 2.66
LINK O ALA A 94 CA CA A 140 1555 1555 2.83
LINK OD1 ASN A 95 CA CA A 140 1555 1555 2.59
SITE 1 AC1 5 ASP A 40 THR A 41 ASP A 43 ASN A 64
SITE 2 AC1 5 ASN A 65
SITE 1 AC2 4 ASP A 43 ASP A 93 ALA A 94 ASN A 95
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