Header list of 1bvm.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 14-SEP-98 1BVM
TITLE SOLUTION NMR STRUCTURE OF BOVINE PANCREATIC PHOSPHOLIPASE A2, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PHOSPHOLIPASE A2);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)[PLYSS];
SOURCE 8 OTHER_DETAILS: BOVINE PANCREAS
KEYWDS PHOSPHOLIPASE A2, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.-H.YUAN,I.-J.L.BYEON,Y.LI,M.-D.TSAI
REVDAT 4 16-FEB-22 1BVM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BVM 1 VERSN
REVDAT 2 01-APR-03 1BVM 1 JRNL
REVDAT 1 16-SEP-99 1BVM 0
JRNL AUTH C.YUAN,I.J.BYEON,Y.LI,M.D.TSAI
JRNL TITL STRUCTURAL ANALYSIS OF PHOSPHOLIPASE A2 FROM FUNCTIONAL
JRNL TITL 2 PERSPECTIVE. 1. FUNCTIONALLY RELEVANT SOLUTION STRUCTURE AND
JRNL TITL 3 ROLES OF THE HYDROGEN-BONDING NETWORK.
JRNL REF BIOCHEMISTRY V. 38 2909 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10074343
JRNL DOI 10.1021/BI982211A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BVM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007109.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 300 MM NACL, 50 MM CACL2
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : H2O AND D2O, 50 MM CACL2, 300 MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D COSY; 2D TOCSY; 2D NOESY; 3D
REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D HN(CO)
REMARK 210 CA; 3D HNHA; 3D HNHB; 15N-EDITED
REMARK 210 NOESY-HSQC; 15N-EDITED TOCSY-
REMARK 210 HSQC; 13C-EDITED NOESY-HMQC; AND
REMARK 210 13C-EDITED HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX 600; DRX 800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO THE MEAN STRUCTURE
REMARK 210 WHICH SHOWS LITTLE RESTRAINT
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE SOLUTION STRUCTURE OF THE BOVINE PANCREATIC PHOSPHOLIPASE A2
REMARK 210 HAS BEEN
REMARK 210 DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR. THE STRUCTURES
REMARK 210 WERE
REMARK 210 CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL.
REMARK 210 (1988) FEBS
REMARK 210 LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER). THE
REMARK 210 CALCULATION IS
REMARK 210 BASED ON 1937 EXPERIMENTAL NMR RESTRAINTS (1823 DISTANCE AND 114 -
REMARK 210 RSION ANGLE
REMARK 210 RESTRAINTS).
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 OD1 ASN A 89 H GLU A 92 1.45
REMARK 500 O SER A 76 H THR A 83 1.54
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 LEU A 2 -43.61 -174.65
REMARK 500 1 ASP A 21 -64.39 -168.42
REMARK 500 1 ASN A 24 73.08 34.98
REMARK 500 1 LEU A 31 -38.10 -136.61
REMARK 500 1 SER A 34 146.43 177.69
REMARK 500 1 VAL A 63 56.67 -117.40
REMARK 500 1 LEU A 64 -74.14 -126.45
REMARK 500 1 VAL A 65 22.34 -155.97
REMARK 500 1 ASP A 66 50.37 35.48
REMARK 500 1 ASN A 67 102.48 -173.99
REMARK 500 1 TYR A 69 -63.48 -94.47
REMARK 500 1 SER A 78 146.57 166.52
REMARK 500 1 ASN A 89 -174.19 -63.78
REMARK 500 2 PHE A 22 51.19 -95.30
REMARK 500 2 SER A 34 125.10 175.24
REMARK 500 2 LEU A 64 -68.94 -107.84
REMARK 500 2 VAL A 65 24.29 -157.17
REMARK 500 2 ASN A 67 105.66 -174.67
REMARK 500 2 ASN A 71 150.49 -45.71
REMARK 500 2 SER A 78 148.64 167.48
REMARK 500 3 PHE A 22 -45.57 -156.09
REMARK 500 3 SER A 34 110.19 179.00
REMARK 500 3 VAL A 38 -44.04 -140.36
REMARK 500 3 LEU A 64 -76.88 -130.24
REMARK 500 3 ASP A 66 149.83 -37.06
REMARK 500 3 TYR A 75 -175.66 -170.48
REMARK 500 3 SER A 78 158.24 165.27
REMARK 500 3 ASN A 89 -175.37 -65.75
REMARK 500 3 ASN A 112 81.51 -63.69
REMARK 500 4 PHE A 22 40.89 -89.23
REMARK 500 4 CYS A 29 93.68 -50.06
REMARK 500 4 LEU A 64 -67.85 -104.33
REMARK 500 4 VAL A 65 22.78 -154.57
REMARK 500 4 ASP A 66 57.92 39.26
REMARK 500 4 ASN A 67 80.78 -174.48
REMARK 500 4 THR A 70 28.27 -174.13
REMARK 500 4 ASN A 72 99.55 -56.24
REMARK 500 4 SER A 78 145.92 169.33
REMARK 500 5 LEU A 2 -44.16 -131.45
REMARK 500 5 ILE A 13 77.98 -113.65
REMARK 500 5 ASP A 21 -48.97 -145.76
REMARK 500 5 ASN A 24 84.77 44.08
REMARK 500 5 TYR A 28 -62.49 -93.11
REMARK 500 5 CYS A 29 93.96 -47.08
REMARK 500 5 SER A 34 155.85 174.13
REMARK 500 5 VAL A 63 -31.11 -159.21
REMARK 500 5 VAL A 65 27.12 -156.73
REMARK 500 5 ASP A 66 146.75 -34.91
REMARK 500 5 ASN A 67 78.24 60.93
REMARK 500 5 TYR A 73 120.72 63.24
REMARK 500
REMARK 500 THIS ENTRY HAS 245 RAMACHANDRAN OUTLIERS.
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 1 ARG A 43 0.20 SIDE CHAIN
REMARK 500 1 ARG A 100 0.09 SIDE CHAIN
REMARK 500 2 ARG A 100 0.19 SIDE CHAIN
REMARK 500 3 ARG A 43 0.10 SIDE CHAIN
REMARK 500 3 ARG A 100 0.31 SIDE CHAIN
REMARK 500 4 ARG A 43 0.17 SIDE CHAIN
REMARK 500 4 ARG A 100 0.32 SIDE CHAIN
REMARK 500 5 ARG A 43 0.32 SIDE CHAIN
REMARK 500 5 ARG A 100 0.10 SIDE CHAIN
REMARK 500 6 ARG A 43 0.29 SIDE CHAIN
REMARK 500 6 ARG A 100 0.24 SIDE CHAIN
REMARK 500 7 ARG A 43 0.16 SIDE CHAIN
REMARK 500 7 ARG A 100 0.31 SIDE CHAIN
REMARK 500 8 ARG A 43 0.27 SIDE CHAIN
REMARK 500 8 ARG A 100 0.18 SIDE CHAIN
REMARK 500 9 ARG A 43 0.26 SIDE CHAIN
REMARK 500 9 ARG A 100 0.29 SIDE CHAIN
REMARK 500 10 ARG A 43 0.23 SIDE CHAIN
REMARK 500 10 ARG A 100 0.32 SIDE CHAIN
REMARK 500 11 ARG A 43 0.32 SIDE CHAIN
REMARK 500 11 ARG A 100 0.31 SIDE CHAIN
REMARK 500 12 ARG A 43 0.30 SIDE CHAIN
REMARK 500 12 ARG A 100 0.27 SIDE CHAIN
REMARK 500 13 ARG A 100 0.13 SIDE CHAIN
REMARK 500 14 ARG A 43 0.28 SIDE CHAIN
REMARK 500 14 ARG A 100 0.31 SIDE CHAIN
REMARK 500 15 ARG A 43 0.30 SIDE CHAIN
REMARK 500 15 ARG A 100 0.25 SIDE CHAIN
REMARK 500 16 ARG A 43 0.22 SIDE CHAIN
REMARK 500 17 ARG A 43 0.25 SIDE CHAIN
REMARK 500 17 ARG A 100 0.19 SIDE CHAIN
REMARK 500 18 ARG A 43 0.20 SIDE CHAIN
REMARK 500 18 ARG A 100 0.21 SIDE CHAIN
REMARK 500 19 ARG A 43 0.32 SIDE CHAIN
REMARK 500 19 ARG A 100 0.30 SIDE CHAIN
REMARK 500 20 ARG A 43 0.24 SIDE CHAIN
REMARK 500 20 ARG A 100 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: 48
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: H48-D99 CATALYTIC DIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: 99
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: H48-D99 CATALYTIC DIAD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEE NOEL, J. P. ET AL.(1989) J. CELL. BIOCHEM. 40, 309-320.
DBREF 1BVM A 1 123 UNP P00593 PA21B_BOVIN 23 145
SEQADV 1BVM ASN A 122 UNP P00593 LYS 144 VARIANT
SEQRES 1 A 123 ALA LEU TRP GLN PHE ASN GLY MET ILE LYS CYS LYS ILE
SEQRES 2 A 123 PRO SER SER GLU PRO LEU LEU ASP PHE ASN ASN TYR GLY
SEQRES 3 A 123 CYS TYR CYS GLY LEU GLY GLY SER GLY THR PRO VAL ASP
SEQRES 4 A 123 ASP LEU ASP ARG CYS CYS GLN THR HIS ASP ASN CYS TYR
SEQRES 5 A 123 LYS GLN ALA LYS LYS LEU ASP SER CYS LYS VAL LEU VAL
SEQRES 6 A 123 ASP ASN PRO TYR THR ASN ASN TYR SER TYR SER CYS SER
SEQRES 7 A 123 ASN ASN GLU ILE THR CYS SER SER GLU ASN ASN ALA CYS
SEQRES 8 A 123 GLU ALA PHE ILE CYS ASN CYS ASP ARG ASN ALA ALA ILE
SEQRES 9 A 123 CYS PHE SER LYS VAL PRO TYR ASN LYS GLU HIS LYS ASN
SEQRES 10 A 123 LEU ASP LYS LYS ASN CYS
HELIX 1 H1 TRP A 3 ILE A 13 1 11
HELIX 2 H2 ASP A 40 LEU A 58 1 19
HELIX 3 H3 ASP A 59 VAL A 63 1 5
HELIX 4 H4 ALA A 90 LYS A 108 1 19
SHEET 1 S1 1 SER A 74 SER A 78 0
SHEET 1 S2 1 GLU A 81 SER A 85 0
SSBOND 1 CYS A 11 CYS A 77 1555 1555 2.02
SSBOND 2 CYS A 27 CYS A 123 1555 1555 2.02
SSBOND 3 CYS A 29 CYS A 45 1555 1555 2.02
SSBOND 4 CYS A 44 CYS A 105 1555 1555 2.02
SSBOND 5 CYS A 51 CYS A 98 1555 1555 2.02
SSBOND 6 CYS A 61 CYS A 91 1555 1555 2.02
SSBOND 7 CYS A 84 CYS A 96 1555 1555 2.02
SITE 1 48 1 HIS A 48
SITE 1 99 1 ASP A 99
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