Header list of 1pmc.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEINASE INHIBITOR 17-SEP-95 1PMC
TITLE PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE INHIBITOR PMP-C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LMCI II;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LOCUSTA MIGRATORIA;
SOURCE 3 ORGANISM_COMMON: MIGRATORY LOCUST;
SOURCE 4 ORGANISM_TAXID: 7004;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 TISSUE: HEMOLYMPH AND FAT BODY
KEYWDS CALCIUM CHANNEL BLOCKER, PROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 36
AUTHOR G.MER,H.HIETTER,J.-F.LEFEVRE
REVDAT 3 23-FEB-22 1PMC 1 REMARK
REVDAT 2 24-FEB-09 1PMC 1 VERSN
REVDAT 1 29-JAN-96 1PMC 0
JRNL AUTH G.MER,H.HIETTER,C.KELLENBERGER,M.RENATUS,B.LUU,J.F.LEFEVRE
JRNL TITL SOLUTION STRUCTURE OF PMP-C: A NEW FOLD IN THE GROUP OF
JRNL TITL 2 SMALL SERINE PROTEINASE INHIBITORS.
JRNL REF J.MOL.BIOL. V. 258 158 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8613985
JRNL DOI 10.1006/JMBI.1996.0240
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 1PMC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175734.
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 : 36
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: 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 ILE A 2 170.86 52.94
REMARK 500 1 SER A 3 149.38 -177.05
REMARK 500 1 CYS A 4 -177.18 175.23
REMARK 500 1 PHE A 10 -163.17 -160.10
REMARK 500 1 ASP A 12 -106.45 58.94
REMARK 500 1 LYS A 13 -159.12 -56.92
REMARK 500 1 ASN A 15 -120.16 -108.41
REMARK 500 1 LYS A 24 17.30 -155.84
REMARK 500 1 ALA A 26 116.85 -177.80
REMARK 500 1 LYS A 31 178.30 166.47
REMARK 500 1 ALA A 32 150.34 -42.89
REMARK 500 1 ASN A 35 -59.91 -138.84
REMARK 500 2 CYS A 4 172.12 169.91
REMARK 500 2 GLU A 5 104.46 -52.88
REMARK 500 2 LYS A 11 -85.26 -94.19
REMARK 500 2 ASP A 12 146.79 62.67
REMARK 500 2 LYS A 13 -146.97 60.68
REMARK 500 2 ASN A 15 -120.32 -126.38
REMARK 500 2 LYS A 24 4.36 -150.38
REMARK 500 2 ALA A 26 147.92 -176.64
REMARK 500 2 LYS A 31 175.30 167.86
REMARK 500 3 SER A 3 142.11 -177.52
REMARK 500 3 CYS A 4 179.68 174.80
REMARK 500 3 PHE A 10 -162.52 -164.87
REMARK 500 3 ASP A 12 176.84 49.92
REMARK 500 3 LYS A 13 -138.76 40.93
REMARK 500 3 ASN A 15 -113.86 -125.83
REMARK 500 3 LYS A 24 21.00 -166.18
REMARK 500 3 SER A 25 -179.93 -171.40
REMARK 500 3 ALA A 26 130.26 -177.59
REMARK 500 3 LYS A 31 -174.22 161.63
REMARK 500 3 ALA A 32 151.00 -43.56
REMARK 500 3 PRO A 34 -176.43 -63.03
REMARK 500 3 ASN A 35 76.62 57.54
REMARK 500 4 SER A 3 147.13 -177.82
REMARK 500 4 CYS A 4 177.18 176.07
REMARK 500 4 PHE A 10 -163.86 -161.94
REMARK 500 4 LYS A 11 -65.93 -101.38
REMARK 500 4 ASP A 12 168.02 54.21
REMARK 500 4 LYS A 13 -139.88 44.46
REMARK 500 4 ASN A 15 -116.62 -128.37
REMARK 500 4 LYS A 24 15.37 -158.16
REMARK 500 4 ALA A 26 141.27 -177.85
REMARK 500 4 LYS A 31 -179.89 166.95
REMARK 500 4 ALA A 32 150.87 -45.40
REMARK 500 4 ASN A 35 175.16 -54.51
REMARK 500 5 SER A 3 148.45 -177.35
REMARK 500 5 CYS A 4 173.69 171.87
REMARK 500 5 GLU A 5 103.44 -47.91
REMARK 500 5 PHE A 10 -162.98 -162.92
REMARK 500
REMARK 500 THIS ENTRY HAS 395 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 18 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.30 SIDE CHAIN
REMARK 500 3 ARG A 18 0.21 SIDE CHAIN
REMARK 500 4 ARG A 18 0.17 SIDE CHAIN
REMARK 500 5 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 18 0.27 SIDE CHAIN
REMARK 500 7 ARG A 18 0.10 SIDE CHAIN
REMARK 500 8 ARG A 18 0.30 SIDE CHAIN
REMARK 500 9 ARG A 18 0.30 SIDE CHAIN
REMARK 500 10 ARG A 18 0.20 SIDE CHAIN
REMARK 500 11 ARG A 18 0.29 SIDE CHAIN
REMARK 500 12 ARG A 18 0.31 SIDE CHAIN
REMARK 500 14 ARG A 18 0.29 SIDE CHAIN
REMARK 500 15 ARG A 18 0.32 SIDE CHAIN
REMARK 500 16 ARG A 18 0.20 SIDE CHAIN
REMARK 500 17 ARG A 18 0.25 SIDE CHAIN
REMARK 500 18 ARG A 18 0.26 SIDE CHAIN
REMARK 500 19 ARG A 18 0.28 SIDE CHAIN
REMARK 500 20 ARG A 18 0.27 SIDE CHAIN
REMARK 500 21 ARG A 18 0.26 SIDE CHAIN
REMARK 500 22 ARG A 18 0.27 SIDE CHAIN
REMARK 500 23 ARG A 18 0.31 SIDE CHAIN
REMARK 500 24 ARG A 18 0.31 SIDE CHAIN
REMARK 500 25 ARG A 18 0.23 SIDE CHAIN
REMARK 500 26 ARG A 18 0.32 SIDE CHAIN
REMARK 500 27 ARG A 18 0.25 SIDE CHAIN
REMARK 500 28 ARG A 18 0.22 SIDE CHAIN
REMARK 500 29 ARG A 18 0.27 SIDE CHAIN
REMARK 500 30 ARG A 18 0.12 SIDE CHAIN
REMARK 500 31 ARG A 18 0.17 SIDE CHAIN
REMARK 500 32 ARG A 18 0.14 SIDE CHAIN
REMARK 500 33 ARG A 18 0.30 SIDE CHAIN
REMARK 500 34 ARG A 18 0.15 SIDE CHAIN
REMARK 500 35 ARG A 18 0.31 SIDE CHAIN
REMARK 500 36 ARG A 18 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: P
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1PMC A 1 36 UNP P80060 LCM_LOCMI 57 92
SEQRES 1 A 36 GLU ILE SER CYS GLU PRO GLY LYS THR PHE LYS ASP LYS
SEQRES 2 A 36 CYS ASN THR CYS ARG CYS GLY ALA ASP GLY LYS SER ALA
SEQRES 3 A 36 ALA CYS THR LEU LYS ALA CYS PRO ASN GLN
SHEET 1 S1 3 LYS A 8 LYS A 11 0
SHEET 2 S1 3 THR A 16 CYS A 19 -1
SHEET 3 S1 3 ALA A 26 LEU A 30 -1
SSBOND 1 CYS A 4 CYS A 19 1555 1555 2.02
SSBOND 2 CYS A 14 CYS A 33 1555 1555 2.03
SSBOND 3 CYS A 17 CYS A 28 1555 1555 2.03
SITE 1 P 4 THR A 29 LEU A 30 LYS A 31 ALA A 32
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 23 2 Bytes