Header list of 1ccv.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE INHIBITOR 02-MAR-99 1CCV TITLE NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR TITLE 2 (AMCI). COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHYMOTRYPSIN INHIBITOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: AMCI SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA; SOURCE 3 ORGANISM_COMMON: HONEY BEE; SOURCE 4 ORGANISM_TAXID: 7460; SOURCE 5 TISSUE: HEMOLYMPH KEYWDS PROTEIN INHIBITOR, HEMOLYMPH, APIS MELLIFERA, CANONICAL INHIBITOR, KEYWDS 2 HYDROLASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.CIERPICKI,J.OTLEWSKI REVDAT 5 16-FEB-22 1CCV 1 REMARK REVDAT 4 24-FEB-09 1CCV 1 VERSN REVDAT 3 26-SEP-01 1CCV 3 ATOM HEADER COMPND JRNL REVDAT 2 18-DEC-99 1CCV 1 JRNL REVDAT 1 12-MAR-99 1CCV 0 JRNL AUTH T.CIERPICKI,J.BANIA,J.OTLEWSKI JRNL TITL NMR SOLUTION STRUCTURE OF APIS MELLIFERA JRNL TITL 2 CHYMOTRYPSIN/CATHEPSIN G INHIBITOR-1 (AMCI-1): STRUCTURAL JRNL TITL 3 SIMILARITY WITH ASCARIS PROTEASE INHIBITORS JRNL REF PROTEIN SCI. V. 9 976 2000 JRNL REFN ISSN 0961-8368 JRNL PMID 10850807 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.BANIA,D.STACHOWIAK,A.POLANOWSKI REMARK 1 TITL PRIMARY STRUCTURE AND PROPERTIES OF THE CATHEPSIN G/ REMARK 1 TITL 2 CHYMOTRYPSIN INHIBITOR FROM THE LARVAL HEMOLYMPH OF APIS REMARK 1 TITL 3 MELLIFERA REMARK 1 REF EUR.J.BIOCHEM. V. 262 680 1999 REMARK 1 REFN ISSN 0014-2956 REMARK 1 PMID 10411628 REMARK 1 DOI 10.1046/J.1432-1327.1999.00406.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CCV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-99. REMARK 100 THE DEPOSITION ID IS D_1000000575. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 2.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQFCOSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY, DYANA REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL NMR REMARK 210 SPECTROSCOPY BASED ON 666 DISTANCE RESTRAINTS, 32 ANGLE REMARK 210 RESTRAINTS AND 16 HYDROGEN BONDS 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 45 H ALA A 49 1.49 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 CYS A 3 -164.25 -62.67 REMARK 500 1 ASN A 6 1.89 83.32 REMARK 500 1 CYS A 12 80.00 -166.61 REMARK 500 1 SER A 14 107.38 -46.04 REMARK 500 1 ALA A 17 161.17 -42.00 REMARK 500 1 ARG A 26 46.00 -175.49 REMARK 500 1 ILE A 27 160.29 58.11 REMARK 500 1 MET A 30 71.11 -68.55 REMARK 500 1 GLN A 31 112.21 174.67 REMARK 500 1 CYS A 32 178.96 -54.45 REMARK 500 1 GLU A 47 35.89 -83.37 REMARK 500 1 LEU A 52 156.67 -49.19 REMARK 500 2 CYS A 3 -166.65 -102.46 REMARK 500 2 ASN A 6 2.07 83.34 REMARK 500 2 ALA A 17 164.01 -44.53 REMARK 500 2 THR A 25 161.39 -40.99 REMARK 500 2 ARG A 26 39.65 -152.60 REMARK 500 2 ILE A 27 167.59 54.32 REMARK 500 2 CYS A 28 -47.91 -147.10 REMARK 500 2 THR A 29 -171.75 -174.41 REMARK 500 2 GLN A 31 161.90 164.35 REMARK 500 2 GLU A 47 32.22 -78.96 REMARK 500 3 GLU A 2 60.92 -177.55 REMARK 500 3 CYS A 3 -164.37 -116.98 REMARK 500 3 ASN A 6 1.80 83.57 REMARK 500 3 CYS A 12 76.91 -153.55 REMARK 500 3 ALA A 17 164.90 -49.47 REMARK 500 3 ARG A 26 48.26 -175.36 REMARK 500 3 ILE A 27 161.53 57.46 REMARK 500 3 THR A 29 -163.12 -174.74 REMARK 500 3 GLN A 31 160.15 169.21 REMARK 500 3 GLU A 47 36.12 -84.57 REMARK 500 4 GLU A 2 84.66 172.06 REMARK 500 4 CYS A 3 157.23 -40.29 REMARK 500 4 ASN A 6 0.88 83.73 REMARK 500 4 ALA A 17 167.69 -44.47 REMARK 500 4 THR A 25 142.35 -38.72 REMARK 500 4 ILE A 27 160.02 -45.08 REMARK 500 4 GLN A 31 149.86 176.07 REMARK 500 4 GLU A 47 32.31 -79.01 REMARK 500 5 GLU A 2 39.52 36.22 REMARK 500 5 ASN A 6 4.54 82.04 REMARK 500 5 CYS A 12 77.87 -170.70 REMARK 500 5 ALA A 17 172.53 -47.19 REMARK 500 5 LYS A 24 140.76 -175.75 REMARK 500 5 ARG A 26 87.32 -172.07 REMARK 500 5 ILE A 27 160.08 -40.77 REMARK 500 5 MET A 30 37.55 -94.71 REMARK 500 5 GLU A 47 35.29 -84.82 REMARK 500 6 ASN A 6 4.75 82.80 REMARK 500 REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1CCV A 1 56 UNP P56682 AMCI_APIME 1 56 SEQRES 1 A 56 GLU GLU CYS GLY PRO ASN GLU VAL PHE ASN THR CYS GLY SEQRES 2 A 56 SER ALA CYS ALA PRO THR CYS ALA GLN PRO LYS THR ARG SEQRES 3 A 56 ILE CYS THR MET GLN CYS ARG ILE GLY CYS GLN CYS GLN SEQRES 4 A 56 GLU GLY PHE LEU ARG ASN GLY GLU GLY ALA CYS VAL LEU SEQRES 5 A 56 PRO GLU ASN CYS HELIX 1 1 LEU A 52 CYS A 56 5 5 SHEET 1 S1 2 GLU A 7 ASN A 10 0 SHEET 2 S1 2 GLY A 35 CYS A 38 -1 SHEET 1 S2 2 LEU A 43 ASN A 45 0 SHEET 2 S2 2 ALA A 49 VAL A 51 -1 SSBOND 1 CYS A 3 CYS A 36 1555 1555 1.99 SSBOND 2 CYS A 12 CYS A 32 1555 1555 2.15 SSBOND 3 CYS A 16 CYS A 28 1555 1555 1.98 SSBOND 4 CYS A 20 CYS A 56 1555 1555 2.03 SSBOND 5 CYS A 38 CYS A 50 1555 1555 2.04 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