Header list of 1i56.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 25-FEB-01 1I56
TITLE SOLUTION STRUCTURE OF CA2+-BOUND STATE OF CANINE MILK LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 STRAIN: FAMILIARIS;
SOURCE 6 ORGAN: MAMMARY GLAND;
SOURCE 7 TISSUE: MILK;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BACTERIA;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PSCREEN 1-B(+)
KEYWDS CALCIUM BINDING LYSOZYME, ENZYME, HYDROLASE
EXPDTA SOLUTION NMR
AUTHOR Y.KOBASHIGAWA,S.TSUDA,K.NITTA
REVDAT 3 23-FEB-22 1I56 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1I56 1 VERSN
REVDAT 1 27-FEB-02 1I56 0
JRNL AUTH Y.KOBASHIGAWA,S.TSUDA,K.NITTA
JRNL TITL SOLUTION STRUCTURE OF CA2+-BOUND STATE OF CANINE MILK
JRNL TITL 2 LYSOZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012917.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: 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 LYS A 2 -172.60 -58.91
REMARK 500 SER A 25 172.47 -59.65
REMARK 500 PHE A 39 18.91 57.25
REMARK 500 ASN A 48 -161.54 -117.69
REMARK 500 LYS A 63 -29.22 -158.74
REMARK 500 TRP A 65 21.26 -158.98
REMARK 500 SER A 68 -155.70 -144.70
REMARK 500 SER A 70 40.06 -89.83
REMARK 500 SER A 72 161.31 65.60
REMARK 500 LYS A 83 54.87 -93.13
REMARK 500 ILE A 89 52.97 -101.70
REMARK 500 CYS A 116 -68.14 -156.24
REMARK 500 TYR A 124 -105.83 -70.44
REMARK 500 ASN A 129 -150.96 38.11
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 11 0.32 SIDE CHAIN
REMARK 500 ARG A 47 0.31 SIDE CHAIN
REMARK 500 ARG A 98 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QQY RELATED DB: PDB
REMARK 900 RELATED ID: 1EL1 RELATED DB: PDB
DBREF 1I56 A 2 130 UNP P81708 LYSC1_CANFA 1 129
SEQADV 1I56 SER A 1 UNP P81708 CLONING ARTIFACT
SEQRES 1 A 130 SER LYS ILE PHE SER LYS CYS GLU LEU ALA ARG LYS LEU
SEQRES 2 A 130 LYS SER MET GLY MET ASP GLY PHE HIS GLY TYR SER LEU
SEQRES 3 A 130 ALA ASN TRP VAL CYS MET ALA GLU TYR GLU SER ASN PHE
SEQRES 4 A 130 ASN THR GLN ALA PHE ASN GLY ARG ASN SER ASN GLY SER
SEQRES 5 A 130 SER ASP TYR GLY ILE PHE GLN LEU ASN SER LYS TRP TRP
SEQRES 6 A 130 CYS LYS SER ASN SER HIS SER SER ALA ASN ALA CYS ASN
SEQRES 7 A 130 ILE MET CYS SER LYS PHE LEU ASP ASP ASN ILE ASP ASP
SEQRES 8 A 130 ASP ILE ALA CYS ALA LYS ARG VAL VAL LYS ASP PRO ASN
SEQRES 9 A 130 GLY MET SER ALA TRP VAL ALA TRP VAL LYS HIS CYS LYS
SEQRES 10 A 130 GLY LYS ASP LEU SER LYS TYR LEU ALA SER CYS ASN LEU
HELIX 1 1 SER A 5 GLY A 17 1 13
HELIX 2 2 SER A 25 GLU A 36 1 12
HELIX 3 3 ASP A 90 ASP A 102 1 13
HELIX 4 4 ASN A 104 ALA A 108 5 5
HELIX 5 5 TRP A 109 CYS A 116 1 8
HELIX 6 6 TYR A 124 CYS A 128 5 5
SHEET 1 A 2 ASP A 54 TYR A 55 0
SHEET 2 A 2 LEU A 60 ASN A 61 -1 N LEU A 60 O TYR A 55
SSBOND 1 CYS A 31 CYS A 116 1555 1555 2.02
SSBOND 2 CYS A 66 CYS A 81 1555 1555 2.02
SSBOND 3 CYS A 77 CYS A 95 1555 1555 2.02
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
Complete list - 23 20 Bytes