Header list of 1p00.pdb file
Complete list - 23 20 Bytes
HEADER ANTIFUNGAL PROTEIN 10-APR-03 1P00
TITLE NMR STRUCTURE OF ETD151, MUTANT OF THE ANTIFUNGAL DEFENSIN ARD1 FROM
TITLE 2 ARCHAEOPREPONA DEMOPHON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFENSIN ARD1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: ETD151 MUTANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOPREPONA DEMOPHON;
SOURCE 3 ORGANISM_TAXID: 191427;
SOURCE 4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEM51
KEYWDS ALPHA-BETA PROTEIN, CSAB MOTIF (CYSTEINE STABILIZED ALPHA-HELIX BETA-
KEYWDS 2 SHEET MOTIF), ANTIFUNGAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.LANDON,M.GUENNEUGUES,F.BARBAULT,M.LEGRAIN,L.MENIN,V.SCHOTT,
AUTHOR 2 F.VOVELLE,J.L.DIMARCQ
REVDAT 3 23-FEB-22 1P00 1 REMARK
REVDAT 2 24-FEB-09 1P00 1 VERSN
REVDAT 1 09-MAR-04 1P00 0
JRNL AUTH C.LANDON,F.BARBAULT,M.LEGRAIN,L.MENIN,M.GUENNEUGUES,
JRNL AUTH 2 V.SCHOTT,F.VOVELLE,J.L.DIMARCQ
JRNL TITL LEAD OPTIMIZATION OF ANTIFUNGAL PEPTIDES WITH 3D NMR
JRNL TITL 2 STRUCTURES ANALYSIS.
JRNL REF PROTEIN SCI. V. 13 703 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 14978308
JRNL DOI 10.1110/PS.03404404
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, CNX 2000.1
REMARK 3 AUTHORS : BRUNGER (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P00 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018856.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.3
REMARK 210 IONIC STRENGTH : 40MM NA ACETATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM ETD151, 40MM NA ACETATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HOMONUCLEAR 2D DQF-COSY, TOCSY,
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.3, ARIA
REMARK 210 1.1, CNX 2000.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY AND THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES
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 H1 ASP A 1 O THR A 44 1.59
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 7 42.86 -92.45
REMARK 500 1 VAL A 12 33.19 -77.79
REMARK 500 1 ASN A 13 41.26 -162.66
REMARK 500 1 SER A 34 -141.01 69.96
REMARK 500 2 CYS A 7 43.64 -84.08
REMARK 500 2 VAL A 12 37.51 -77.75
REMARK 500 2 ASN A 13 44.31 -172.61
REMARK 500 2 SER A 34 -141.29 59.58
REMARK 500 3 CYS A 7 39.97 -88.02
REMARK 500 3 VAL A 12 41.59 -75.57
REMARK 500 3 ASN A 13 35.78 -163.34
REMARK 500 3 CYS A 18 -61.49 -28.63
REMARK 500 3 SER A 34 -141.74 70.45
REMARK 500 3 ALA A 36 -69.30 68.19
REMARK 500 3 ASN A 37 112.55 176.79
REMARK 500 3 VAL A 38 -57.25 -164.05
REMARK 500 4 VAL A 12 36.56 -78.47
REMARK 500 4 ASN A 13 34.57 -163.26
REMARK 500 4 ASN A 17 59.42 -94.58
REMARK 500 4 SER A 34 -149.60 66.17
REMARK 500 5 VAL A 12 35.62 -80.20
REMARK 500 5 ASN A 13 26.24 -153.33
REMARK 500 5 SER A 34 -139.47 56.52
REMARK 500 5 ALA A 36 27.74 47.35
REMARK 500 6 CYS A 7 44.33 -84.25
REMARK 500 6 VAL A 12 31.81 -75.06
REMARK 500 6 ASN A 13 42.97 -165.52
REMARK 500 6 SER A 34 -143.81 64.87
REMARK 500 6 ALA A 36 17.44 55.20
REMARK 500 7 CYS A 7 34.32 -85.43
REMARK 500 7 VAL A 12 43.43 -80.03
REMARK 500 7 ASN A 13 44.89 -178.61
REMARK 500 7 SER A 34 -138.13 61.77
REMARK 500 7 ALA A 36 26.81 48.81
REMARK 500 8 SER A 34 -153.40 66.51
REMARK 500 9 VAL A 12 17.95 56.16
REMARK 500 9 ASN A 13 49.64 -176.45
REMARK 500 9 CYS A 32 43.78 -85.51
REMARK 500 9 ASN A 37 95.01 50.33
REMARK 500 9 VAL A 38 -45.22 -142.14
REMARK 500 10 CYS A 7 30.51 -84.32
REMARK 500 10 SER A 34 -143.12 67.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OZZ RELATED DB: PDB
REMARK 900 STRUCTURE OF ARD1
REMARK 900 RELATED ID: 1P0A RELATED DB: PDB
REMARK 900 STRUCTURE OF ETD135, MUTANT OF ARD1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AT THE TIME OF PROCESSING, NO SEQUENCE
REMARK 999 DATABASE REFERENCE WAS AVAILABLE FOR
REMARK 999 THIS SEQUENCE. THERE IS A N19R MUTATION
REMARK 999 COMPARED TO THE WILD TYPE SEQUENCE.
DBREF 1P00 A 1 44 UNP P84156 P84156_9NEOP 1 44
SEQRES 1 A 44 ASP LYS LEU ILE GLY SER CYS VAL TRP GLY ALA VAL ASN
SEQRES 2 A 44 TYR THR SER ASN CYS ARG ALA GLU CYS LYS ARG ARG GLY
SEQRES 3 A 44 TYR LYS GLY GLY HIS CYS GLY SER PHE ALA ASN VAL ASN
SEQRES 4 A 44 CYS TRP CYS GLU THR
HELIX 1 1 ASN A 17 ARG A 25 1 9
SHEET 1 A 3 LYS A 2 SER A 6 0
SHEET 2 A 3 ASN A 39 GLU A 43 -1 O CYS A 42 N LYS A 2
SHEET 3 A 3 GLY A 29 GLY A 33 -1 N HIS A 31 O TRP A 41
SSBOND 1 CYS A 7 CYS A 32 1555 1555 2.03
SSBOND 2 CYS A 18 CYS A 40 1555 1555 2.03
SSBOND 3 CYS A 22 CYS A 42 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
MODEL 1
Complete list - 23 20 Bytes