Header list of 1hvz.pdb file
Complete list - 23 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 09-JAN-01 1HVZ
TITLE RTD-1, A CYCLIC ANTIMICROBIAL DEFENSIN FROM RHESUS MACAQUE LEUKOCYTES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THETA DEFENSIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RTD-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OCCURS NATURALLY IN RHESUS MACAQUES (MUCACA MULATTA)
KEYWDS CYCLIC, BETA-SHEET, DISULFIDE-RICH, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.CRAIK,M.TRABI,H.J.SCHIRRA
REVDAT 3 23-FEB-22 1HVZ 1 REMARK LINK
REVDAT 2 24-FEB-09 1HVZ 1 VERSN
REVDAT 1 30-MAY-01 1HVZ 0
JRNL AUTH M.TRABI,H.J.SCHIRRA,D.J.CRAIK
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF RTD-1, A CYCLIC ANTIMICROBIAL
JRNL TITL 2 DEFENSIN FROM RHESUS MACAQUE LEUKOCYTES.
JRNL REF BIOCHEMISTRY V. 40 4211 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11284676
JRNL DOI 10.1021/BI002028T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 94 RESTRAINTS, 87 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 7
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1HVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012617.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 300; 280
REMARK 210 PH : 4.5; 4.5; 4.5
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE; 20MM
REMARK 210 SODIUM PHOSPHATE; 20MM SODIUM
REMARK 210 PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM RTD-1, 20MM SODIUM PHOSPHATE
REMARK 210 PH 4.5, 80% H2O, 10% D2O, 10%
REMARK 210 ACETONITRILE-D3; 1MM RTD-1, 20MM
REMARK 210 SODIUM PHOSPHATE PH 4.5, 90% H2O,
REMARK 210 10% D2O; 1MM RTD-1, 20MM SODIUM
REMARK 210 PHOSPHATE PH 4.5, 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, CCNMR, X-PLOR
REMARK 210 3.851, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING, EXPLICIT
REMARK 210 INCLUSION OF WATER MOLECULES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 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
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 ARG A 9 79.33 -62.53
REMARK 500 2 LEU A 6 69.01 -106.65
REMARK 500 2 ARG A 9 79.60 -60.82
REMARK 500 2 CYS A 14 58.55 -110.16
REMARK 500 3 ARG A 9 78.36 -61.77
REMARK 500 4 CYS A 5 66.83 -118.43
REMARK 500 4 CYS A 7 146.59 69.83
REMARK 500 4 ARG A 9 80.62 -63.76
REMARK 500 4 CYS A 12 55.37 -96.82
REMARK 500 4 CYS A 14 174.42 65.52
REMARK 500 5 PHE A 2 135.51 -178.26
REMARK 500 5 ARG A 9 79.09 -61.78
REMARK 500 6 ARG A 4 -64.57 -122.44
REMARK 500 6 ARG A 9 80.93 -67.61
REMARK 500 6 ARG A 13 79.33 -103.79
REMARK 500 7 ARG A 9 78.77 -65.13
REMARK 500 7 CYS A 16 74.48 58.05
REMARK 500 8 PHE A 2 146.01 -178.24
REMARK 500 8 ARG A 9 79.98 -60.01
REMARK 500 9 ARG A 4 -24.89 -161.10
REMARK 500 9 ARG A 9 78.51 -63.42
REMARK 500 9 ARG A 13 26.70 -161.11
REMARK 500 9 CYS A 14 81.49 58.61
REMARK 500 10 LEU A 6 55.33 -113.27
REMARK 500 10 ARG A 9 78.21 -61.36
REMARK 500 11 ARG A 9 77.69 -63.62
REMARK 500 11 CYS A 12 52.32 -109.98
REMARK 500 11 ARG A 13 61.97 -158.97
REMARK 500 11 CYS A 14 82.83 56.55
REMARK 500 12 ARG A 9 77.95 -65.87
REMARK 500 13 PHE A 2 146.61 -177.43
REMARK 500 13 CYS A 7 107.80 -51.71
REMARK 500 13 ARG A 9 81.10 -66.04
REMARK 500 13 ARG A 13 -16.21 179.67
REMARK 500 13 CYS A 16 146.68 72.13
REMARK 500 14 ARG A 9 79.76 -63.18
REMARK 500 14 CYS A 14 94.41 -64.82
REMARK 500 14 CYS A 16 143.96 76.92
REMARK 500 15 ARG A 9 80.07 -67.41
REMARK 500 16 PHE A 2 142.65 -171.08
REMARK 500 16 CYS A 5 44.79 -107.56
REMARK 500 16 CYS A 7 152.78 68.93
REMARK 500 16 ARG A 9 78.94 -62.44
REMARK 500 17 ARG A 9 79.72 -66.23
REMARK 500 17 CYS A 16 100.81 63.93
REMARK 500 18 ARG A 9 79.40 -64.32
REMARK 500 19 PHE A 2 139.64 -172.95
REMARK 500 19 CYS A 7 149.18 71.65
REMARK 500 19 ARG A 9 82.34 -65.26
REMARK 500 19 CYS A 14 131.11 68.02
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE RESIDUES NUMBERED ACCORDING TO TANG ET AL., SCIENCE 286
REMARK 999 (1999), PP. 498-502
DBREF 1HVZ A 1 12 GB 7512249 C59089 7 18
DBREF 1HVZ A 13 18 GB 7512249 C59089 1 6
SEQRES 1 A 18 GLY PHE CYS ARG CYS LEU CYS ARG ARG GLY VAL CYS ARG
SEQRES 2 A 18 CYS ILE CYS THR ARG
SHEET 1 A 2 CYS A 5 ARG A 8 0
SHEET 2 A 2 VAL A 11 CYS A 14 -1 O VAL A 11 N ARG A 8
SSBOND 1 CYS A 3 CYS A 16 1555 1555 2.03
SSBOND 2 CYS A 5 CYS A 14 1555 1555 2.03
SSBOND 3 CYS A 7 CYS A 12 1555 1555 2.03
LINK N GLY A 1 C ARG A 18 1555 1555 1.33
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