Header list of 1s6w.pdb file
Complete list - 2 20 Bytes
HEADER ANTIBIOTIC 28-JAN-04 1S6W
TITLE SOLUTION STRUCTURE OF HYBRID WHITE STRIPED BASS HEPCIDIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPCIDIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEPCIDIN, MATURE FORM (RESIDUES 65-85);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED, THE SEQUENCE
SOURCE 4 OF THE PROTEIN OCCURS NATURALLY IN HYBRID WHITE STRIPED BASS
KEYWDS TWO STRAND ANTIPARALELL BETA SHEET, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.J.BABON,S.SINGH,M.W.PENNINGTON,R.S.NORTON,M.E.WESTERMAN
REVDAT 4 02-MAR-22 1S6W 1 REMARK
REVDAT 3 24-FEB-09 1S6W 1 VERSN
REVDAT 2 19-APR-05 1S6W 1 JRNL
REVDAT 1 14-DEC-04 1S6W 0
JRNL AUTH X.LAUTH,J.J.BABON,J.A.STANNARD,S.SINGH,V.NIZET,J.M.CARLBERG,
JRNL AUTH 2 V.E.OSTLAND,M.W.PENNINGTON,R.S.NORTON,M.E.WESTERMAN
JRNL TITL BASS HEPCIDIN SYNTHESIS, SOLUTION STRUCTURE, ANTIMICROBIAL
JRNL TITL 2 ACTIVITIES AND SYNERGISM, AND IN VIVO HEPATIC RESPONSE TO
JRNL TITL 3 BACTERIAL INFECTIONS.
JRNL REF J.BIOL.CHEM. V. 280 9272 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15546886
JRNL DOI 10.1074/JBC.M411154200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR-NIH 2.0.6, X-PLOR-NIH 2.0.6
REMARK 3 AUTHORS : C.D.SCHWIETERS, J.J.KUSZEWSKI, N.TJANDRA AND
REMARK 3 G.M.CLORE (X-PLOR-NIH), C.D.SCHWIETERS,
REMARK 3 J.J.KUSZEWSKI, N.TJANDRA AND G.M.CLORE (X-PLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 188 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 238 DIHEDRAL ANGLE RESTRAINTS, 4
REMARK 3 DISTANCE RESTRAINTSFROM HYDROGEN BONDS
REMARK 4
REMARK 4 1S6W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021442.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 4.7; 4.5
REMARK 210 IONIC STRENGTH : 0; 10MM CD3COONA
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 3.5MM HEPCIDIN, 95% H2O, 5% D2O,
REMARK 210 PH=4.7; 3.5MM HEPCIDIN, 100% D2O,
REMARK 210 10MM CD3COONA, PH=4.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; E
REMARK 210 -COSY; 13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, XWINNMR 3.5
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND CHEMICAL SHIFT DATA WAS OBTAINED
REMARK 210 USING STANDARD 2D HETERONUCLEAR TECHNIQUES PERFORMED AT NATURAL
REMARK 210 ABUNDANCE ISOTOPE LEVELS
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 O ARG A 3 H CYS A 18 1.57
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 ASN A 7 55.52 -170.57
REMARK 500 1 ASN A 11 24.69 -153.96
REMARK 500 2 CYS A 6 51.29 -117.63
REMARK 500 2 ASN A 7 54.67 -178.87
REMARK 500 2 ASN A 11 -40.43 -141.99
REMARK 500 3 ASN A 7 68.35 -174.33
REMARK 500 3 PRO A 10 48.43 -73.45
REMARK 500 3 ASN A 11 47.98 -161.18
REMARK 500 3 SER A 13 48.82 -94.87
REMARK 500 4 ASN A 7 69.24 -169.57
REMARK 500 4 ASN A 11 33.94 -160.85
REMARK 500 5 ASN A 7 101.15 -178.28
REMARK 500 5 CYS A 8 -40.01 -139.34
REMARK 500 5 ASN A 11 24.53 -159.33
REMARK 500 5 MET A 12 88.75 -174.38
REMARK 500 6 CYS A 6 42.26 -106.19
REMARK 500 6 ASN A 7 52.63 -172.59
REMARK 500 6 PRO A 10 46.34 -74.78
REMARK 500 6 ASN A 11 41.09 -160.67
REMARK 500 6 SER A 13 38.38 -96.39
REMARK 500 7 ASN A 7 133.41 -179.16
REMARK 500 7 CYS A 8 -40.08 -169.07
REMARK 500 7 ASN A 11 34.74 -160.90
REMARK 500 7 MET A 12 80.91 -175.78
REMARK 500 8 ASN A 7 59.34 -162.70
REMARK 500 8 ASN A 11 32.08 -160.25
REMARK 500 9 CYS A 6 46.40 -96.93
REMARK 500 9 ASN A 7 63.69 -175.12
REMARK 500 9 PRO A 10 49.70 -71.08
REMARK 500 9 ASN A 11 48.41 -161.47
REMARK 500 10 ASN A 7 64.39 -170.35
REMARK 500 10 ASN A 11 17.41 -146.50
REMARK 500 10 SER A 13 54.78 -98.19
REMARK 500 11 ASN A 7 100.53 -174.04
REMARK 500 11 CYS A 8 -40.60 -145.35
REMARK 500 11 ASN A 11 26.71 -156.12
REMARK 500 11 MET A 12 99.77 -173.12
REMARK 500 12 ASN A 7 44.91 -175.73
REMARK 500 12 ASN A 11 -49.26 -152.66
REMARK 500 13 CYS A 6 33.38 -97.07
REMARK 500 13 ASN A 7 98.42 -174.51
REMARK 500 13 ASN A 11 21.67 -154.45
REMARK 500 13 MET A 12 104.35 -160.78
REMARK 500 14 ASN A 7 123.68 -177.07
REMARK 500 14 CYS A 8 -44.04 -176.87
REMARK 500 14 ASN A 11 32.88 -144.90
REMARK 500 14 MET A 12 103.56 -173.11
REMARK 500 15 ASN A 7 103.25 -164.67
REMARK 500 15 CYS A 8 -42.68 -141.59
REMARK 500 15 ASN A 11 36.25 -160.95
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1S6W A 1 21 UNP P82951 HEPC_MORCS 65 85
SEQRES 1 A 21 GLY CYS ARG PHE CYS CYS ASN CYS CYS PRO ASN MET SER
SEQRES 2 A 21 GLY CYS GLY VAL CYS CYS ARG PHE
SHEET 1 A 2 ARG A 3 CYS A 5 0
SHEET 2 A 2 GLY A 16 CYS A 18 -1 O CYS A 18 N ARG A 3
SSBOND 1 CYS A 2 CYS A 19 1555 1555 2.02
SSBOND 2 CYS A 5 CYS A 18 1555 1555 2.02
SSBOND 3 CYS A 6 CYS A 15 1555 1555 2.02
SSBOND 4 CYS A 8 CYS A 9 1555 1555 2.05
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 - 2 20 Bytes