Header list of 1j4v.pdb file
Complete list - 23 20 Bytes
HEADER IMMUNE SYSTEM 21-NOV-01 1J4V TITLE CYANOVIRIN-N COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYANOVIRIN-N; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: CV-N; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC ELLIPSOSPORUM; SOURCE 3 ORGANISM_TAXID: 45916; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CYANOVIRIN-N, HIV-INACTIVATING, DOMAIN-SWAPPED DIMER, DIPOLAR KEYWDS 2 COUPLINGS / CONJOINED RIGID BODY-TORSION ANGLE DYNAMICS, IMMUNE KEYWDS 3 SYSTEM EXPDTA SOLUTION NMR AUTHOR G.M.CLORE,C.A.BEWLEY REVDAT 3 23-FEB-22 1J4V 1 REMARK REVDAT 2 24-FEB-09 1J4V 1 VERSN REVDAT 1 06-MAR-02 1J4V 0 JRNL AUTH G.M.CLORE,C.A.BEWLEY JRNL TITL USING CONJOINED RIGID BODY/TORSION ANGLE SIMULATED ANNEALING JRNL TITL 2 TO DETERMINE THE RELATIVE ORIENTATION OF COVALENTLY LINKED JRNL TITL 3 PROTEIN DOMAINS FROM DIPOLAR COUPLINGS. JRNL REF J.MAGN.RESON. V. 154 329 2002 JRNL REFN ISSN 0022-2364 JRNL PMID 11846592 JRNL DOI 10.1006/JMRE.2001.2489 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.A.BEWLEY,K.R.GUSTAFSON,M.R.BOYD,D.G.COVELL,A.BAX, REMARK 1 AUTH 2 G.M.CLORE,A.M.GRONENBORN REMARK 1 TITL SOLUTION STRUCTURE OF CYANOVIRIN-N, A POTENT REMARK 1 TITL 2 HIV-INACTIVATING PROTEIN REMARK 1 REF NAT.STRUCT.BIOL. V. 5 571 1998 REMARK 1 REFN ISSN 1072-8368 REMARK 1 DOI 10.1038/828 REMARK 1 REFERENCE 2 REMARK 1 AUTH F.YANG,C.A.BEWLEY,J.M.LOUIS,K.R.GUSTAFSON,M.R.BOYD, REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE,A.WLODAWER REMARK 1 TITL CRYSTAL STRUCTURE OF CYANOVIRIN-N, A POTENT HIV-INACTIVATING REMARK 1 TITL 2 PROTEIN, SHOWS UNEXPECTED DOMAIN SWAPPING REMARK 1 REF J.MOL.BIOL. V. 288 403 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1999.2693 REMARK 1 REFERENCE 3 REMARK 1 AUTH C.A.BEWLEY,G.M.CLORE REMARK 1 TITL DETERMINATION OF THE RELATIVE ORIENTATION OF THE TWO HALVES REMARK 1 TITL 2 OF THE DOMAIN-SWAPPED DIMER OF CYANOVIRIN-N IN SOLUTION REMARK 1 TITL 3 USING DIPOLAR COUPLINGS AND RIGID BODY MINIMIZATION. REMARK 1 REF J.AM.CHEM.SOC. V. 122 6009 2000 REMARK 1 REFN ISSN 0002-7863 REMARK 1 DOI 10.1021/JA000858O REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR-NIH (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH) REMARK 3 AUTHORS : CLORE, KUSZEWSKI, SCHWIETERS, TJANDRA REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE COORDINATES ARE NUMBERED AS FOLLOWS: REMARK 3 SUBUNIT 1: 1-101. REMARK 3 SUBUNIT 2: 201-301. REMARK 3 THE DIMER IS FULLY SYMMETRIC. REMARK 3 THE AB' HALF OF THE DIMER COMPRISES RESIDUES 1-48 AND 255-301. REMARK 3 THE A'B HALF OF THE DIMER COMPRISES RESIDUES 201-248 AND 55-101. REMARK 3 THE COORDINATES OF THE TWO HALVES OF THE DIMER ARE TAKEN FROM REMARK 3 THE X-RAY COORDINATES (3EZM, 1.5 A RESOLUTION). REMARK 3 THE ORIENTATION OF THE AB' HALF OF THE DIMER REMARK 3 (RESIDUES 1-48 AND 255-301) REMARK 3 RELATIVE TO THE A'B HALF OF THE DIMER (RESIDUES 201-248 AND REMARK 3 55-101) ARE DETERMINED BY CONJOINED RIGID BODY/TORSION ANGLE REMARK 3 DYNAMICS ON THE BASIS OF RESIDUAL DIPOLAR COUPLINGS (68 X 2), REMARK 3 ALLOWING ONLY THE PHI/PSI TORSION ANGLES OF RESIDUES 49-54 REMARK 3 AND 249-254 TO ALTER THEIR CONFORMATION (SUBJECT TO REMARK 3 NON-CRYSTALLOGRAPHIC SYMMETRY). IN ADDITION TO TERMS REMARK 3 FOR DIPOLAR COUPLINGS (CLORE ET AL. J.MAGN.RESON. 131, 159-162 REMARK 3 (1998) AND NON-CRYSTALLOGRAPHIC SYMMETRY, REMARK 3 THE TARGET FUNCTION ALSO INCLUDES A TERM OF A TORSION ANGLE REMARK 3 DATABASE POTENTIAL OF MEAN FORCE (KUSZEWSKI AND CLORE, REMARK 3 J. MAGN. RESON 146, 249-254 (2000)). REMARK 3 REMARK 3 DATA USED IN REFINEMENT: REMARK 3 68 X 2 1DNH DIPOLAR COUPLINGS MEASURED IN 5% C12E5 POLYETHYLENE REMARK 3 GLYCOL/HEXANOL MIXTURE WITH A MOLAR RATIO OF SURFACTANT TO REMARK 3 ALCOHOL OF 0.96 (PEG). REMARK 3 REMARK 3 AGREEMENT WITH EXPERIMENTAL DATA: REMARK 3 DIPOLAR COUPLING R-FACTOR (CLORE AND GARRETT (1999) REMARK 3 J. AM. CHEM. SOC. 121, 9008-9012): REMARK 3 R-DIPOLAR (WORK/PEG) (68 X 2 COUPLINGS): 14.2% REMARK 3 R-DIPOLAR (FREE/BICELLES) (18 X 2 COUPLINGS): 15.3% REMARK 3 (CROSS-VALIDATED). REMARK 3 REMARK 3 (FOR REFERENCE, THE VALUES OF R-DIPOLAR IN PEG AND BICELLES REMARK 3 FOR THE ORIENTATION OF THE TWO-HALVES OF THE DOMAIN-SWAPPED REMARK 3 DIMER IN THE X-RAY COORDINATES, 3EZM, ARE 55.9% AND 56.6%, REMARK 3 RESPECTIVELY). REMARK 3 REMARK 3 THE ONLY PROTONS IN THE COORDINATES ARE THE BACKBONE AMIDE REMARK 3 PROTONS AND THE NE1H PROTON OF TRP. NOTE THE COORDINATES FOR REMARK 3 THE TWO HALVES OF THE DOMAIN-SWAPPED DIMER ARE TAKEN DIRECTLY REMARK 3 FROM THE X-RAY COORDINATES (3EZM) AND THEIR RELATIVE ORIENTATION REMARK 3 IS DETERMINED ONLY ON THE BASIS OF N-H DIPOLAR COUPLINGS. HENCE, REMARK 3 THERE WAS NO NEED TO ADD THE OTHER PROTONS TO THE COORDINATES. REMARK 3 IN THIS ENTRY, THE LAST COLUMN REPRESENTS THE AVERAGE RMS REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES REMARK 3 (20) AND THE MEAN COORDINATE POSITIONS. BEST FITTING TO GENERATE REMARK 3 THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 1-101 AND REMARK 3 201-301. NOTE THESE ERRORS ONLY REFLECT THE PRECISION WITH REMARK 3 WHICH THE RELATIVE ORIENTATION OF THE TWO HALVES OF THE REMARK 3 DOMAIN-SWAPPED DIMER HAS BEEN DETERMINED RELATIVE TO EACH OTHER. REMARK 3 THEY DO NOT REFLECT THE ERRORS IN THE X-RAY COORDINATES OF 3EZM REMARK 3 (WHICH ARE AROUND 0.09-0.16 A). REMARK 3 NOTE THE OCCUPANCY FIELD HAS NO MEANING. REMARK 4 REMARK 4 1J4V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-01. REMARK 100 THE DEPOSITION ID IS D_1000001615. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 306 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINED REGULARIZED MEAN REMARK 210 STRUCTURE 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 RES CSSEQI ATOMS REMARK 470 GLU A 101 O REMARK 470 GLU B 301 O REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2EZM RELATED DB: PDB REMARK 900 RESTRAINED REGULARIZED MEAN NMR STRUCTURE OF CYANOVIRIN MONOMER REMARK 900 RELATED ID: 2EZN RELATED DB: PDB REMARK 900 40 STRUCTURE NMR ENSEMBLE OF CYANOVIRIN MONOMER REMARK 900 RELATED ID: 3EZM RELATED DB: PDB REMARK 900 X-RAY COORDINATES OF DOMAIN-SWAPPED DIMER OF CYANOVIRIN REMARK 900 (CRYSTALLIZED AT LOW PH) DBREF 1J4V A 1 101 UNP P81180 CVN_NOSEL 1 101 DBREF 1J4V B 201 301 UNP P81180 CVN_NOSEL 1 101 SEQRES 1 A 101 LEU GLY LYS PHE SER GLN THR CYS TYR ASN SER ALA ILE SEQRES 2 A 101 GLN GLY SER VAL LEU THR SER THR CYS GLU ARG THR ASN SEQRES 3 A 101 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL SEQRES 4 A 101 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN PRO SER SEQRES 5 A 101 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY SEQRES 6 A 101 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN SEQRES 7 A 101 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE SEQRES 8 A 101 ALA ASN ILE ASP GLY THR LEU LYS TYR GLU SEQRES 1 B 101 LEU GLY LYS PHE SER GLN THR CYS TYR ASN SER ALA ILE SEQRES 2 B 101 GLN GLY SER VAL LEU THR SER THR CYS GLU ARG THR ASN SEQRES 3 B 101 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL SEQRES 4 B 101 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN PRO SER SEQRES 5 B 101 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY SEQRES 6 B 101 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN SEQRES 7 B 101 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE SEQRES 8 B 101 ALA ASN ILE ASP GLY THR LEU LYS TYR GLU HELIX 1 1 LYS A 3 GLN A 6 5 4 HELIX 2 2 LYS B 203 GLN B 206 5 4 SHEET 1 A 3 CYS A 8 GLN A 14 0 SHEET 2 A 3 VAL A 17 GLU A 23 -1 O THR A 19 N ALA A 12 SHEET 3 A 3 TYR A 29 ASP A 35 -1 O ASN A 30 N CYS A 22 SHEET 1 B 2 ILE A 40 VAL A 43 0 SHEET 2 B 2 SER A 46 TRP A 49 -1 O LYS A 48 N GLU A 41 SHEET 1 C 3 CYS A 58 ALA A 64 0 SHEET 2 C 3 GLU A 68 LYS A 74 -1 O GLU A 68 N ALA A 64 SHEET 3 C 3 PHE A 80 ASN A 86 -1 O ILE A 85 N LEU A 69 SHEET 1 D 2 ILE A 91 ILE A 94 0 SHEET 2 D 2 THR A 97 TYR A 100 -1 O LYS A 99 N ALA A 92 SHEET 1 E 3 CYS B 208 GLN B 214 0 SHEET 2 E 3 VAL B 217 GLU B 223 -1 O THR B 219 N ALA B 212 SHEET 3 E 3 TYR B 229 ASP B 235 -1 O ASN B 230 N CYS B 222 SHEET 1 F 2 ILE B 240 VAL B 243 0 SHEET 2 F 2 SER B 246 TRP B 249 -1 O LYS B 248 N GLU B 241 SHEET 1 G 3 CYS B 258 ALA B 264 0 SHEET 2 G 3 GLU B 268 LYS B 274 -1 O GLU B 268 N ALA B 264 SHEET 3 G 3 PHE B 280 ASN B 286 -1 O ILE B 285 N LEU B 269 SHEET 1 H 2 ILE B 291 ILE B 294 0 SHEET 2 H 2 THR B 297 TYR B 300 -1 O LYS B 299 N ALA B 292 SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.03 SSBOND 2 CYS A 58 CYS A 73 1555 1555 2.04 SSBOND 3 CYS B 208 CYS B 222 1555 1555 2.03 SSBOND 4 CYS B 258 CYS B 273 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
Complete list - 23 20 Bytes