Header list of 1z66.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 21-MAR-05 1Z66 TITLE NMR SOLUTION STRUCTURE OF DOMAIN III OF E-PROTEIN OF TICK-BORNE LANGAT TITLE 2 FLAVIVIRUS (NO RDC RESTRAINTS) COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR ENVELOPE PROTEIN E; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DOMAIN III; COMPND 5 SYNONYM: E-PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LANGAT VIRUS; SOURCE 3 ORGANISM_TAXID: 11085; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-DE3 CODON PLUS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: HIS-MBP-T KEYWDS VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.MUKHERJEE,K.DUTTA,M.A.WHITE,D.COWBURN,R.O.FOX REVDAT 4 02-MAR-22 1Z66 1 REMARK REVDAT 3 24-FEB-09 1Z66 1 VERSN REVDAT 2 31-OCT-06 1Z66 1 JRNL REVDAT 1 28-MAR-06 1Z66 0 JRNL AUTH M.MUKHERJEE,K.DUTTA,M.A.WHITE,D.COWBURN,R.O.FOX JRNL TITL NMR SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF DOMAIN III JRNL TITL 2 OF THE E PROTEIN OF TICK-BORNE LANGAT FLAVIVIRUS SUGGESTS A JRNL TITL 3 POTENTIAL SITE FOR MOLECULAR RECOGNITION. JRNL REF PROTEIN SCI. V. 15 1342 2006 JRNL REFN ISSN 0961-8368 JRNL PMID 16731969 JRNL DOI 10.1110/PS.051844006 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 2.0, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z66 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000032347. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 10MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM LANGAT E-PROTEIN DOMAIN REMARK 210 III, U-15N, 13C, 20MM BIS TRIS, REMARK 210 10MM NACL, 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : C13 EDITED NOESYHSQC; N15 EDITED REMARK 210 NOESYHSQC; HNHA; HNCO-3J REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ; 500 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D REMARK 210 HETERONUCLEAR NMR EXPERIMENTS. 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 LYS A 300 REMARK 465 GLY A 301 REMARK 465 LEU A 302 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 HB ILE A 382 HA GLN A 391 1.16 REMARK 500 HG LEU A 376 HD2 PRO A 377 1.30 REMARK 500 HD1 HIS A 323 OD1 ASP A 324 1.60 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 THR A 305 -166.59 -173.48 REMARK 500 1 TRP A 314 96.45 -53.49 REMARK 500 1 HIS A 323 -56.46 -126.89 REMARK 500 1 ASP A 324 -23.30 -175.31 REMARK 500 1 SER A 333 28.50 -149.32 REMARK 500 1 PRO A 337 97.07 -25.90 REMARK 500 1 ASN A 353 107.77 -53.20 REMARK 500 1 PRO A 360 41.68 -87.28 REMARK 500 1 ASN A 361 73.55 -165.61 REMARK 500 1 GLU A 365 -165.80 -104.24 REMARK 500 1 PRO A 377 138.20 -37.08 REMARK 500 1 PRO A 378 136.45 -34.92 REMARK 500 1 HIS A 390 122.24 -171.77 REMARK 500 2 ASP A 324 -24.73 74.13 REMARK 500 2 SER A 333 52.84 -157.25 REMARK 500 2 PRO A 337 98.25 -27.26 REMARK 500 2 PRO A 360 41.04 -91.75 REMARK 500 2 ASN A 361 65.84 -152.94 REMARK 500 2 GLU A 365 -168.53 -111.03 REMARK 500 2 PRO A 377 136.68 -32.93 REMARK 500 2 PRO A 378 128.75 -35.79 REMARK 500 3 THR A 305 -167.67 -171.29 REMARK 500 3 ARG A 316 110.24 -168.89 REMARK 500 3 PRO A 318 118.25 -30.78 REMARK 500 3 ASP A 324 23.08 47.41 REMARK 500 3 PRO A 337 92.73 -25.51 REMARK 500 3 ASN A 353 108.67 -53.29 REMARK 500 3 PRO A 360 48.93 -92.07 REMARK 500 3 ASN A 361 70.11 -170.47 REMARK 500 3 PRO A 377 133.35 -27.83 REMARK 500 3 PRO A 378 138.46 -37.09 REMARK 500 4 THR A 305 -173.61 176.78 REMARK 500 4 LYS A 311 38.19 -83.02 REMARK 500 4 HIS A 323 55.33 -140.01 REMARK 500 4 PRO A 337 92.30 -26.05 REMARK 500 4 PRO A 360 43.30 -86.71 REMARK 500 4 ASN A 361 61.03 -150.54 REMARK 500 4 GLU A 365 -168.72 -109.46 REMARK 500 4 GLN A 375 145.78 -176.04 REMARK 500 4 PRO A 377 136.36 -23.94 REMARK 500 4 PRO A 378 134.20 -37.11 REMARK 500 4 HIS A 390 116.07 -170.08 REMARK 500 5 THR A 305 -167.18 -168.43 REMARK 500 5 PRO A 318 110.69 -36.34 REMARK 500 5 ASP A 324 -24.42 170.08 REMARK 500 5 PRO A 337 97.22 -25.48 REMARK 500 5 ASN A 353 107.99 -54.37 REMARK 500 5 ALA A 355 96.93 -60.02 REMARK 500 5 PRO A 360 37.91 -92.47 REMARK 500 5 GLU A 365 -165.47 -100.12 REMARK 500 REMARK 500 THIS ENTRY HAS 218 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1YZO RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF DOMAIN III OF THE E-PROTEIN OF TICK-BORNE REMARK 900 LANGAT FLAVIVIRUS (WITHOUT RDC RESTRAINTS) REMARK 900 RELATED ID: 1SVB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ENVELOPE GLYCOPROTEIN FROM TICK-BORNE REMARK 900 ENCEPHALITIS VIRUS REMARK 900 RELATED ID: 1PJW RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE DOMAIN III OF THE JAPAN ENCEPHALITIS REMARK 900 VIRUS ENVELOPE PROTEIN REMARK 900 RELATED ID: 1S6N RELATED DB: PDB REMARK 900 NMR STRUCTURE OF DOMAIN III OF THE WEST NILE VIRUS ENVELOPE PROTEIN. DBREF 1Z66 A 300 395 UNP P29838 POLG_LANVY 580 675 SEQRES 1 A 96 LYS GLY LEU THR TYR THR VAL CYS ASP LYS THR LYS PHE SEQRES 2 A 96 THR TRP LYS ARG ALA PRO THR ASP SER GLY HIS ASP THR SEQRES 3 A 96 VAL VAL MET GLU VAL GLY PHE SER GLY THR ARG PRO CYS SEQRES 4 A 96 ARG ILE PRO VAL ARG ALA VAL ALA HIS GLY VAL PRO GLU SEQRES 5 A 96 VAL ASN VAL ALA MET LEU ILE THR PRO ASN PRO THR MET SEQRES 6 A 96 GLU ASN ASN GLY GLY GLY PHE ILE GLU MET GLN LEU PRO SEQRES 7 A 96 PRO GLY ASP ASN ILE ILE TYR VAL GLY ASP LEU ASN HIS SEQRES 8 A 96 GLN TRP PHE GLN LYS SHEET 1 A 3 THR A 313 ASP A 320 0 SHEET 2 A 3 VAL A 326 GLY A 331 -1 O VAL A 327 N THR A 319 SHEET 3 A 3 GLY A 370 MET A 374 -1 O MET A 374 N VAL A 326 SHEET 1 B 2 CYS A 338 ARG A 339 0 SHEET 2 B 2 THR A 363 MET A 364 -1 O MET A 364 N CYS A 338 SHEET 1 C 3 VAL A 342 ALA A 346 0 SHEET 2 C 3 GLY A 379 VAL A 385 -1 O ILE A 382 N VAL A 345 SHEET 3 C 3 LEU A 388 GLN A 394 -1 O LEU A 388 N VAL A 385 SSBOND 1 CYS A 307 CYS A 338 1555 1555 2.03 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 - r 2 2 Bytes