Header list of 2gg1.pdb file
Complete list - b 19 2 Bytes
HEADER VIRAL PROTEIN 23-MAR-06 2GG1 TITLE NMR SOLUTION STRUCTURE OF DOMAIN III OF THE E-PROTEIN OF TICK-BORNE TITLE 2 LANGAT FLAVIVIRUS (INCLUDES RDC RESTRAINTS) COMPND MOL_ID: 1; COMPND 2 MOLECULE: GENOME POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DOMAIN III, MAJOR ENVELOPE PROTEIN E; COMPND 5 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, DOMAIN III EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.MUKHERJEE,K.DUTTA,M.A.WHITE,D.COWBURN,R.O.FOX REVDAT 4 19-FEB-20 2GG1 1 REMARK SEQADV REVDAT 3 24-FEB-09 2GG1 1 VERSN REVDAT 2 13-JUN-06 2GG1 1 JRNL REVDAT 1 25-APR-06 2GG1 0 SPRSDE 25-APR-06 2GG1 1YZO 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 2.2, CNS 1.1 REMARK 3 AUTHORS : M. NILGES (ARIA), ALEX BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GG1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000037071. 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 : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HNCO-J REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ; 800 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 : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 GLY A 294 REMARK 465 SER A 295 REMARK 465 GLU A 296 REMARK 465 PHE A 297 REMARK 465 GLY A 298 REMARK 465 SER A 299 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 1.02 REMARK 500 HE21 GLN A 375 H LEU A 376 1.23 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 -166.83 172.22 REMARK 500 1 LYS A 309 -18.52 -44.85 REMARK 500 1 ASP A 324 53.74 86.86 REMARK 500 1 PRO A 337 96.96 -23.99 REMARK 500 1 GLU A 365 -166.13 -120.42 REMARK 500 1 PRO A 377 126.49 -28.07 REMARK 500 1 PRO A 378 134.03 -35.12 REMARK 500 1 HIS A 390 116.93 -174.83 REMARK 500 1 TRP A 392 115.27 -179.49 REMARK 500 2 THR A 305 -173.91 -179.90 REMARK 500 2 LYS A 309 -12.17 -46.12 REMARK 500 2 HIS A 323 46.46 -106.42 REMARK 500 2 PRO A 337 98.26 -26.64 REMARK 500 2 MET A 356 51.96 -97.46 REMARK 500 2 LEU A 357 111.59 -24.53 REMARK 500 2 PRO A 360 45.34 -82.17 REMARK 500 2 ASN A 361 80.44 -174.58 REMARK 500 2 GLN A 375 -173.81 -173.50 REMARK 500 2 PRO A 378 140.04 -37.80 REMARK 500 2 HIS A 390 123.19 -175.03 REMARK 500 3 THR A 305 -168.33 174.90 REMARK 500 3 PRO A 318 112.70 -39.71 REMARK 500 3 HIS A 323 53.09 -111.86 REMARK 500 3 PRO A 337 96.74 -26.63 REMARK 500 3 PRO A 350 49.70 -76.15 REMARK 500 3 VAL A 352 106.31 -169.80 REMARK 500 3 PRO A 360 36.86 -83.87 REMARK 500 3 ASN A 361 71.56 -153.35 REMARK 500 3 ASN A 366 -7.82 -54.05 REMARK 500 3 GLN A 375 175.00 177.54 REMARK 500 3 HIS A 390 116.38 -173.41 REMARK 500 4 THR A 305 -169.17 173.10 REMARK 500 4 LYS A 309 -29.71 -38.47 REMARK 500 4 PRO A 337 96.06 -24.35 REMARK 500 4 GLU A 365 -163.29 -121.71 REMARK 500 4 PRO A 377 125.79 -24.97 REMARK 500 4 PRO A 378 134.42 -35.51 REMARK 500 4 HIS A 390 116.34 -173.49 REMARK 500 5 THR A 305 -176.75 -179.85 REMARK 500 5 LYS A 309 -28.94 -38.59 REMARK 500 5 PRO A 318 108.87 -36.87 REMARK 500 5 PRO A 337 98.36 -31.70 REMARK 500 5 HIS A 347 75.50 30.37 REMARK 500 5 PRO A 360 34.60 -81.83 REMARK 500 5 ASN A 361 70.68 -151.63 REMARK 500 5 GLU A 365 -168.50 -125.64 REMARK 500 5 PRO A 377 129.63 -33.89 REMARK 500 5 PRO A 378 138.85 -34.03 REMARK 500 5 HIS A 390 119.50 -175.56 REMARK 500 6 THR A 305 -167.18 173.02 REMARK 500 REMARK 500 THIS ENTRY HAS 206 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6800 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR LANGAT DOMAIN III REMARK 900 RELATED ID: 1Z66 RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF LANGAT DOMAIN III (WITHOUT RDC RESTRAINTS) REMARK 900 RELATED ID: 1SVB RELATED DB: NDB REMARK 900 ENVELOPE GLYCOPROTEIN FROM TICK-BORNE ENCEPHALITIS VIRUS DBREF 2GG1 A 300 395 UNP P29838 POLG_LANVY 580 675 SEQADV 2GG1 GLY A 294 UNP P29838 CLONING ARTIFACT SEQADV 2GG1 SER A 295 UNP P29838 CLONING ARTIFACT SEQADV 2GG1 GLU A 296 UNP P29838 CLONING ARTIFACT SEQADV 2GG1 PHE A 297 UNP P29838 CLONING ARTIFACT SEQADV 2GG1 GLY A 298 UNP P29838 CLONING ARTIFACT SEQADV 2GG1 SER A 299 UNP P29838 CLONING ARTIFACT SEQRES 1 A 102 GLY SER GLU PHE GLY SER LYS GLY LEU THR TYR THR VAL SEQRES 2 A 102 CYS ASP LYS THR LYS PHE THR TRP LYS ARG ALA PRO THR SEQRES 3 A 102 ASP SER GLY HIS ASP THR VAL VAL MET GLU VAL GLY PHE SEQRES 4 A 102 SER GLY THR ARG PRO CYS ARG ILE PRO VAL ARG ALA VAL SEQRES 5 A 102 ALA HIS GLY VAL PRO GLU VAL ASN VAL ALA MET LEU ILE SEQRES 6 A 102 THR PRO ASN PRO THR MET GLU ASN ASN GLY GLY GLY PHE SEQRES 7 A 102 ILE GLU MET GLN LEU PRO PRO GLY ASP ASN ILE ILE TYR SEQRES 8 A 102 VAL GLY ASP LEU ASN HIS 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 GLY A 370 N VAL A 330 SHEET 1 B 4 VAL A 349 ASN A 353 0 SHEET 2 B 4 VAL A 342 ALA A 346 -1 N ALA A 346 O VAL A 349 SHEET 3 B 4 GLY A 379 VAL A 385 -1 O TYR A 384 N ARG A 343 SHEET 4 B 4 HIS A 390 GLN A 394 -1 O TRP A 392 N ASN A 381 SSBOND 1 CYS A 307 CYS A 338 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 MODEL 1
Complete list - b 19 2 Bytes