Header list of 1z3r.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 14-MAR-05 1Z3R TITLE SOLUTION STRUCTURE OF THE OMSK HEMHORRAGHIC FEVER ENVELOPE PROTEIN TITLE 2 DOMAIN III COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: OMSK HEMORRHAGIC FEVER ENVELOPE PROTEIN DOMAIN III; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: OMSK HEMORRHAGIC FEVER VIRUS; SOURCE 3 ORGANISM_TAXID: 12542; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMAL_C2X KEYWDS FLAVIVIRUS DOMAIN III, OMSK HEMORRHAGIC FEVER, OHF, ENVELOPE PROTEIN, KEYWDS 2 VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR D.E.VOLK,L.CHAVEZ,D.W.BEASLEY,A.D.BARRETT,D.G.GORENSTEIN REVDAT 4 02-MAR-22 1Z3R 1 REMARK SEQADV REVDAT 3 24-FEB-09 1Z3R 1 VERSN REVDAT 2 01-AUG-06 1Z3R 1 JRNL REVDAT 1 14-MAR-06 1Z3R 0 JRNL AUTH D.E.VOLK,L.CHAVEZ,D.W.BEASLEY,A.D.BARRETT,M.R.HOLBROOK, JRNL AUTH 2 D.G.GORENSTEIN JRNL TITL STRUCTURE OF THE ENVELOPE PROTEIN DOMAIN III OF OMSK JRNL TITL 2 HEMORRHAGIC FEVER VIRUS. JRNL REF VIROLOGY V. 351 188 2006 JRNL REFN ISSN 0042-6822 JRNL PMID 16647096 JRNL DOI 10.1016/J.VIROL.2006.03.030 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 2000, TALOS 1.0 REMARK 3 AUTHORS : ACCELRYS, INC. (FELIX), CORNILESCU, DELAGLIO AND REMARK 3 BAX (TALOS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z3R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032260. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : 100 MM NACL 25 MM TRIS-D11 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : UNIFORM (RANDOM) LABELING WITH REMARK 210 15N REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; VXRS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.3, SANE 04-04-27, AMBER REMARK 210 6.0 REMARK 210 METHOD USED : SIMULATED ANNEALING AND REMARK 210 MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 HG1 THR A 28 OE2 GLU A 76 1.33 REMARK 500 HG1 THR A 66 OE2 GLU A 68 1.37 REMARK 500 HG SER A 24 OG1 THR A 28 1.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 2 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 3 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 3 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 4 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 4 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 5 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES REMARK 500 5 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 6 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 6 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 7 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 7 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 8 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 9 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 10 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 10 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 10 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 11 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 11 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 11 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 12 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 12 TYR A 87 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 13 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 14 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 14 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 15 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES 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 SER A 2 103.73 -58.00 REMARK 500 1 HIS A 50 99.82 -48.55 REMARK 500 1 ASN A 64 101.98 -34.18 REMARK 500 2 SER A 2 92.19 -40.74 REMARK 500 2 LYS A 3 46.86 -72.74 REMARK 500 2 THR A 38 160.77 -49.78 REMARK 500 2 HIS A 50 92.65 -55.95 REMARK 500 2 ALA A 58 95.42 -69.77 REMARK 500 2 ASN A 64 102.40 -33.22 REMARK 500 3 LEU A 5 -45.59 68.02 REMARK 500 3 THR A 6 -65.45 -91.43 REMARK 500 3 THR A 38 160.38 -47.52 REMARK 500 3 HIS A 50 105.47 -52.15 REMARK 500 3 ASN A 64 97.90 -35.79 REMARK 500 3 ASN A 70 27.45 -64.80 REMARK 500 4 THR A 38 160.43 -49.89 REMARK 500 4 HIS A 50 95.29 -51.01 REMARK 500 4 ASN A 64 101.25 -34.58 REMARK 500 5 LYS A 12 -9.52 -58.79 REMARK 500 5 HIS A 50 100.65 -48.72 REMARK 500 5 ASN A 64 106.13 -32.23 REMARK 500 6 SER A 2 97.66 -39.27 REMARK 500 6 THR A 38 158.29 -48.45 REMARK 500 6 HIS A 50 104.79 -53.77 REMARK 500 6 ASN A 64 102.17 -43.41 REMARK 500 7 SER A 2 93.52 -68.44 REMARK 500 7 LYS A 3 48.70 -72.22 REMARK 500 7 LYS A 14 0.50 -69.46 REMARK 500 7 THR A 38 170.66 -54.05 REMARK 500 7 HIS A 50 103.30 -41.63 REMARK 500 7 ASN A 64 96.84 -23.87 REMARK 500 8 LYS A 3 29.57 -75.11 REMARK 500 8 THR A 38 150.98 -49.00 REMARK 500 8 HIS A 50 99.90 -55.43 REMARK 500 8 ASN A 64 110.46 -38.09 REMARK 500 9 HIS A 50 104.17 -53.45 REMARK 500 9 ASN A 64 109.14 -36.59 REMARK 500 10 SER A 2 103.97 -54.17 REMARK 500 10 THR A 38 152.05 -48.43 REMARK 500 10 HIS A 50 91.94 -56.62 REMARK 500 10 ASN A 64 103.89 -32.92 REMARK 500 11 THR A 38 161.86 -49.41 REMARK 500 11 HIS A 50 103.51 -41.97 REMARK 500 11 ASN A 64 105.26 -43.82 REMARK 500 12 SER A 2 -164.91 59.94 REMARK 500 12 HIS A 50 97.47 -51.79 REMARK 500 12 ASN A 64 98.68 -29.18 REMARK 500 12 ASN A 70 26.88 -145.38 REMARK 500 12 PRO A 81 151.59 -49.44 REMARK 500 13 SER A 2 95.94 -49.70 REMARK 500 REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 2 ARG A 42 0.09 SIDE CHAIN REMARK 500 4 ARG A 42 0.09 SIDE CHAIN REMARK 500 4 TYR A 87 0.09 SIDE CHAIN REMARK 500 12 TYR A 87 0.08 SIDE CHAIN REMARK 500 15 TYR A 87 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z3R A 3 99 UNP Q80J38 Q80J38_9FLAV 57 153 SEQADV 1Z3R ILE A 1 UNP Q80J38 CLONING ARTIFACT SEQADV 1Z3R SER A 2 UNP Q80J38 CLONING ARTIFACT SEQRES 1 A 99 ILE SER LYS GLY LEU THR TYR THR MET CYS ASP LYS ALA SEQRES 2 A 99 LYS PHE THR TRP LYS ARG ALA PRO THR ASP SER GLY HIS SEQRES 3 A 99 ASP THR VAL VAL MET GLU VAL ALA PHE SER GLY THR LYS SEQRES 4 A 99 PRO CYS ARG ILE PRO VAL ARG ALA VAL ALA HIS GLY ALA SEQRES 5 A 99 PRO ASP VAL ASP VAL ALA MET LEU ILE THR PRO ASN PRO SEQRES 6 A 99 THR MET GLU ASN ASN GLY GLY GLY PHE ILE GLU MET GLN SEQRES 7 A 99 LEU PRO PRO GLY ASP ASN ILE ILE TYR VAL GLY GLU LEU SEQRES 8 A 99 LYS HIS GLN TRP PHE GLN LYS GLY SHEET 1 A 4 PHE A 15 ASP A 23 0 SHEET 2 A 4 VAL A 29 PHE A 35 -1 O GLU A 32 N ARG A 19 SHEET 3 A 4 PHE A 74 GLN A 78 -1 O MET A 77 N VAL A 29 SHEET 4 A 4 MET A 59 LEU A 60 -1 N MET A 59 O GLN A 78 SHEET 1 B 2 CYS A 41 ARG A 42 0 SHEET 2 B 2 THR A 66 MET A 67 -1 O MET A 67 N CYS A 41 SHEET 1 C 3 VAL A 45 ALA A 49 0 SHEET 2 C 3 GLY A 82 VAL A 88 -1 O ILE A 85 N VAL A 48 SHEET 3 C 3 LEU A 91 GLN A 97 -1 O LEU A 91 N VAL A 88 SSBOND 1 CYS A 10 CYS A 41 1555 1555 2.02 CISPEP 1 LYS A 39 PRO A 40 1 0.71 CISPEP 2 LYS A 39 PRO A 40 2 -5.68 CISPEP 3 LYS A 39 PRO A 40 3 -7.84 CISPEP 4 LYS A 39 PRO A 40 4 -7.56 CISPEP 5 LYS A 39 PRO A 40 5 -6.38 CISPEP 6 LYS A 39 PRO A 40 6 -9.77 CISPEP 7 LYS A 39 PRO A 40 7 -9.88 CISPEP 8 LYS A 39 PRO A 40 8 -4.34 CISPEP 9 LYS A 39 PRO A 40 9 -7.82 CISPEP 10 LYS A 39 PRO A 40 10 7.62 CISPEP 11 LYS A 39 PRO A 40 11 -4.50 CISPEP 12 LYS A 39 PRO A 40 12 2.25 CISPEP 13 LYS A 39 PRO A 40 13 -6.12 CISPEP 14 LYS A 39 PRO A 40 14 -1.95 CISPEP 15 LYS A 39 PRO A 40 15 1.40 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