Header list of 1xpv.pdb file
Complete list - n 31 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 09-OCT-04 1XPV TITLE SOLUTION STRUCTURE OF NORTHEAST STRUCTURAL GENOMICS TARGET PROTEIN TITLE 2 XCR50 FROM X. CAMPESTRIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN XCC2852; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS; SOURCE 3 ORGANISM_TAXID: 339; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ALPHA+BETA, GFT NMR, STRUCTURAL GENOMICS, NESGC, XCR50, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, KEYWDS 3 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.SHAO,T.B.ACTON,G.LIU,L.MA,Y.SHEN,R.XIAO,G.T.MONTELIONE,T.SZYPERSKI, AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 5 31-JAN-18 1XPV 1 JRNL REMARK REVDAT 4 24-FEB-09 1XPV 1 VERSN REVDAT 3 22-MAY-07 1XPV 1 AUTHOR JRNL REVDAT 2 25-JAN-05 1XPV 1 AUTHOR KEYWDS REMARK REVDAT 1 14-DEC-04 1XPV 0 JRNL AUTH Y.SHAO,T.B.ACTON,G.LIU,L.MA,Y.SHEN,R.XIAO,G.T.MONTELIONE, JRNL AUTH 2 T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) JRNL TITL SOLUTION STRUCTURE OF NORTHEAST STRUCTURAL GENOMICS TARGET JRNL TITL 2 PROTEIN XCR50 FROM X. CAMPESTRIS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AUTOASSIGN 1.13, DYANA 1.5 REMARK 3 AUTHORS : ZIMMERMAN (AUTOASSIGN), GUENTER (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XPV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030625. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.77 MM PROTEIN, 0.02% NAN3, REMARK 210 10MM DTT, 5MM CACL2, 100MM NACL, REMARK 210 20MM MES, 5% D2O, 95% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : GFT (4,3)D HNNCABCA; GFT (4,3)D REMARK 210 CABCA(CO)NHN; GFT (4,3)D REMARK 210 HABCAB(CO)NHN; GFT (4,3)D HCCH; REMARK 210 SIMULTANEOUS HETERONUCLEAR- REMARK 210 RESOLVED [1H, 1H]-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, XEASY 1.3.1.3, REMARK 210 DYANA 1.5, AUTOSTRUCTURE 2.0.0, REMARK 210 CYANA 1.1 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 : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING GFT NMR 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 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 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 ALA A 2 -135.16 -90.67 REMARK 500 1 ASP A 9 158.65 -43.46 REMARK 500 1 ASP A 10 143.48 62.83 REMARK 500 1 HIS A 12 -64.30 -174.65 REMARK 500 1 ASP A 36 -32.64 168.96 REMARK 500 1 TYR A 44 -71.92 -100.60 REMARK 500 1 ARG A 47 37.33 -90.50 REMARK 500 2 LEU A 3 -177.68 -64.45 REMARK 500 2 ASP A 9 94.16 59.48 REMARK 500 2 ASP A 10 111.15 63.47 REMARK 500 2 ASP A 36 -52.57 82.26 REMARK 500 2 TYR A 44 -70.27 -107.90 REMARK 500 2 ARG A 47 37.57 -90.40 REMARK 500 2 ARG A 57 -172.34 80.59 REMARK 500 2 ALA A 75 64.43 39.97 REMARK 500 2 HIS A 77 -66.92 -127.74 REMARK 500 3 ALA A 2 -157.55 -69.96 REMARK 500 3 ASP A 9 80.08 48.90 REMARK 500 3 HIS A 12 -54.82 -172.58 REMARK 500 3 ASP A 35 172.80 -59.57 REMARK 500 3 ASP A 37 94.69 -163.15 REMARK 500 3 ARG A 47 36.60 -90.44 REMARK 500 4 ALA A 2 -166.38 -102.37 REMARK 500 4 HIS A 12 -66.95 -167.73 REMARK 500 4 ASP A 36 -53.02 81.95 REMARK 500 4 TYR A 44 -71.15 -110.67 REMARK 500 4 ARG A 47 37.07 -90.11 REMARK 500 4 ALA A 75 138.07 -39.73 REMARK 500 4 HIS A 77 89.64 38.46 REMARK 500 5 ALA A 2 -169.75 -102.58 REMARK 500 5 ASP A 9 147.18 73.07 REMARK 500 5 CYS A 11 -66.49 -131.63 REMARK 500 5 HIS A 12 -59.14 -169.15 REMARK 500 5 ASP A 36 -53.04 81.84 REMARK 500 5 ASP A 37 94.30 -68.19 REMARK 500 5 TYR A 44 -73.34 -115.08 REMARK 500 5 ARG A 47 36.42 -89.76 REMARK 500 6 ASP A 9 -56.46 78.06 REMARK 500 6 HIS A 12 -78.22 -150.80 REMARK 500 6 ASP A 36 -40.47 -177.46 REMARK 500 6 TYR A 44 -70.70 -106.69 REMARK 500 6 ARG A 47 37.43 -90.63 REMARK 500 6 ALA A 75 86.45 39.67 REMARK 500 7 ASP A 9 90.20 64.03 REMARK 500 7 HIS A 12 -60.60 -167.23 REMARK 500 7 ASP A 37 94.36 172.45 REMARK 500 7 ARG A 47 38.86 -93.07 REMARK 500 7 ALA A 75 166.56 56.13 REMARK 500 7 HIS A 77 -70.69 -153.50 REMARK 500 8 ASP A 9 101.25 64.19 REMARK 500 REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: XCR50 RELATED DB: TARGETDB DBREF 1XPV A 1 78 UNP Q8P6W3 Q8P6W3_XANCP 1 78 SEQRES 1 A 78 MET ALA LEU THR LEU TYR GLN ARG ASP ASP CYS HIS LEU SEQRES 2 A 78 CYS ASP GLN ALA VAL GLU ALA LEU ALA GLN ALA ARG ALA SEQRES 3 A 78 GLY ALA PHE PHE SER VAL PHE ILE ASP ASP ASP ALA ALA SEQRES 4 A 78 LEU GLU SER ALA TYR GLY LEU ARG VAL PRO VAL LEU ARG SEQRES 5 A 78 ASP PRO MET GLY ARG GLU LEU ASP TRP PRO PHE ASP ALA SEQRES 6 A 78 PRO ARG LEU ARG ALA TRP LEU ASP ALA ALA PRO HIS ALA HELIX 1 1 HIS A 12 ARG A 25 1 14 HELIX 2 2 ASP A 37 TYR A 44 1 8 HELIX 3 3 GLY A 45 VAL A 48 5 4 HELIX 4 4 ASP A 64 ALA A 74 1 11 SHEET 1 A 4 PHE A 30 PHE A 33 0 SHEET 2 A 4 THR A 4 GLN A 7 1 N GLN A 7 O VAL A 32 SHEET 3 A 4 LEU A 51 ARG A 52 -1 O ARG A 52 N THR A 4 SHEET 4 A 4 GLU A 58 LEU A 59 -1 O LEU A 59 N LEU A 51 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 - n 31 2 Bytes