Header list of 1nxi.pdb file
Complete list - g 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-FEB-03 1NXI
TITLE SOLUTION STRUCTURE OF VIBRIO CHOLERAE PROTEIN VC0424
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN VC0424;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: VC0424;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA (LAMDADE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS STRUCTURAL GENOMICS, AB SANDWICH, COG 3076, ATCC NO. 51394D, NESG
KEYWDS 2 TARGET OP3, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.A.RAMELOT,S.NI,S.GOLDSMITH-FISCHMAN,J.R.CORT,B.HONIG,M.A.KENNEDY,
AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 6 14-JUN-23 1NXI 1 REMARK
REVDAT 5 05-FEB-20 1NXI 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1NXI 1 VERSN
REVDAT 3 25-JAN-05 1NXI 1 AUTHOR KEYWDS REMARK
REVDAT 2 04-NOV-03 1NXI 1 JRNL
REVDAT 1 01-JUL-03 1NXI 0
JRNL AUTH T.A.RAMELOT,S.NI,S.GOLDSMITH-FISCHMAN,J.R.CORT,B.HONIG,
JRNL AUTH 2 M.A.KENNEDY
JRNL TITL SOLUTION STRUCTURE OF VIBRIO CHOLERAE PROTEIN VC0424: A
JRNL TITL 2 VARIATION OF THE FERREDOXIN-LIKE FOLD.
JRNL REF PROTEIN SCI. V. 12 1556 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 12824501
JRNL DOI 10.1110/PS.03108103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH-2.0.4, X-PLOR NIH-2.0.4
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE (X-PLOR),
REMARK 3 SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1263 RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: DISTANCE
REMARK 3 CONSTRAINTS: TOTAL = 1030; INTRA-RESIDUE [I=J] = 5; SEQUENTIAL
REMARK 3 [(I-J)=1] = 250; MEDIUM RANGE [1<(I-J)<5] = 329; LONG RANGE [(I-
REMARK 3 J)>=5] = 446; HYDROGEN BOND CONSTRAINTS = 116 (2 PER H-BOND);
REMARK 3 NUMBER OF DISTANCE CONSTRAINTS PER RESIDUE = 9.0; DIHEDRAL-ANGLE
REMARK 3 CONSTRAINTS = 117 (44 PHI, 62 PSI, 11 CHI1); TOTAL NUMBER OF
REMARK 3 CONSTRAINTS PER RESIDUE = 11.0 (RESIDES 9-124); NUMBER OF LONG
REMARK 3 RANGE CONSTRAINTS PER RESIDUE = 3.9; NUMBER OF STRUCTURES
REMARK 3 COMPUTED = 20; NUMBER OF STRUCTURES USED = 20. AVERAGE DISTANCE
REMARK 3 VIOLATIONS >0.001 ANG = 27.7; AVERAGE R.M.S. DISTANCE VIOLATION =
REMARK 3 0.002 ANG; MAXIMUM NUMBER OF DISTANCE VIOLATIONS 36. AVERAGE
REMARK 3 DIHEDRAL ANGLE VIOLATIONS: >0.001 DEG = 2.0; MAX NUMBER OF
REMARK 3 DIHEDRAL ANGLE VIOLATIONS = 4 DEG; AVERAGE R.M.S. ANGLE
REMARK 3 VIOLATION = 0.03 DEG. RMSD VALUES: BACKBONE ATOMS (N,C,C',O) =
REMARK 3 0.51 ANG; ALL HEAVY ATOMS = 1.03 ANG; PROCHECK: MOST FAVORED
REMARK 3 REGIONS = 82%; ADDITIONAL ALLOWED REGIONS = 16%; GENEROUSLY
REMARK 3 ALLOWED REGIONS = 1%; DISALLOWED REGIONS = 1%.
REMARK 4
REMARK 4 1NXI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018318.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.8
REMARK 210 IONIC STRENGTH : 20MM TRIS HCL, 500MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM VC0424_DELTA16C, U-15N,
REMARK 210 13C, TRIS, PH 7.2; 1.5MM VC0424_
REMARK 210 DELTA16C, U-15N, 13C, TRIS, PH
REMARK 210 6.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; 4D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, VNMR 6.1C, SPARKY 3.98
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 O LEU A 29 H GLY A 32 1.40
REMARK 500 H LEU A 68 O ASP A 85 1.49
REMARK 500 O SER A 9 H GLU A 12 1.52
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 85.02 42.18
REMARK 500 1 HIS A 3 43.80 -80.11
REMARK 500 1 ASP A 5 67.61 -153.62
REMARK 500 1 SER A 9 60.14 -170.18
REMARK 500 1 VAL A 10 -36.94 -34.63
REMARK 500 1 ILE A 16 -75.53 -45.92
REMARK 500 1 GLN A 17 -35.41 -35.93
REMARK 500 1 GLU A 30 -36.96 -36.19
REMARK 500 1 LEU A 38 125.33 56.75
REMARK 500 1 GLU A 72 117.95 -35.41
REMARK 500 1 GLU A 76 22.46 37.89
REMARK 500 1 ASP A 77 -9.63 -154.46
REMARK 500 1 ASN A 79 -9.54 65.86
REMARK 500 1 LYS A 80 76.12 -165.64
REMARK 500 1 PHE A 111 -76.97 -98.46
REMARK 500 1 ASP A 112 33.43 166.08
REMARK 500 1 ASP A 116 73.62 -158.86
REMARK 500 1 GLU A 126 -99.35 -84.67
REMARK 500 1 HIS A 128 -124.17 -112.89
REMARK 500 1 HIS A 129 -170.22 -53.26
REMARK 500 1 HIS A 130 110.40 53.79
REMARK 500 1 HIS A 131 98.86 64.09
REMARK 500 2 GLN A 4 -161.05 -76.53
REMARK 500 2 ASP A 6 74.14 -110.25
REMARK 500 2 SER A 33 156.73 -34.51
REMARK 500 2 LEU A 38 150.85 56.25
REMARK 500 2 PHE A 50 -17.65 -41.15
REMARK 500 2 ASP A 51 -77.50 -65.81
REMARK 500 2 GLU A 69 165.33 -39.02
REMARK 500 2 THR A 73 -139.69 -117.67
REMARK 500 2 GLU A 74 128.56 178.78
REMARK 500 2 ASP A 75 -178.03 -63.23
REMARK 500 2 GLU A 76 29.91 -73.44
REMARK 500 2 ASP A 77 -35.26 -145.48
REMARK 500 2 LYS A 80 100.44 54.06
REMARK 500 2 PHE A 111 -74.89 -101.10
REMARK 500 2 ASP A 112 32.72 166.90
REMARK 500 2 HIS A 127 89.20 -67.04
REMARK 500 2 HIS A 128 -179.45 47.04
REMARK 500 2 HIS A 129 -82.18 -83.77
REMARK 500 2 HIS A 130 49.14 -178.18
REMARK 500 2 HIS A 131 -45.60 -156.67
REMARK 500 3 SER A 2 76.49 -116.55
REMARK 500 3 ILE A 25 -31.50 -36.96
REMARK 500 3 SER A 33 -175.05 -53.13
REMARK 500 3 ASP A 36 0.46 -65.36
REMARK 500 3 LEU A 38 167.29 55.00
REMARK 500 3 PHE A 50 -15.76 -46.50
REMARK 500 3 GLU A 69 158.47 -40.89
REMARK 500 3 ASP A 77 -13.76 171.35
REMARK 500
REMARK 500 THIS ENTRY HAS 416 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5589 RELATED DB: BMRB
REMARK 900 RELATED ID: OP3 RELATED DB: TARGETDB
DBREF 1NXI A 1 124 UNP Q9KUU1 Q9KUU1_VIBCH 1 124
SEQADV 1NXI LEU A 125 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI GLU A 126 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 127 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 128 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 129 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 130 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 131 UNP Q9KUU1 EXPRESSION TAG
SEQADV 1NXI HIS A 132 UNP Q9KUU1 EXPRESSION TAG
SEQRES 1 A 132 MET SER HIS GLN ASP ASP TYR LEU SER VAL GLU GLU LEU
SEQRES 2 A 132 ILE GLU ILE GLN LYS GLU GLU THR ARG ASP ILE ILE GLN
SEQRES 3 A 132 ALA LEU LEU GLU ASP GLY SER ASP PRO ASP ALA LEU TYR
SEQRES 4 A 132 GLU ILE GLU HIS HIS LEU PHE ALA GLU ASP PHE ASP LYS
SEQRES 5 A 132 LEU GLU LYS ALA ALA VAL GLU ALA PHE LYS MET GLY PHE
SEQRES 6 A 132 GLU VAL LEU GLU ALA GLU GLU THR GLU ASP GLU ASP GLY
SEQRES 7 A 132 ASN LYS LEU LEU CYS PHE ASP ALA THR MET GLN SER ALA
SEQRES 8 A 132 LEU ASP ALA LYS LEU ILE ASP GLU GLN VAL GLU LYS LEU
SEQRES 9 A 132 VAL ASN LEU ALA GLU LYS PHE ASP ILE ILE TYR ASP GLY
SEQRES 10 A 132 TRP GLY THR TYR TYR GLU GLY LEU GLU HIS HIS HIS HIS
SEQRES 11 A 132 HIS HIS
HELIX 1 1 SER A 9 GLY A 32 1 24
HELIX 2 2 ASP A 49 GLY A 64 1 16
HELIX 3 3 ASP A 93 ASP A 112 1 20
SHEET 1 A 3 LEU A 82 SER A 90 0
SHEET 2 A 3 TYR A 39 ALA A 47 -1 N HIS A 43 O ALA A 86
SHEET 3 A 3 ILE A 114 THR A 120 -1 O GLY A 119 N GLU A 42
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 - g 9 2 Bytes