Header list of 1kkg.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS 07-DEC-01 1KKG
TITLE NMR STRUCTURE OF RIBOSOME-BINDING FACTOR A (RBFA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOME-BINDING FACTOR A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RBFA, COLD-SHOCK ADAPTATION PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: RBFA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS COLD-SHOCK ADAPTATION, RIBOSOME-BINDING FACTOR, NESG PROJECT,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR Y.J.HUANG,G.V.T.SWAPNA,P.K.RAJAN,H.KE,B.XIA,K.SHUKLA,M.INOUYE,
AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 23-FEB-22 1KKG 1 REMARK
REVDAT 3 24-FEB-09 1KKG 1 VERSN
REVDAT 2 25-JAN-05 1KKG 1 AUTHOR KEYWDS REMARK
REVDAT 1 18-MAR-03 1KKG 0
JRNL AUTH Y.J.HUANG,G.V.T.SWAPNA,P.K.RAJAN,H.KE,B.XIA,K.SHUKLA,
JRNL AUTH 2 M.INOUYE,G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF RIBOSOME-BINDING FACTOR A (RBFA),
JRNL TITL 2 A COLD-SHOCK ADAPTATION PROTEIN FROM ESCHERICHIA COLI
JRNL REF J.MOL.BIOL. V. 327 521 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12628255
JRNL DOI 10.1016/S0022-2836(03)00061-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.V.SWAPNA,K.SHUKLA,Y.J.HUANG,H.KE,B.XIA,M.INOUYE,
REMARK 1 AUTH 2 G.T.MONTELIONE
REMARK 1 TITL RESONANCE ASSIGNMENTS FOR COLD-SHOCK PROTEIN
REMARK 1 TITL 2 RIBOSOME-BINDING FACTOR A (RBFA) FROM ESCHERICHIA COLI.
REMARK 1 REF J.BIOMOL.NMR V. 21 389 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1013302924843
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AUTOASSIGN 1.7.7, DYANA 1.5
REMARK 3 AUTHORS : MOSELEY, H., ZIMMERMANN, D.E., HUANG, Y.J.,
REMARK 3 KULIKOWSKI, C.G. AND MONTELIONE, G.T. (AUTOASSIGN),
REMARK 3 GUNTERT, P., MUMENTHALER, C. AND WUTHRICH, K.
REMARK 3 (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 1970 RESTRAINTS, 1698 CONFORMATIONALLY-RESTRICTING NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS, 184 DIHEDRAL ANGLE CONSTRAINTS,
REMARK 3 88 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. SUMMARY OF
REMARK 3 RBFA STRUCTURE CALCULATION BY AUTOSTRUCTURE: SUMMARY OF
REMARK 3 EXPERIMENTAL CONSTRAINTS: DISTANCE CONSTRAINTS: TOTAL = 1698;
REMARK 3 INTRA-RESIDUE [I=J] = 175; SEQUENTIAL [(I-J)=1] = 454; MEDIUM
REMARK 3 RANGE [1<(I-J)<5] = 595; LONG RANGE [(I-J)>=5] = 474; NUMBER
REMARK 3 OF DISTANCE CONSTRAINTS PER RESIDUE = 15.7; DIHEDRAL-ANGLE
REMARK 3 CONSTRAINTS = 184; TOTAL HYDROGEN BOND CONSTRAINTS = 88; LONG
REMARK 3 RANGE HYDROGEN BOND CONSTRAINTS = 24; TOTAL NUMBER OF
REMARK 3 CONSTRAINTS PER RESIDUE = 18.2; NUMBER OF LONG RANGE
REMARK 3 CONSTRAINTS PER RESIDUE = 4.6; NUMBER OF STRUCTURES COMPUTED =
REMARK 3 200; NUMBER OF STRUCTURES USED = 16. RESIDUAL CONSTRAINT
REMARK 3 VIOLATIONS: DISTANCE VIOLATIONS 0.1-0.2ANG = 31; 0.2-0.5ANG
REMARK 3 = 9; >0.5ANG = 1. MAX DISTANCE VIOLATION = 0.57ANG; AVERAGE
REMARK 3 DISTANCE VIOLATION = 0.00ANG. MAX. VDW VIOLATION = 0.37 ANG.
REMARK 3 DIHEDRAL ANGLE VIOLATIONS: 0 - 10 DEG = 6; >10 DEG = 0; MAX
REMARK 3 ANGLE VIOLATION = 9 DEG; AVERAGE ANGLE VIOLATION = 0.06 DEG.
REMARK 3 RMSD VALUES : ALL BACKBONE ATOMS OF ALL RESIDUES = 0.5 ANG; ALL
REMARK 3 BACKBONE ATOMS OF ORDERED RESIDUES = 0.5 ANG; ALL HEAVY ATOMS OF
REMARK 3 ALL RESIDUES = 1.0 ANG; ALL HEAVY ATOMS OF ORDERED RESIDUES =
REMARK 3 1.0 ANG. PROCHECK USING ALL RESIDUES: MOST FAVORED REGIONS =
REMARK 3 73%; ADDITIONAL ALLOWED REGIONS = 23%; GENEROUSLY ALLOWED
REMARK 3 REGIONS = 4%; DISALLOWED REGIONS = 0%. NMR R-FACTORS : M =
REMARK 3 39% I=46% L=27% . SPECTRAL INFORMATION: TOTAL NUMBER OF PEAKS
REMARK 3 IN N15-NOESY = 1536; TOTAL NUMBER OF ASSIGNABLE PEAKS IN N15-
REMARK 3 NOESY = 1239; TOTAL NUMBER OF PEAKS ASSIGNED IN N15-NOESY =
REMARK 3 814; TOTAL NUMBER OF PEAKS IN C13-NOESY = 3115; TOTAL NUMBER
REMARK 3 OF ASSIGNABLE PEAKS IN C13-NOESY = 2494; TOTAL NUMBER OF PEAKS
REMARK 3 ASSIGNED IN C13-NOESY = 1802.
REMARK 4
REMARK 4 1KKG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015048.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.05
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.6 MM RBFA, U-15N,13C; 10 MM
REMARK 210 SODIUM PHOSPHATE, 0.5 MM SODIUM
REMARK 210 AZIDE, 95% H2O, 5% D2O; 1.6 MM
REMARK 210 RBFA, U-15N; 10 MM POTASSIUM
REMARK 210 ACETATE 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; NH_HSQC_JHAHN;
REMARK 210 NH_HSQC_1H/2H_EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AUTOSTRUCTURE 1.0ALPHA, SPARKY
REMARK 210 3.69, VNMR 6.3B, TALOS
REMARK 210 98.040.21.02
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS, AUTOMATED
REMARK 210 ANALYSIS OF NOESY DATA AND 3D
REMARK 210 STRUCTURES.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : BEST TARGET FUNCTION
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, AUTOMATED ANALYSIS OF ASSIGNMENTS AND AUTOMATED
REMARK 210 ANALYSIS OF 3D STRUCTURE.
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 45.71 162.61
REMARK 500 1 ARG A 25 -62.08 -109.04
REMARK 500 1 LYS A 28 73.12 -101.85
REMARK 500 1 SER A 39 33.24 -91.29
REMARK 500 1 LEU A 47 -71.22 -143.89
REMARK 500 1 ALA A 48 61.96 159.67
REMARK 500 1 SER A 76 -74.36 -55.12
REMARK 500 1 ARG A 88 78.51 22.42
REMARK 500 1 LEU A 89 -150.97 -119.25
REMARK 500 1 ARG A 90 -44.69 -148.12
REMARK 500 1 ILE A 91 -36.49 -37.37
REMARK 500 1 VAL A 92 60.12 23.75
REMARK 500 1 GLU A 94 66.47 -67.26
REMARK 500 1 GLU A 105 -38.33 -150.13
REMARK 500 2 ALA A 2 -130.70 -150.83
REMARK 500 2 ARG A 7 177.54 -57.12
REMARK 500 2 GLN A 13 -70.34 -64.79
REMARK 500 2 GLU A 14 -37.38 -38.73
REMARK 500 2 LYS A 28 72.01 -102.68
REMARK 500 2 LEU A 47 -63.45 -148.26
REMARK 500 2 ALA A 48 70.72 163.03
REMARK 500 2 SER A 76 -72.73 -54.57
REMARK 500 2 ARG A 88 79.30 23.06
REMARK 500 2 LEU A 89 -158.08 -120.47
REMARK 500 2 ARG A 90 -42.93 -141.89
REMARK 500 2 ILE A 91 -35.17 -36.98
REMARK 500 2 VAL A 92 59.71 24.14
REMARK 500 2 GLU A 94 66.86 -69.04
REMARK 500 2 GLU A 105 -42.31 -142.63
REMARK 500 2 MET A 107 33.21 -156.11
REMARK 500 3 ALA A 2 167.86 179.43
REMARK 500 3 ARG A 25 -64.13 -107.02
REMARK 500 3 LYS A 28 72.86 -104.42
REMARK 500 3 LEU A 47 -71.70 -143.66
REMARK 500 3 ALA A 48 58.52 159.23
REMARK 500 3 SER A 76 -74.36 -56.65
REMARK 500 3 ARG A 88 77.83 22.34
REMARK 500 3 LEU A 89 -148.68 -116.60
REMARK 500 3 ARG A 90 -43.24 -153.05
REMARK 500 3 ILE A 91 -34.55 -37.48
REMARK 500 3 VAL A 92 60.44 23.42
REMARK 500 3 GLU A 94 64.24 -67.17
REMARK 500 3 LEU A 95 90.54 -69.96
REMARK 500 3 GLU A 105 -39.28 -160.55
REMARK 500 4 LEU A 47 -70.86 -144.06
REMARK 500 4 ALA A 48 63.04 159.80
REMARK 500 4 SER A 76 -75.18 -55.25
REMARK 500 4 ARG A 88 83.41 22.20
REMARK 500 4 LEU A 89 -148.22 -126.58
REMARK 500 4 ARG A 90 -41.57 -155.19
REMARK 500
REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5093 RELATED DB: BMRB
REMARK 900 BMRB 5093 IS THE 1H, 13C, 15N RESONANCE ASSIGNMENTS FOR RBFA
REMARK 900 RELATED ID: WR90EC RELATED DB: TARGETDB
DBREF 1KKG A 1 108 UNP P0A7G2 RBFA_ECOLI 0 107
SEQRES 1 A 108 MET ALA LYS GLU PHE GLY ARG PRO GLN ARG VAL ALA GLN
SEQRES 2 A 108 GLU MET GLN LYS GLU ILE ALA LEU ILE LEU GLN ARG GLU
SEQRES 3 A 108 ILE LYS ASP PRO ARG LEU GLY MET MET THR THR VAL SER
SEQRES 4 A 108 GLY VAL GLU MET SER ARG ASP LEU ALA TYR ALA LYS VAL
SEQRES 5 A 108 TYR VAL THR PHE LEU ASN ASP LYS ASP GLU ASP ALA VAL
SEQRES 6 A 108 LYS ALA GLY ILE LYS ALA LEU GLN GLU ALA SER GLY PHE
SEQRES 7 A 108 ILE ARG SER LEU LEU GLY LYS ALA MET ARG LEU ARG ILE
SEQRES 8 A 108 VAL PRO GLU LEU THR PHE PHE TYR ASP ASN SER LEU VAL
SEQRES 9 A 108 GLU GLY MET ARG
HELIX 1 1 GLN A 9 LEU A 23 1 15
HELIX 2 2 GLU A 62 GLU A 74 5 13
HELIX 3 3 SER A 76 ALA A 86 5 11
SHEET 1 A 3 VAL A 41 SER A 44 0
SHEET 2 A 3 TYR A 49 THR A 55 -1 O TYR A 49 N SER A 44
SHEET 3 A 3 GLU A 94 ASP A 100 1 O PHE A 98 N VAL A 54
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 23 2 Bytes