Header list of 1zg2.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-APR-05 1ZG2
TITLE SOLUTION NMR STRUCTURE OF THE UPF0213 PROTEIN BH0048 FROM BACILLUS
TITLE 2 HALODURANS. NORTHEAST STRUCTURAL GENOMICS TARGET BHR2.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL UPF0213 PROTEIN BH0048;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;
SOURCE 3 ORGANISM_TAXID: 86665;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21MGK;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BHR2-21
KEYWDS BHR2, AUTOSTRUCTURE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NESG, STRUCTURAL GENOMICS, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.M.ARAMINI,G.V.T.SWAPNA,R.XIAO,L.MA,R.SHASTRY,M.CIANO,T.B.ACTON,
AUTHOR 2 J.LIU,B.ROST,J.R.CORT,M.A.KENNEDY,G.T.MONTELIONE,NORTHEAST
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 3 02-MAR-22 1ZG2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZG2 1 VERSN
REVDAT 1 21-JUN-05 1ZG2 0
JRNL AUTH J.M.ARAMINI,G.V.T.SWAPNA,R.XIAO,L.MA,R.SHASTRY,M.CIANO,
JRNL AUTH 2 T.B.ACTON,J.LIU,B.ROST,J.R.CORT,M.A.KENNEDY,G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF THE UPF0213 PROTEIN BH0048 FROM
JRNL TITL 2 BACILLUS HALODURANS. NORTHEAST STRUCTURAL GENOMICS TARGET
JRNL TITL 3 BHR2.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5PL6, AUTOSTRUCTURE 2.1.0, XPLOR-NIH
REMARK 3 2.0.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), HUANG, MONTELIONE
REMARK 3 (AUTOSTRUCTURE), CLORE ET AL. (XPLOR-NIH), BRUNGER
REMARK 3 ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 835 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS, 250 DIHEDRAL ANGLE CONSTRAINTS, AND 52 HYDROGEN
REMARK 3 BOND CONSTRAINTS (12.2 CONSTRAINTS PER RESIDUE EXCLUDING TAGS;
REMARK 3 2.9 LONG RANGE CONSTRAINTS PER RESIDUE). STRUCTURE DETERMINATION
REMARK 3 WAS PERFORMED ITERATIVELY USING AUTOSTRUCTURE (XPLOR). THE 10
REMARK 3 LOWEST ENERGY STRUCTURES WERE FURTHER REFINED BY RESTRAINED
REMARK 3 MOLECULAR DYANMICS/ENERGY MINIMIZATION IN EXPLICIT WATER (CNS).
REMARK 3 THE UNSTRUCTURED N- (MAGDP) AND C- (LEHHHHHH) TERMINAL TAGS WERE
REMARK 3 INCLUDED IN ALL CALCULATIONS BUT HAVE BEEN OMITTED FROM THIS
REMARK 3 DEPOSITION.
REMARK 4
REMARK 4 1ZG2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032677.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.67 MM U-13C,15N BHR2, 20MM
REMARK 210 MES, 100MM NACL, 5MM CACL2, 10MM
REMARK 210 DTT, 0.02% NAN3, PH 6.5; 0.67 MM
REMARK 210 U-13C,15N BHR2, 20MM MES, 100MM
REMARK 210 NACL, 5MM CACL2, 10MM DTT, 0.02%
REMARK 210 NAN3, PH 6.5; 0.56 MM U-15N,5%
REMARK 210 13C BHR2, 20MM MES, 100MM NACL,
REMARK 210 5MM CACL2, 10MM DTT, 0.02% NAN3,
REMARK 210 PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; HIGH
REMARK 210 RESOLUTION CH-HSQC; BACKBONE TR
REMARK 210 EXPTS, TOCSYS, HCCH COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 2.3, SPARKY
REMARK 210 3.91, AUTOASSIGN 1.15, PDBSTAT
REMARK 210 3.25, PSVS 1.0, FINDCORE 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR
REMARK 210 SPECTROSCOPY. PARTIAL AUTOMATED BACKBONE ASSIGNMENTS WERE MADE
REMARK 210 USING AUTOASSIGN, AND THE ASSIGNMENTS WERE COMPLETED MANUALLY.
REMARK 210 AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND
REMARK 210 CONSTRAINTS WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE
REMARK 210 CONSTRAINTS WERE DETERMINED USING HYPER AND TALOS. COMPLETENESS
REMARK 210 OF NMR ASSIGNMENTS (EXCLUDING N- AND C-TAGS): BACKBONE, 98%; SIDE
REMARK 210 CHAIN, 86%, AROMATICS, 100%; STEREOSPECIFIC METHYL, 100%.
REMARK 210 FINAL STRUCTURE QUALITY FACTORS (EXCLUDING THE TAGS), WHERE
REMARK 210 ORDERED RESIDUES [S(PHI) + S(PSI) > 1.8] COMPRISE 7-16,19-25,27-38,
REMARK 210 51-85: (A) RMSD (6-30,48-86): BB 1.0; HEAVY ATOM, 1.6. FINDCORE
REMARK 210 RMSD: BB, 0.63; HEAVY ATOM, 0.86. (B) RAMACHANDRAN STATISTICS
REMARK 210 FOR ORDERED RESIDUES: MOST FAVORED, 96.7%, ADDITIONALLY ALLOWED,
REMARK 210 3.3%, GENEROUSLY ALLOWED, 0.0%, DISALLOWED, 0.0%. (C) PROCHECK
REMARK 210 SCORES FOR ORDERED RESIDUES (RAW/Z-): PHI-PSI, 0.02/0.39; ALL, -
REMARK 210 0.10/-0.59. (D) MOLPROBITY CLASH SCORE (RAW/Z-): 24.24/-2.63. (E)
REMARK 210 RPF SCORES FOR GOODNESS OF FIT TO NOESY DATA: F-MEASURE, 0.916;
REMARK 210 RECALL, 0.922; PRECISION, 0.910; DP-SCORE, 0.663.
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 PRO A 5
REMARK 465 LEU A 100
REMARK 465 GLU A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
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 THR A 26 74.76 -152.05
REMARK 500 1 LYS A 39 92.00 -66.60
REMARK 500 1 ARG A 45 118.11 -161.00
REMARK 500 1 ARG A 47 -47.94 -158.61
REMARK 500 1 LYS A 86 119.64 -163.16
REMARK 500 1 LYS A 95 -66.03 -170.73
REMARK 500 1 LEU A 96 -86.76 61.79
REMARK 500 1 SER A 97 12.52 -157.53
REMARK 500 2 ALA A 41 -40.30 73.73
REMARK 500 2 THR A 44 -75.69 -53.06
REMARK 500 2 ARG A 45 -129.39 44.13
REMARK 500 2 ARG A 47 102.61 67.66
REMARK 500 2 GLU A 91 -114.27 -82.59
REMARK 500 2 LYS A 95 28.20 -170.28
REMARK 500 2 LEU A 96 -79.95 63.75
REMARK 500 2 SER A 97 25.57 -174.15
REMARK 500 2 THR A 98 -80.02 64.79
REMARK 500 3 LYS A 39 -97.25 47.89
REMARK 500 3 THR A 44 -163.04 -163.41
REMARK 500 3 ARG A 45 171.15 71.52
REMARK 500 3 GLU A 91 -153.64 56.55
REMARK 500 3 ASN A 92 31.32 71.77
REMARK 500 3 THR A 93 34.77 -83.60
REMARK 500 3 THR A 94 90.70 -65.82
REMARK 500 3 LYS A 95 -44.84 -170.74
REMARK 500 3 LEU A 96 76.52 56.13
REMARK 500 4 ALA A 41 129.86 66.18
REMARK 500 4 TYR A 43 -74.71 70.11
REMARK 500 4 THR A 44 -170.60 50.80
REMARK 500 4 TYR A 90 104.77 -163.18
REMARK 500 4 GLU A 91 142.74 74.27
REMARK 500 4 THR A 94 -96.40 -103.05
REMARK 500 4 LYS A 95 14.80 58.36
REMARK 500 5 ALA A 41 -78.54 -149.45
REMARK 500 5 LYS A 42 71.68 52.93
REMARK 500 5 VAL A 53 -61.10 -91.88
REMARK 500 5 TYR A 90 -32.13 168.33
REMARK 500 5 THR A 93 81.85 56.21
REMARK 500 5 LEU A 96 -4.43 73.57
REMARK 500 6 ASP A 17 -70.52 -74.49
REMARK 500 6 ARG A 45 171.99 69.50
REMARK 500 6 GLU A 91 73.14 -167.06
REMARK 500 6 ASN A 92 -61.03 67.14
REMARK 500 6 THR A 93 -12.59 61.13
REMARK 500 6 THR A 94 134.12 73.98
REMARK 500 6 LYS A 95 87.99 74.32
REMARK 500 6 SER A 97 167.22 76.22
REMARK 500 7 THR A 26 57.89 -154.09
REMARK 500 7 LYS A 39 77.48 73.34
REMARK 500 7 ALA A 41 -91.92 61.20
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BHR2 RELATED DB: TARGETDB
DBREF 1ZG2 A 6 99 UNP Q9KGL3 Y048_BACHD 1 94
SEQADV 1ZG2 MET A 1 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 ALA A 2 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 GLY A 3 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 ASP A 4 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 PRO A 5 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 LEU A 100 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 GLU A 101 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 102 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 103 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 104 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 105 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 106 UNP Q9KGL3 CLONING ARTIFACT
SEQADV 1ZG2 HIS A 107 UNP Q9KGL3 CLONING ARTIFACT
SEQRES 1 A 107 MET ALA GLY ASP PRO MET ASN HIS TYR VAL TYR ILE LEU
SEQRES 2 A 107 GLU CYS LYS ASP GLY SER TRP TYR THR GLY TYR THR THR
SEQRES 3 A 107 ASP VAL ASP ARG ARG ILE LYS LYS HIS ALA SER GLY LYS
SEQRES 4 A 107 GLY ALA LYS TYR THR ARG GLY ARG GLY PRO PHE ARG LEU
SEQRES 5 A 107 VAL ALA THR TRP ALA PHE PRO SER LYS GLU GLU ALA MET
SEQRES 6 A 107 ARG TRP GLU TYR GLU VAL LYS HIS LEU SER ARG ARG LYS
SEQRES 7 A 107 LYS GLU GLN LEU VAL SER LEU LYS GLY GLY PRO TYR GLU
SEQRES 8 A 107 ASN THR THR LYS LEU SER THR THR LEU GLU HIS HIS HIS
SEQRES 9 A 107 HIS HIS HIS
HELIX 1 1 ASP A 27 LYS A 39 1 13
HELIX 2 2 SER A 60 LEU A 74 1 15
HELIX 3 3 SER A 75 LYS A 86 1 12
HELIX 4 4 GLY A 88 THR A 93 1 6
SHEET 1 A 3 TRP A 20 THR A 25 0
SHEET 2 A 3 HIS A 8 GLU A 14 -1 N LEU A 13 O TYR A 21
SHEET 3 A 3 ARG A 51 PHE A 58 -1 O TRP A 56 N VAL A 10
CISPEP 1 GLY A 48 PRO A 49 1 -2.96
CISPEP 2 GLY A 48 PRO A 49 2 -0.90
CISPEP 3 GLY A 48 PRO A 49 3 -1.67
CISPEP 4 GLY A 48 PRO A 49 4 -0.69
CISPEP 5 GLY A 48 PRO A 49 5 -2.96
CISPEP 6 GLY A 48 PRO A 49 6 -2.04
CISPEP 7 GLY A 48 PRO A 49 7 -4.02
CISPEP 8 GLY A 48 PRO A 49 8 -4.21
CISPEP 9 GLY A 48 PRO A 49 9 -6.89
CISPEP 10 GLY A 48 PRO A 49 10 -1.79
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