Header list of 1xax.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 26-AUG-04 1XAX
TITLE NMR STRUCTURE OF HI0004, A PUTATIVE ESSENTIAL GENE PRODUCT FROM
TITLE 2 HAEMOPHILUS INFLUENZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL UPF0054 PROTEIN HI0004;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HAEMOPHILUS INFLUENZAE, STRUCTURAL GENOMICS, MMP, HYDROLASE, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, S2F, STRUCTURE 2 FUNCTION PROJECT, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.C.YEH,J.F.PARSONS,L.M.PARSONS,F.LIU,E.EISENSTEIN,J.ORBAN,STRUCTURE
AUTHOR 2 2 FUNCTION PROJECT (S2F)
REVDAT 5 02-MAR-22 1XAX 1 REMARK
REVDAT 4 24-FEB-09 1XAX 1 VERSN
REVDAT 3 14-NOV-06 1XAX 1 HEADER KEYWDS AUTHOR
REVDAT 2 01-FEB-05 1XAX 1 JRNL
REVDAT 1 18-JAN-05 1XAX 0
JRNL AUTH D.C.YEH,L.M.PARSONS,J.F.PARSONS,F.LIU,E.EISENSTEIN,J.ORBAN
JRNL TITL NMR STRUCTURE OF HI0004, A PUTATIVE ESSENTIAL GENE PRODUCT
JRNL TITL 2 FROM HAEMOPHILUS INFLUENZAE, AND COMPARISON WITH THE X-RAY
JRNL TITL 3 STRUCTURE OF AN AQUIFEX AEOLICUS HOMOLOG
JRNL REF PROTEIN SCI. V. 14 424 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15632286
JRNL DOI 10.1110/PS.041096705
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.C.YEH,J.F.PARSONS,L.M.PARSONS,F.LIU,E.EISENSTEIN,J.ORBAN
REMARK 1 TITL NMR ASSIGNMENT OF THE HYPOTHETICAL PROTEIN HI0004 FROM
REMARK 1 TITL 2 HAEMOPHILUS INFLUENZAE - A PUTATIVE ESSENTIAL GENE PRODUCT
REMARK 1 REF J.BIOMOL.NMR V. 29 101 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15017148
REMARK 1 DOI 10.1023/B:JNMR.0000019469.77977.72
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : CLORE, M. (CNS), CLORE, M. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XAX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000030152.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N,13C HI0004, 50MM
REMARK 210 PHOSPHATE BUFFER, 10MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNCACB;
REMARK 210 CBCACONH; CCONH; HCCONH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: NH RESIDUAL DIPOLAR COUPLING WERE USED FOR VALIDATION OF
REMARK 210 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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ASP A 147
REMARK 465 ASP A 148
REMARK 465 PRO A 149
REMARK 465 TYR A 150
REMARK 465 LEU A 151
REMARK 465 ALA A 152
REMARK 465 GLU A 153
REMARK 465 LYS A 154
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 LEU A 18 151.62 -49.67
REMARK 500 1 THR A 20 128.48 58.10
REMARK 500 1 ALA A 28 -77.00 -78.56
REMARK 500 1 GLU A 38 111.35 177.46
REMARK 500 1 VAL A 39 164.94 164.13
REMARK 500 1 ASP A 47 169.62 -47.25
REMARK 500 1 ARG A 59 -32.57 -155.05
REMARK 500 1 LYS A 61 -165.74 -62.35
REMARK 500 1 ASP A 62 -150.16 -55.29
REMARK 500 1 PRO A 64 82.06 -38.18
REMARK 500 1 CYS A 74 70.85 -109.39
REMARK 500 1 PRO A 75 -80.56 -60.80
REMARK 500 1 ASP A 76 -79.56 -120.63
REMARK 500 1 VAL A 78 98.23 41.65
REMARK 500 1 GLU A 101 34.37 71.30
REMARK 500 1 LEU A 120 -36.51 -131.89
REMARK 500 1 TYR A 122 16.27 -69.23
REMARK 500 1 ASP A 123 42.71 -85.54
REMARK 500 1 HIS A 124 -176.01 -47.86
REMARK 500 1 ILE A 125 127.09 -10.68
REMARK 500 1 ASP A 128 -63.38 -96.71
REMARK 500 1 ALA A 130 -74.89 -52.21
REMARK 500 2 LEU A 5 77.03 -40.44
REMARK 500 2 ASP A 7 128.17 -173.11
REMARK 500 2 LEU A 18 108.70 -55.87
REMARK 500 2 ALA A 28 -78.09 -77.83
REMARK 500 2 ARG A 59 -32.44 -152.19
REMARK 500 2 LYS A 61 -168.60 -54.77
REMARK 500 2 ASP A 62 -167.89 -53.24
REMARK 500 2 ARG A 63 -157.34 -102.91
REMARK 500 2 PRO A 64 79.22 -58.51
REMARK 500 2 GLU A 73 106.57 -52.30
REMARK 500 2 PRO A 75 -93.70 -67.85
REMARK 500 2 ASP A 76 -83.07 -121.06
REMARK 500 2 LEU A 120 -69.09 -147.22
REMARK 500 2 HIS A 124 -78.82 -50.43
REMARK 500 2 ASP A 128 -60.18 -97.21
REMARK 500 2 ALA A 130 -75.69 -70.81
REMARK 500 3 ALA A 11 33.83 -149.11
REMARK 500 3 GLU A 16 31.34 -97.49
REMARK 500 3 ALA A 28 -77.11 -81.48
REMARK 500 3 ARG A 59 -32.92 -146.60
REMARK 500 3 LYS A 61 -165.99 -73.81
REMARK 500 3 ASP A 62 -170.55 -50.34
REMARK 500 3 PRO A 64 79.45 -43.86
REMARK 500 3 VAL A 67 80.29 -155.44
REMARK 500 3 GLU A 73 89.34 -55.58
REMARK 500 3 CYS A 74 102.83 -56.09
REMARK 500 3 PRO A 75 -155.18 -77.71
REMARK 500 3 ASP A 76 -83.69 -83.00
REMARK 500
REMARK 500 THIS ENTRY HAS 387 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HI0004 RELATED DB: TARGETDB
DBREF 1XAX A 1 154 UNP P71335 Y004_HAEIN 1 154
SEQRES 1 A 154 MET GLY SER VAL LEU VAL ASP LEU GLN ILE ALA THR GLU
SEQRES 2 A 154 ASN ILE GLU GLY LEU PRO THR GLU GLU GLN ILE VAL GLN
SEQRES 3 A 154 TRP ALA THR GLY ALA VAL GLN PRO GLU GLY ASN GLU VAL
SEQRES 4 A 154 GLU MET THR VAL ARG ILE VAL ASP GLU ALA GLU SER HIS
SEQRES 5 A 154 GLU LEU ASN LEU THR TYR ARG GLY LYS ASP ARG PRO THR
SEQRES 6 A 154 ASN VAL LEU SER PHE PRO PHE GLU CYS PRO ASP GLU VAL
SEQRES 7 A 154 GLU LEU PRO LEU LEU GLY ASP LEU VAL ILE CYS ARG GLN
SEQRES 8 A 154 VAL VAL GLU ARG GLU ALA SER GLU GLN GLU LYS PRO LEU
SEQRES 9 A 154 MET ALA HIS TRP ALA HIS MET VAL VAL HIS GLY SER LEU
SEQRES 10 A 154 HIS LEU LEU GLY TYR ASP HIS ILE GLU ASP ASP GLU ALA
SEQRES 11 A 154 GLU GLU MET GLU SER LEU GLU THR GLN ILE MET GLN GLY
SEQRES 12 A 154 LEU GLY PHE ASP ASP PRO TYR LEU ALA GLU LYS
HELIX 1 1 THR A 20 GLN A 33 1 14
HELIX 2 2 ASP A 47 ARG A 59 1 13
HELIX 3 3 CYS A 89 GLU A 101 1 13
HELIX 4 4 PRO A 103 HIS A 118 1 16
HELIX 5 5 ASP A 128 GLN A 142 1 15
SHEET 1 A 4 VAL A 4 ILE A 10 0
SHEET 2 A 4 VAL A 39 ILE A 45 1 O MET A 41 N LEU A 5
SHEET 3 A 4 ASP A 85 ILE A 88 1 O LEU A 86 N ARG A 44
SHEET 4 A 4 VAL A 67 PHE A 70 -1 N PHE A 70 O ASP A 85
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