Header list of 2akl.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 03-AUG-05 2AKL
TITLE SOLUTION STRUCTURE FOR PHN-A LIKE PROTEIN PA0128 FROM PSEUDOMONAS
TITLE 2 AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHNA-LIKE PROTEIN PA0128;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYPOTHETICAL PROTEIN PA0128;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TWO DOMAINS; ZN BINDING PROTEIN; BETA-STRAND PROTEIN, STRUCTURAL
KEYWDS 2 GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM; NESG; ONTARIO CENTRE FOR STRUCTURAL PROTEOMICS;
KEYWDS 4 OCSP, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SRISAILAM,A.YEE,A.LEMAK,J.A.LUKIN,S.BANSAL,J.H.PRESTEGARD,
AUTHOR 2 C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG),
AUTHOR 3 ONTARIO CENTRE FOR STRUCTURAL PROTEOMICS (OCSP)
REVDAT 5 09-MAR-22 2AKL 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 2AKL 1 VERSN
REVDAT 3 10-APR-07 2AKL 1 JRNL
REVDAT 2 19-SEP-06 2AKL 1 JRNL
REVDAT 1 18-JUL-06 2AKL 0
JRNL AUTH S.SRISAILAM,J.A.LUKIN,A.LEMAK,A.YEE,C.H.ARROWSMITH
JRNL TITL SEQUENCE SPECIFIC RESONANCE ASSIGNMENT OF A HYPOTHETICAL
JRNL TITL 2 PROTEIN PA0128 FROM PSEUDOMONAS AERUGINOSA
JRNL REF J.BIOMOL.NMR V. 36 27 2006
JRNL REFN ISSN 0925-2738
JRNL PMID 16703420
JRNL DOI 10.1007/S10858-006-0011-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER, A. T. ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2448 NOE DERIVED DISTANCE RESTRAINTS,
REMARK 3 132 TORSION ANGLE RESTRAINTS, 62 RDC RESTRAINTS
REMARK 4
REMARK 4 2AKL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034004.
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 : 400 MM NACL, 20 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PA0128, U-15N,13C: 400 MM
REMARK 210 NACL, 20 MM NA2PO4, 1 MM
REMARK 210 BENZAMIDINE, 15 MM DTT, 20 UM
REMARK 210 ZNSO4, 0.01% NAN3, 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; J MODULATED
REMARK 210 HSQC FOR RDC
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 : SPARKY 3.106, CYANA 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
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 PRO A 7 -169.69 -65.78
REMARK 500 1 PRO A 9 11.31 -68.19
REMARK 500 1 GLU A 14 5.76 84.85
REMARK 500 1 TYR A 15 47.32 -82.70
REMARK 500 1 ASP A 19 74.76 -110.04
REMARK 500 1 THR A 39 150.21 70.41
REMARK 500 1 ASP A 57 94.96 -69.13
REMARK 500 1 VAL A 78 97.27 -50.04
REMARK 500 1 HIS A 92 51.56 -100.64
REMARK 500 1 ASP A 93 102.15 -161.53
REMARK 500 2 PRO A 7 -167.51 -73.06
REMARK 500 2 PRO A 9 7.76 -68.44
REMARK 500 2 SER A 13 -77.40 -57.88
REMARK 500 2 GLU A 14 -21.07 171.15
REMARK 500 2 TYR A 15 36.99 -78.87
REMARK 500 2 THR A 39 -67.55 69.54
REMARK 500 2 ASP A 42 153.51 68.65
REMARK 500 2 LEU A 55 -157.89 -95.79
REMARK 500 2 VAL A 78 96.54 -51.98
REMARK 500 2 ILE A 85 -178.72 -67.58
REMARK 500 2 HIS A 92 54.17 -106.91
REMARK 500 3 PRO A 7 -167.03 -71.28
REMARK 500 3 SER A 13 -77.93 -59.50
REMARK 500 3 GLU A 14 -15.59 176.91
REMARK 500 3 TYR A 15 32.74 -81.81
REMARK 500 3 ASP A 43 -78.17 -156.94
REMARK 500 3 VAL A 78 96.99 -49.92
REMARK 500 3 ILE A 85 -175.53 -66.58
REMARK 500 3 HIS A 92 52.16 -108.33
REMARK 500 4 THR A 4 33.04 -83.54
REMARK 500 4 PRO A 7 -163.93 -73.50
REMARK 500 4 SER A 13 -78.39 -48.47
REMARK 500 4 GLU A 14 -27.83 169.86
REMARK 500 4 GLU A 27 -73.46 -69.36
REMARK 500 4 LYS A 70 -88.84 -43.14
REMARK 500 4 VAL A 78 97.48 -52.12
REMARK 500 4 ASN A 84 42.38 71.95
REMARK 500 4 ILE A 85 -177.42 -67.27
REMARK 500 4 HIS A 92 45.98 -84.34
REMARK 500 5 PRO A 7 -169.43 -64.57
REMARK 500 5 PRO A 9 7.25 -69.11
REMARK 500 5 ASN A 12 -3.30 70.44
REMARK 500 5 SER A 13 -77.68 -55.34
REMARK 500 5 GLU A 14 -7.24 164.31
REMARK 500 5 TYR A 15 41.56 -80.64
REMARK 500 5 ASP A 19 79.07 -115.75
REMARK 500 5 THR A 39 -85.17 67.40
REMARK 500 5 ALA A 40 50.72 175.10
REMARK 500 5 SER A 41 88.54 -69.03
REMARK 500 5 ASP A 42 177.99 68.11
REMARK 500
REMARK 500 THIS ENTRY HAS 205 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 117 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 CYS A 11 SG 110.4
REMARK 620 3 CYS A 25 SG 107.5 112.1
REMARK 620 4 CYS A 28 SG 111.2 107.9 107.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 117
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PAT1 RELATED DB: TARGETDB
DBREF 2AKL A 3 114 UNP Q9I704 Q9I704_PSEAE 2 113
SEQADV 2AKL MET A -21 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL GLY A -20 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL SER A -19 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL SER A -18 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -17 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -16 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -15 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -14 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -13 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A -12 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL SER A -11 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL SER A -10 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL GLY A -9 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL ARG A -8 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL GLU A -7 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL ASN A -6 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL LEU A -5 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL TYR A -4 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL PHE A -3 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL GLN A -2 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL GLY A -1 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL HIS A 0 UNP Q9I704 EXPRESSION TAG
SEQADV 2AKL MET A 1 UNP Q9I704 CLONING ARTIFACT
SEQADV 2AKL VAL A 2 UNP Q9I704 CLONING ARTIFACT
SEQADV 2AKL GLY A 115 UNP Q9I704 CLONING ARTIFACT
SEQADV 2AKL SER A 116 UNP Q9I704 CLONING ARTIFACT
SEQRES 1 A 138 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 138 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET VAL SER THR
SEQRES 3 A 138 LEU PRO PRO CYS PRO GLN CYS ASN SER GLU TYR THR TYR
SEQRES 4 A 138 GLU ASP GLY ALA LEU LEU VAL CYS PRO GLU CYS ALA HIS
SEQRES 5 A 138 GLU TRP SER PRO ASN GLU ALA ALA THR ALA SER ASP ASP
SEQRES 6 A 138 GLY LYS VAL ILE LYS ASP SER VAL GLY ASN VAL LEU GLN
SEQRES 7 A 138 ASP GLY ASP THR ILE THR VAL ILE LYS ASP LEU LYS VAL
SEQRES 8 A 138 LYS GLY SER SER LEU VAL VAL LYS VAL GLY THR LYS VAL
SEQRES 9 A 138 LYS ASN ILE ARG LEU VAL ASP GLY ASP HIS ASP ILE ASP
SEQRES 10 A 138 CYS LYS ILE ASP GLY ILE GLY ALA MET LYS LEU LYS SER
SEQRES 11 A 138 GLU PHE VAL ARG LYS VAL GLY SER
HET ZN A 117 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 LYS A 107 VAL A 111 5 5
SHEET 1 A 3 TYR A 17 GLU A 18 0
SHEET 2 A 3 LEU A 23 CYS A 25 -1 O VAL A 24 N TYR A 17
SHEET 3 A 3 HIS A 30 TRP A 32 -1 O TRP A 32 N LEU A 23
SHEET 1 B 2 THR A 60 THR A 62 0
SHEET 2 B 2 LYS A 81 LYS A 83 -1 O VAL A 82 N ILE A 61
SHEET 1 C 2 LEU A 67 LYS A 68 0
SHEET 2 C 2 VAL A 75 VAL A 76 -1 O VAL A 76 N LEU A 67
SHEET 1 D 3 ARG A 86 LEU A 87 0
SHEET 2 D 3 ILE A 94 ILE A 98 -1 O ASP A 95 N ARG A 86
SHEET 3 D 3 GLY A 102 LEU A 106 -1 O GLY A 102 N ILE A 98
LINK SG CYS A 8 ZN ZN A 117 1555 1555 2.33
LINK SG CYS A 11 ZN ZN A 117 1555 1555 2.33
LINK SG CYS A 25 ZN ZN A 117 1555 1555 2.32
LINK SG CYS A 28 ZN ZN A 117 1555 1555 2.32
SITE 1 AC1 4 CYS A 8 CYS A 11 CYS A 25 CYS A 28
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 9 2 Bytes