Header list of 2h3k.pdb file
Complete list - g 9 2 Bytes
HEADER PROTEIN BINDING 22-MAY-06 2H3K TITLE SOLUTION STRUCTURE OF THE FIRST NEAT DOMAIN OF ISDH COMPND MOL_ID: 1; COMPND 2 MOLECULE: HAPTOGLOBIN-BINDING SURFACE ANCHORED PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FIRST NEAT DOMAIN, ISDH-N1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS; SOURCE 3 ORGANISM_TAXID: 282459; SOURCE 4 STRAIN: MSSA476; SOURCE 5 GENE: SA1552; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS NEAT DOMAIN, ISDH, HARA, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR R.M.PILPA,E.A.FADEEV,V.A.VILLAREAL,M.A.WONG,M.PHILLIPS,R.T.CLUBB REVDAT 5 14-JUN-23 2H3K 1 REMARK REVDAT 4 19-FEB-20 2H3K 1 REMARK REVDAT 3 13-JUL-11 2H3K 1 VERSN REVDAT 2 24-FEB-09 2H3K 1 VERSN REVDAT 1 22-AUG-06 2H3K 0 JRNL AUTH R.M.PILPA,E.A.FADEEV,V.A.VILLAREAL,M.L.WONG,M.PHILLIPS, JRNL AUTH 2 R.T.CLUBB JRNL TITL SOLUTION STRUCTURE OF THE NEAT (NEAR TRANSPORTER) DOMAIN JRNL TITL 2 FROM ISDH/HARA: THE HUMAN HEMOGLOBIN RECEPTOR IN JRNL TITL 3 STAPHYLOCOCCUS AUREUS. JRNL REF J.MOL.BIOL. V. 360 435 2006 JRNL REFN ISSN 0022-2836 JRNL PMID 16762363 JRNL DOI 10.1016/J.JMB.2006.05.019 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 4.3.5 REMARK 3 AUTHORS : DELAGLIO REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1841 EXPERIMENTALLY DERIVED RESTRAINTS REMARK 3 (1741 NOE-DERIVED DISTANCE CONSTRAINTS, 64 DIHEDRAL ANGLE REMARK 3 RESTRAINTS, 40 HYDROGEN BOND RESTRAINTS) REMARK 4 REMARK 4 2H3K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-06. REMARK 100 THE DEPOSITION ID IS D_1000037885. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : UNIFORM LABELING WITH 15N AT 1MM REMARK 210 IN 50MM SODIUM PHOSPHATE PH 6.0 REMARK 210 AND 100MM NACL; UNIFORM LABELING REMARK 210 WITH 13C/15N AT 1MM IN 50MM REMARK 210 SODIUM PHOSPHATE PH 6.0 AND REMARK 210 100MM NACL WITH 7% D2O; UNIFORM REMARK 210 LABELING WITH 13C/15N AT 1MM IN REMARK 210 50MM SODIUM PHOSPHATE PH 6.0 AND REMARK 210 100MM NACL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.2, XWINNMR 3.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST 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 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 H VAL A 27 O ALA A 50 1.59 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 GLU A 3 -149.47 -135.17 REMARK 500 1 ASN A 16 57.23 -160.33 REMARK 500 1 ASP A 20 70.36 -162.19 REMARK 500 1 ARG A 24 149.84 -178.61 REMARK 500 1 ASP A 33 70.43 -113.84 REMARK 500 1 LYS A 34 24.97 49.75 REMARK 500 1 ASN A 35 21.64 -153.55 REMARK 500 1 ASN A 36 26.22 49.58 REMARK 500 1 SER A 45 -78.92 -100.20 REMARK 500 1 LYS A 47 -63.93 -136.15 REMARK 500 1 THR A 55 -164.93 -102.43 REMARK 500 1 LYS A 57 -70.67 -88.59 REMARK 500 1 PHE A 74 118.96 -175.98 REMARK 500 1 ASN A 79 -71.11 66.69 REMARK 500 1 ASN A 80 37.46 -172.57 REMARK 500 1 ASP A 96 84.89 46.59 REMARK 500 1 HIS A 97 117.81 -162.61 REMARK 500 1 THR A 108 122.52 -36.53 REMARK 500 1 GLU A 123 -154.60 -101.48 REMARK 500 1 PHE A 134 162.02 -47.96 REMARK 500 2 GLU A 3 -149.58 -115.66 REMARK 500 2 ASN A 16 47.61 -161.52 REMARK 500 2 ASP A 33 -150.38 -75.42 REMARK 500 2 ASN A 35 20.52 -143.41 REMARK 500 2 THR A 38 108.06 -55.83 REMARK 500 2 TYR A 41 87.58 -65.68 REMARK 500 2 HIS A 42 -161.85 -111.10 REMARK 500 2 PHE A 43 -165.41 -118.44 REMARK 500 2 SER A 45 -80.91 -177.35 REMARK 500 2 LYS A 47 -50.68 -148.17 REMARK 500 2 LYS A 57 -77.28 -102.12 REMARK 500 2 THR A 67 62.96 -103.52 REMARK 500 2 PHE A 74 127.39 -176.73 REMARK 500 2 GLU A 75 92.51 -165.71 REMARK 500 2 GLN A 81 103.56 -175.53 REMARK 500 2 ASP A 96 84.96 45.53 REMARK 500 2 HIS A 97 113.50 -162.12 REMARK 500 2 ARG A 101 143.19 -173.73 REMARK 500 2 THR A 108 128.58 -36.40 REMARK 500 2 TYR A 129 114.61 -161.63 REMARK 500 2 ASN A 140 153.13 -49.59 REMARK 500 3 GLU A 3 -150.55 -131.22 REMARK 500 3 ASN A 16 93.75 63.75 REMARK 500 3 HIS A 19 41.44 -91.63 REMARK 500 3 ILE A 21 76.21 -117.19 REMARK 500 3 ASP A 33 -146.48 -73.18 REMARK 500 3 ASN A 35 25.06 -152.07 REMARK 500 3 SER A 45 -75.45 -177.34 REMARK 500 3 LYS A 47 -47.42 -154.25 REMARK 500 3 THR A 55 -162.67 -118.28 REMARK 500 REMARK 500 THIS ENTRY HAS 406 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 24 0.32 SIDE CHAIN REMARK 500 1 ARG A 86 0.31 SIDE CHAIN REMARK 500 1 ARG A 101 0.28 SIDE CHAIN REMARK 500 2 ARG A 24 0.29 SIDE CHAIN REMARK 500 2 ARG A 86 0.28 SIDE CHAIN REMARK 500 2 ARG A 101 0.18 SIDE CHAIN REMARK 500 3 ARG A 24 0.31 SIDE CHAIN REMARK 500 3 ARG A 86 0.25 SIDE CHAIN REMARK 500 3 ARG A 101 0.24 SIDE CHAIN REMARK 500 4 ARG A 24 0.29 SIDE CHAIN REMARK 500 4 ARG A 86 0.16 SIDE CHAIN REMARK 500 4 ARG A 101 0.32 SIDE CHAIN REMARK 500 5 ARG A 24 0.32 SIDE CHAIN REMARK 500 5 ARG A 86 0.18 SIDE CHAIN REMARK 500 5 ARG A 101 0.23 SIDE CHAIN REMARK 500 6 ARG A 24 0.28 SIDE CHAIN REMARK 500 6 ARG A 86 0.29 SIDE CHAIN REMARK 500 6 ARG A 101 0.14 SIDE CHAIN REMARK 500 7 ARG A 24 0.28 SIDE CHAIN REMARK 500 7 ARG A 86 0.32 SIDE CHAIN REMARK 500 7 ARG A 101 0.26 SIDE CHAIN REMARK 500 8 ARG A 24 0.14 SIDE CHAIN REMARK 500 8 ARG A 86 0.21 SIDE CHAIN REMARK 500 8 ARG A 101 0.17 SIDE CHAIN REMARK 500 9 ARG A 24 0.27 SIDE CHAIN REMARK 500 9 ARG A 86 0.21 SIDE CHAIN REMARK 500 9 ARG A 101 0.24 SIDE CHAIN REMARK 500 10 ARG A 24 0.30 SIDE CHAIN REMARK 500 10 ARG A 86 0.31 SIDE CHAIN REMARK 500 10 ARG A 101 0.29 SIDE CHAIN REMARK 500 11 ARG A 24 0.28 SIDE CHAIN REMARK 500 11 ARG A 86 0.24 SIDE CHAIN REMARK 500 11 ARG A 101 0.30 SIDE CHAIN REMARK 500 12 ARG A 24 0.30 SIDE CHAIN REMARK 500 12 ARG A 86 0.27 SIDE CHAIN REMARK 500 12 ARG A 101 0.26 SIDE CHAIN REMARK 500 13 ARG A 24 0.32 SIDE CHAIN REMARK 500 13 ARG A 86 0.32 SIDE CHAIN REMARK 500 13 ARG A 101 0.23 SIDE CHAIN REMARK 500 14 ARG A 24 0.32 SIDE CHAIN REMARK 500 14 ARG A 86 0.31 SIDE CHAIN REMARK 500 14 ARG A 101 0.25 SIDE CHAIN REMARK 500 15 ARG A 24 0.31 SIDE CHAIN REMARK 500 15 ARG A 86 0.23 SIDE CHAIN REMARK 500 15 ARG A 101 0.14 SIDE CHAIN REMARK 500 16 ARG A 24 0.30 SIDE CHAIN REMARK 500 16 ARG A 86 0.31 SIDE CHAIN REMARK 500 16 ARG A 101 0.21 SIDE CHAIN REMARK 500 17 ARG A 24 0.23 SIDE CHAIN REMARK 500 17 ARG A 86 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6759 RELATED DB: BMRB DBREF 2H3K A 1 144 UNP Q6G8J7 Q6G8J7_STAAS 86 229 SEQRES 1 A 144 ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP PRO ALA SEQRES 2 A 144 LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG GLU GLN SEQRES 3 A 144 VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU THR GLN SEQRES 4 A 144 TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA ASP VAL SEQRES 5 A 144 TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU ASP ILE SEQRES 6 A 144 ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL TYR GLU SEQRES 7 A 144 ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER TYR SER SEQRES 8 A 144 PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE PRO VAL SEQRES 9 A 144 SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER SER THR SEQRES 10 A 144 GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP TYR THR SEQRES 11 A 144 LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP PRO SER SEQRES 12 A 144 LEU HELIX 1 1 SER A 4 ILE A 9 1 6 HELIX 2 2 THR A 67 TRP A 71 5 5 SHEET 1 A 5 GLN A 26 VAL A 27 0 SHEET 2 A 5 ALA A 50 VAL A 52 -1 O ALA A 50 N VAL A 27 SHEET 3 A 5 GLU A 60 ILE A 65 -1 O GLU A 62 N ASP A 51 SHEET 4 A 5 HIS A 97 PRO A 103 -1 O ALA A 98 N ILE A 65 SHEET 5 A 5 ARG A 86 SER A 91 -1 N SER A 89 O TYR A 99 SHEET 1 B 3 PHE A 29 LEU A 32 0 SHEET 2 B 3 THR A 125 PHE A 134 -1 O VAL A 133 N GLN A 30 SHEET 3 B 3 GLU A 110 THR A 117 -1 N SER A 115 O TYR A 127 SHEET 1 C 2 VAL A 76 GLU A 78 0 SHEET 2 C 2 GLN A 81 LEU A 83 -1 O LEU A 83 N VAL A 76 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