Header list of 1tdp.pdb file
Complete list - r 2 2 Bytes
HEADER ANTIMICROBIAL PROTEIN 23-MAY-04 1TDP
TITLE NMR SOLUTION STRUCTURE OF THE CARNOBACTERIOCIN B2 IMMUNITY PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARNOBACTERIOCIN B2 IMMUNITY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARNOCIN CP52 IMMUNITY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CARNOBACTERIUM MALTAROMATICUM;
SOURCE 3 ORGANISM_TAXID: 2751;
SOURCE 4 GENE: CBIB2;
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: PMALC
KEYWDS FOUR-HELIX BUNDLE, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR T.SPRULES,K.E.KAWULKA,J.C.VEDERAS
REVDAT 3 02-MAR-22 1TDP 1 REMARK
REVDAT 2 24-FEB-09 1TDP 1 VERSN
REVDAT 1 28-SEP-04 1TDP 0
JRNL AUTH T.SPRULES,K.E.KAWULKA,J.C.VEDERAS
JRNL TITL NMR SOLUTION STRUCTURE OF IMB2, A PROTEIN CONFERRING
JRNL TITL 2 IMMUNITY TO ANTIMICROBIAL ACTIVITY OF THE TYPE IIA
JRNL TITL 3 BACTERIOCIN, CARNOBACTERIOCIN B2
JRNL REF BIOCHEMISTRY V. 43 11740 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15362858
JRNL DOI 10.1021/BI048854+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1
REMARK 3 AUTHORS : BRUNGER, A.T., ADAMS, P.D., CLORE, G.M., DELANO,
REMARK 3 W.L., GROS, P., GROSSE-KUNSTLEVE, R.W., JIANG,
REMARK 3 J.S., KUSZEWSKI, J., NILGES, M., PANNU, N.S., READ,
REMARK 3 R. J., RICE, L.M., SIMONSON, T., AND WARREN, G.L.
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 2118 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS, 84 HYDROGEN BONDS AND 130 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1TDP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022565.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE; 25 MM
REMARK 210 NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM CBIB2 U-15N; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER; 25 MM NACL; 90%
REMARK 210 H2O, 10%D2O; 0.8 MM CBIB2 U-15N,
REMARK 210 13C; 20 MM SODIUM PHOSPHATE
REMARK 210 BUFFER; 25 MM NACL; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, NMRVIEW 5.0, CNS
REMARK 210 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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 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 O ALA A 15 H ASP A 18 1.36
REMARK 500 O ARG A 95 HG13 ILE A 99 1.57
REMARK 500 O ASP A 18 H VAL A 21 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 ASP A 2 -158.56 -79.53
REMARK 500 1 ALA A 40 34.84 -80.77
REMARK 500 1 SER A 43 59.35 -94.72
REMARK 500 1 TYR A 62 -100.19 -58.42
REMARK 500 1 LEU A 63 -124.98 47.47
REMARK 500 1 HIS A 65 70.85 -119.77
REMARK 500 1 ARG A 67 -157.47 -155.64
REMARK 500 1 ILE A 68 -76.96 -104.02
REMARK 500 1 ILE A 69 88.69 114.83
REMARK 500 1 SER A 71 -71.29 11.12
REMARK 500 1 SER A 72 19.21 -63.36
REMARK 500 1 LEU A 74 -33.27 -161.94
REMARK 500 1 SER A 105 22.38 -163.08
REMARK 500 1 VAL A 106 86.91 8.61
REMARK 500 1 TYR A 110 30.60 -98.42
REMARK 500 2 ASP A 2 173.32 -52.60
REMARK 500 2 ALA A 40 40.23 -102.93
REMARK 500 2 SER A 55 47.86 -78.96
REMARK 500 2 ARG A 56 -46.83 171.20
REMARK 500 2 TYR A 62 67.61 176.23
REMARK 500 2 SER A 64 60.77 -109.35
REMARK 500 2 HIS A 65 -70.15 67.36
REMARK 500 2 LYS A 66 31.22 -168.83
REMARK 500 2 PRO A 70 43.99 -84.88
REMARK 500 2 SER A 71 -50.64 67.19
REMARK 500 2 SER A 72 19.36 -63.28
REMARK 500 2 LEU A 74 -32.13 -137.41
REMARK 500 2 PRO A 107 -139.36 -63.02
REMARK 500 2 ILE A 109 108.81 154.26
REMARK 500 3 ASP A 2 -171.06 56.39
REMARK 500 3 ASP A 18 108.50 -56.68
REMARK 500 3 LEU A 63 -77.97 -41.25
REMARK 500 3 SER A 64 52.98 -109.77
REMARK 500 3 ARG A 67 -83.36 171.95
REMARK 500 3 ILE A 68 -176.32 -177.67
REMARK 500 3 SER A 72 18.71 -64.16
REMARK 500 3 PRO A 107 -139.36 -67.16
REMARK 500 3 ILE A 109 93.00 -160.58
REMARK 500 4 ASP A 2 -178.20 58.08
REMARK 500 4 ASN A 24 68.84 -102.28
REMARK 500 4 ALA A 40 31.60 -95.31
REMARK 500 4 SER A 43 73.03 -102.28
REMARK 500 4 ARG A 56 -28.70 142.66
REMARK 500 4 SER A 59 -67.17 178.21
REMARK 500 4 TYR A 62 -43.72 -160.96
REMARK 500 4 LEU A 63 107.41 -49.34
REMARK 500 4 SER A 64 62.09 -104.06
REMARK 500 4 HIS A 65 95.52 66.50
REMARK 500 4 ILE A 68 -123.17 -63.09
REMARK 500 4 ILE A 69 142.57 64.19
REMARK 500
REMARK 500 THIS ENTRY HAS 211 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TDP A 1 111 UNP P38582 CB2I_CARPI 1 111
SEQRES 1 A 111 MET ASP ILE LYS SER GLN THR LEU TYR LEU ASN LEU SER
SEQRES 2 A 111 GLU ALA TYR LYS ASP PRO GLU VAL LYS ALA ASN GLU PHE
SEQRES 3 A 111 LEU SER LYS LEU VAL VAL GLN CYS ALA GLY LYS LEU THR
SEQRES 4 A 111 ALA SER ASN SER GLU ASN SER TYR ILE GLU VAL ILE SER
SEQRES 5 A 111 LEU LEU SER ARG GLY ILE SER SER TYR TYR LEU SER HIS
SEQRES 6 A 111 LYS ARG ILE ILE PRO SER SER MET LEU THR ILE TYR THR
SEQRES 7 A 111 GLN ILE GLN LYS ASP ILE LYS ASN GLY ASN ILE ASP THR
SEQRES 8 A 111 GLU LYS LEU ARG LYS TYR GLU ILE ALA LYS GLY LEU MET
SEQRES 9 A 111 SER VAL PRO TYR ILE TYR PHE
HELIX 1 1 ILE A 3 LYS A 17 1 15
HELIX 2 2 ASP A 18 ALA A 23 1 6
HELIX 3 3 ASN A 24 ALA A 40 1 17
HELIX 4 4 SER A 43 TYR A 61 1 19
HELIX 5 5 PRO A 70 MET A 73 5 4
HELIX 6 6 LEU A 74 ASN A 86 1 13
HELIX 7 7 ASP A 90 ALA A 100 1 11
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