Header list of 1n5h.pdb file
Complete list - b 23 2 Bytes
HEADER ANTIBIOTIC 06-NOV-02 1N5H
TITLE SOLUTION STRUCTURE OF THE CATHELIN-LIKE DOMAIN OF PROTEGRINS (THE R87-
TITLE 2 P88 AND D118-P119 AMIDE BONDS ARE IN THE CIS CONFORMATION)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEGRINS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATHELIN-LIKE DOMAIN;
COMPND 5 SYNONYM: PROTEGRIN 1, PROTEGRIN 2, PROTEGRIN 3, PROTEGRIN 4,
COMPND 6 PROTEGRIN 5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS CATHELIN-LIKE DOMAIN, CATHELICIDIN, PROLINE ISOMERIZATION, CYSTATIN
KEYWDS 2 FOLD, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR Y.YANG,J.F.SANCHEZ,M.P.STRUB,B.BRUTSCHER,A.AUMELAS
REVDAT 3 23-FEB-22 1N5H 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1N5H 1 VERSN
REVDAT 1 03-JUN-03 1N5H 0
JRNL AUTH Y.YANG,J.F.SANCHEZ,M.P.STRUB,B.BRUTSCHER,A.AUMELAS
JRNL TITL NMR STRUCTURE OF THE CATHELIN-LIKE DOMAIN OF THE PROTEGRIN-3
JRNL TITL 2 PRECURSOR
JRNL REF BIOCHEMISTRY V. 42 4669 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12705830
JRNL DOI 10.1021/BI027133C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4.4, X-PLOR 3.8
REMARK 3 AUTHORS : DELSUC, M.A. (GIFA), RICE, L.M., BRUNGER, A.T. (X
REMARK 3 -PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N5H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017542.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5-2MM; U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER; PH 6.2; 1.5-
REMARK 210 2MM; U-15N, 13C; 50MM PHOSPHATE
REMARK 210 BUFFER; PH 6.2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HNCO, CBCA(CO)NH, 3D_15N
REMARK 210 -SEPARATED_NOESY; HC(C)H-TOCSY,
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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
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 HIS A 28 79.25 -110.37
REMARK 500 1 GLN A 30 72.49 52.20
REMARK 500 1 LYS A 65 70.83 57.31
REMARK 500 1 GLN A 115 64.52 -102.94
REMARK 500 2 SER A 27 58.57 -119.21
REMARK 500 2 HIS A 28 -65.33 -163.06
REMARK 500 2 LEU A 32 171.04 61.75
REMARK 500 2 TYR A 34 -58.40 68.04
REMARK 500 2 ASP A 97 -169.81 -76.68
REMARK 500 2 ASP A 121 81.49 -69.33
REMARK 500 2 GLU A 126 80.29 14.58
REMARK 500 2 GLN A 128 71.36 -104.13
REMARK 500 3 GLN A 30 176.74 62.92
REMARK 500 3 TYR A 34 -57.13 67.97
REMARK 500 3 GLU A 68 67.04 -159.34
REMARK 500 3 ASP A 69 96.91 -179.27
REMARK 500 3 PRO A 70 -81.00 -74.13
REMARK 500 4 LEU A 32 132.91 67.14
REMARK 500 4 ALA A 52 48.17 -100.53
REMARK 500 4 LYS A 65 82.18 53.42
REMARK 500 4 ASP A 67 45.25 -97.38
REMARK 500 4 GLU A 68 -165.27 179.71
REMARK 500 4 ASP A 69 75.47 56.04
REMARK 500 4 PRO A 86 -163.45 -77.39
REMARK 500 4 ASP A 114 -64.57 -99.07
REMARK 500 4 GLN A 128 141.42 67.87
REMARK 500 5 SER A 50 -86.78 -121.61
REMARK 500 5 GLU A 51 -179.82 58.01
REMARK 500 5 GLU A 68 27.47 -151.30
REMARK 500 5 PRO A 70 -80.88 -74.60
REMARK 500 5 ILE A 116 97.96 -66.75
REMARK 500 5 ASP A 121 83.20 -66.87
REMARK 500 5 GLN A 128 -176.40 60.27
REMARK 500 6 MET A 29 -178.89 61.19
REMARK 500 6 GLU A 68 26.97 -145.10
REMARK 500 6 PRO A 70 -74.24 -71.31
REMARK 500 6 GLN A 115 116.60 -165.03
REMARK 500 6 GLU A 126 76.16 42.33
REMARK 500 7 GLN A 30 167.23 65.11
REMARK 500 7 LEU A 32 81.90 -151.92
REMARK 500 7 LYS A 65 70.47 52.04
REMARK 500 7 ASP A 69 87.07 57.70
REMARK 500 7 PRO A 75 90.22 -69.19
REMARK 500 7 VAL A 84 46.11 -85.67
REMARK 500 7 ASP A 97 -164.06 -102.10
REMARK 500 7 ILE A 116 99.00 -65.51
REMARK 500 7 ASN A 125 48.50 -143.67
REMARK 500 7 GLU A 126 92.87 32.06
REMARK 500 8 LEU A 32 142.27 66.39
REMARK 500 8 ASP A 67 44.55 -142.61
REMARK 500
REMARK 500 THIS ENTRY HAS 105 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 35 0.29 SIDE CHAIN
REMARK 500 1 ARG A 40 0.27 SIDE CHAIN
REMARK 500 1 ARG A 44 0.31 SIDE CHAIN
REMARK 500 1 ARG A 56 0.32 SIDE CHAIN
REMARK 500 1 ARG A 87 0.25 SIDE CHAIN
REMARK 500 1 ARG A 90 0.32 SIDE CHAIN
REMARK 500 1 ARG A 103 0.31 SIDE CHAIN
REMARK 500 2 ARG A 35 0.31 SIDE CHAIN
REMARK 500 2 ARG A 40 0.32 SIDE CHAIN
REMARK 500 2 ARG A 44 0.31 SIDE CHAIN
REMARK 500 2 ARG A 56 0.26 SIDE CHAIN
REMARK 500 2 ARG A 87 0.32 SIDE CHAIN
REMARK 500 2 ARG A 90 0.32 SIDE CHAIN
REMARK 500 2 ARG A 103 0.32 SIDE CHAIN
REMARK 500 3 ARG A 35 0.31 SIDE CHAIN
REMARK 500 3 ARG A 40 0.32 SIDE CHAIN
REMARK 500 3 ARG A 44 0.31 SIDE CHAIN
REMARK 500 3 ARG A 56 0.31 SIDE CHAIN
REMARK 500 3 ARG A 87 0.32 SIDE CHAIN
REMARK 500 3 ARG A 90 0.32 SIDE CHAIN
REMARK 500 3 ARG A 103 0.32 SIDE CHAIN
REMARK 500 4 ARG A 35 0.31 SIDE CHAIN
REMARK 500 4 ARG A 40 0.28 SIDE CHAIN
REMARK 500 4 ARG A 44 0.32 SIDE CHAIN
REMARK 500 4 ARG A 56 0.27 SIDE CHAIN
REMARK 500 4 ARG A 87 0.25 SIDE CHAIN
REMARK 500 4 ARG A 90 0.32 SIDE CHAIN
REMARK 500 4 ARG A 103 0.31 SIDE CHAIN
REMARK 500 5 ARG A 35 0.32 SIDE CHAIN
REMARK 500 5 ARG A 40 0.29 SIDE CHAIN
REMARK 500 5 ARG A 44 0.29 SIDE CHAIN
REMARK 500 5 ARG A 56 0.26 SIDE CHAIN
REMARK 500 5 ARG A 87 0.18 SIDE CHAIN
REMARK 500 5 ARG A 90 0.28 SIDE CHAIN
REMARK 500 5 ARG A 103 0.31 SIDE CHAIN
REMARK 500 6 ARG A 35 0.32 SIDE CHAIN
REMARK 500 6 ARG A 40 0.31 SIDE CHAIN
REMARK 500 6 ARG A 44 0.24 SIDE CHAIN
REMARK 500 6 ARG A 56 0.31 SIDE CHAIN
REMARK 500 6 ARG A 87 0.11 SIDE CHAIN
REMARK 500 6 ARG A 90 0.32 SIDE CHAIN
REMARK 500 6 ARG A 103 0.31 SIDE CHAIN
REMARK 500 7 ARG A 35 0.32 SIDE CHAIN
REMARK 500 7 ARG A 40 0.28 SIDE CHAIN
REMARK 500 7 ARG A 44 0.30 SIDE CHAIN
REMARK 500 7 ARG A 56 0.21 SIDE CHAIN
REMARK 500 7 ARG A 87 0.30 SIDE CHAIN
REMARK 500 7 ARG A 90 0.30 SIDE CHAIN
REMARK 500 7 ARG A 103 0.29 SIDE CHAIN
REMARK 500 8 ARG A 35 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 104 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N5P RELATED DB: PDB
REMARK 900 STRUCTURE WITH ALL AMIDE BONDS INVOLVING PROLINE RESIDUES IN TRANS
REMARK 900 CONFORMATION
DBREF 1N5H A 30 130 UNP P49933 PG4_PIG 30 130
SEQADV 1N5H GLY A 26 UNP P49933 CLONING ARTIFACT
SEQADV 1N5H SER A 27 UNP P49933 CLONING ARTIFACT
SEQADV 1N5H HIS A 28 UNP P49933 CLONING ARTIFACT
SEQADV 1N5H MET A 29 UNP P49933 CLONING ARTIFACT
SEQRES 1 A 105 GLY SER HIS MET GLN ALA LEU SER TYR ARG GLU ALA VAL
SEQRES 2 A 105 LEU ARG ALA VAL ASP ARG LEU ASN GLU GLN SER SER GLU
SEQRES 3 A 105 ALA ASN LEU TYR ARG LEU LEU GLU LEU ASP GLN PRO PRO
SEQRES 4 A 105 LYS ALA ASP GLU ASP PRO GLY THR PRO LYS PRO VAL SER
SEQRES 5 A 105 PHE THR VAL LYS GLU THR VAL CYS PRO ARG PRO THR ARG
SEQRES 6 A 105 GLN PRO PRO GLU LEU CYS ASP PHE LYS GLU ASN GLY ARG
SEQRES 7 A 105 VAL LYS GLN CYS VAL GLY THR VAL THR LEU ASP GLN ILE
SEQRES 8 A 105 LYS ASP PRO LEU ASP ILE THR CYS ASN GLU VAL GLN GLY
SEQRES 9 A 105 VAL
HELIX 1 1 SER A 33 SER A 49 1 17
SHEET 1 A 4 ASN A 53 LEU A 60 0
SHEET 2 A 4 LYS A 74 PRO A 86 -1 O THR A 79 N GLU A 59
SHEET 3 A 4 VAL A 104 VAL A 111 -1 O GLY A 109 N VAL A 76
SHEET 4 A 4 ILE A 122 VAL A 127 -1 O THR A 123 N VAL A 108
SSBOND 1 CYS A 85 CYS A 96 1555 1555 2.02
SSBOND 2 CYS A 107 CYS A 124 1555 1555 2.02
CISPEP 1 ARG A 87 PRO A 88 1 -1.15
CISPEP 2 ASP A 118 PRO A 119 1 -0.07
CISPEP 3 ARG A 87 PRO A 88 2 -1.22
CISPEP 4 ASP A 118 PRO A 119 2 0.02
CISPEP 5 ARG A 87 PRO A 88 3 -0.49
CISPEP 6 ASP A 118 PRO A 119 3 0.02
CISPEP 7 ARG A 87 PRO A 88 4 -0.01
CISPEP 8 ASP A 118 PRO A 119 4 0.16
CISPEP 9 ARG A 87 PRO A 88 5 -0.90
CISPEP 10 ASP A 118 PRO A 119 5 0.18
CISPEP 11 ARG A 87 PRO A 88 6 -0.56
CISPEP 12 ASP A 118 PRO A 119 6 -0.20
CISPEP 13 ARG A 87 PRO A 88 7 -0.63
CISPEP 14 ASP A 118 PRO A 119 7 -0.14
CISPEP 15 ARG A 87 PRO A 88 8 -0.84
CISPEP 16 ASP A 118 PRO A 119 8 -0.23
CISPEP 17 ARG A 87 PRO A 88 9 -1.15
CISPEP 18 ASP A 118 PRO A 119 9 0.13
CISPEP 19 ARG A 87 PRO A 88 10 -1.02
CISPEP 20 ASP A 118 PRO A 119 10 -0.35
CISPEP 21 ARG A 87 PRO A 88 11 -0.72
CISPEP 22 ASP A 118 PRO A 119 11 -0.04
CISPEP 23 ARG A 87 PRO A 88 12 -0.25
CISPEP 24 ASP A 118 PRO A 119 12 -0.07
CISPEP 25 ARG A 87 PRO A 88 13 -0.77
CISPEP 26 ASP A 118 PRO A 119 13 0.07
CISPEP 27 ARG A 87 PRO A 88 14 -0.53
CISPEP 28 ASP A 118 PRO A 119 14 -0.44
CISPEP 29 ARG A 87 PRO A 88 15 -0.72
CISPEP 30 ASP A 118 PRO A 119 15 0.20
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 - b 23 2 Bytes