Header list of 1dum.pdb file
Complete list - 3 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 18-JAN-00 1DUM
TITLE NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAGAININ 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS PREPARED BY SOLID-PHASE SYNTHESIS.
SOURCE 4 THE SEQUENCE OF THIS PEPTIDE NATURALLY OCCURS IN XENOPUS LAEVIS
SOURCE 5 (AFRICAN CLAWED FROG)
KEYWDS ANTIBIOTIC, MAGAININ, DIMER, AMPHIPATHIC HELIX, MEMBRANE, VESICLE,
KEYWDS 2 BILAYER, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.TAKEDA,K.WAKAMATSU,T.TACHI,K.MATSUZAKI
REVDAT 4 03-NOV-21 1DUM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1DUM 1 VERSN
REVDAT 2 01-APR-03 1DUM 1 JRNL
REVDAT 1 27-JUN-01 1DUM 0
JRNL AUTH T.HARA,H.KODAMA,M.KONDO,K.WAKAMATSU,A.TAKEDA,T.TACHI,
JRNL AUTH 2 K.MATSUZAKI
JRNL TITL EFFECTS OF PEPTIDE DIMERIZATION ON PORE FORMATION:
JRNL TITL 2 ANTIPARALLEL DISULFIDE-DIMERIZED MAGAININ 2 ANALOGUE.
JRNL REF BIOPOLYMERS V. 58 437 2001
JRNL REFN ISSN 0006-3525
JRNL PMID 11180056
JRNL DOI 10.1002/1097-0282(20010405)58:4<437::AID-BIP1019>3.3.CO;2-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR 1.3, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (UXNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 466 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS (PER PROTOMER), 32 OF WHICH ARE
REMARK 3 TREATED AS AMBIGUOUS.
REMARK 4
REMARK 4 1DUM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010384.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM [F5Y, F16W] MAGAININ 2,
REMARK 210 0.5MM DLPC-D64
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 B 9 H GLY B 13 1.43
REMARK 500 O ALA A 9 H GLY A 13 1.47
REMARK 500 O PHE B 12 H TRP B 16 1.57
REMARK 500 O PHE A 12 H TRP A 16 1.58
REMARK 500 O LYS B 4 H ALA B 9 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 ILE A 2 131.40 64.19
REMARK 500 1 HIS A 7 13.48 -149.39
REMARK 500 1 SER A 8 -37.49 -165.39
REMARK 500 1 ILE B 2 91.72 62.44
REMARK 500 1 LYS B 4 -41.37 -146.36
REMARK 500 2 LYS A 4 -41.34 -158.87
REMARK 500 2 HIS A 7 -31.64 -131.14
REMARK 500 2 ALA A 9 -75.72 -51.19
REMARK 500 2 LYS A 10 -42.66 -29.16
REMARK 500 2 LYS B 4 -46.03 -148.61
REMARK 500 2 HIS B 7 12.91 -141.29
REMARK 500 2 SER B 8 -35.72 -164.89
REMARK 500 2 GLU B 19 -68.82 -91.89
REMARK 500 3 LYS A 4 -48.45 175.84
REMARK 500 3 SER A 8 -37.66 -157.98
REMARK 500 3 GLU A 19 -64.11 -91.32
REMARK 500 3 LYS B 4 -46.22 175.31
REMARK 500 3 HIS B 7 -32.97 -142.36
REMARK 500 3 LYS B 10 -39.20 -30.85
REMARK 500 4 LYS A 4 -41.56 -136.22
REMARK 500 4 HIS A 7 -28.42 -151.61
REMARK 500 4 ALA A 9 -63.80 -92.24
REMARK 500 4 GLU A 19 -72.44 -86.65
REMARK 500 4 LYS B 4 -45.94 -137.10
REMARK 500 4 SER B 8 -35.26 -168.94
REMARK 500 5 LYS A 4 -41.78 -147.26
REMARK 500 5 HIS A 7 12.51 -140.31
REMARK 500 5 SER A 8 -36.55 -165.85
REMARK 500 5 ALA A 9 -70.89 -60.40
REMARK 500 5 GLU A 19 -65.75 -91.32
REMARK 500 5 HIS B 7 -30.41 -152.81
REMARK 500 5 LYS B 10 -34.78 -39.64
REMARK 500 6 LYS A 4 -41.89 -144.05
REMARK 500 6 SER A 8 -36.32 -163.23
REMARK 500 6 ILE B 2 78.65 51.66
REMARK 500 6 LYS B 4 -44.68 -135.67
REMARK 500 6 SER B 8 -37.38 -158.24
REMARK 500 6 GLU B 19 -72.50 -86.82
REMARK 500 7 LYS A 4 -39.69 -136.77
REMARK 500 7 SER A 8 -37.93 -169.49
REMARK 500 7 GLU A 19 -71.32 -87.22
REMARK 500 7 LYS B 4 -39.35 -136.91
REMARK 500 7 SER B 8 -34.22 -171.16
REMARK 500 7 GLU B 19 -71.90 -87.69
REMARK 500 8 ILE A 2 75.38 59.40
REMARK 500 8 LYS A 4 -40.64 -137.70
REMARK 500 8 SER A 8 -36.26 -165.26
REMARK 500 8 LYS A 10 -48.05 -28.67
REMARK 500 8 GLU A 19 -61.57 -92.92
REMARK 500 8 SER B 8 -38.19 -141.90
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DUM A 1 23 UNP P11006 MAGA_XENLA 129 151
DBREF 1DUM B 1 23 UNP P11006 MAGA_XENLA 129 151
SEQADV 1DUM TYR A 5 UNP P11006 PHE 133 ENGINEERED MUTATION
SEQADV 1DUM TRP A 16 UNP P11006 PHE 144 ENGINEERED MUTATION
SEQADV 1DUM TYR B 5 UNP P11006 PHE 133 ENGINEERED MUTATION
SEQADV 1DUM TRP B 16 UNP P11006 PHE 144 ENGINEERED MUTATION
SEQRES 1 A 23 GLY ILE GLY LYS TYR LEU HIS SER ALA LYS LYS PHE GLY
SEQRES 2 A 23 LYS ALA TRP VAL GLY GLU ILE MET ASN SER
SEQRES 1 B 23 GLY ILE GLY LYS TYR LEU HIS SER ALA LYS LYS PHE GLY
SEQRES 2 B 23 LYS ALA TRP VAL GLY GLU ILE MET ASN SER
HELIX 1 1 SER A 8 MET A 21 1 14
HELIX 2 2 SER B 8 MET B 21 1 14
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 - 3 20 Bytes