Header list of 1l4v.pdb file
Complete list - 23 20 Bytes
HEADER ANTIBIOTIC 06-MAR-02 1L4V
TITLE SOLUTION STRUCTURE OF SAPECIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SAPECIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SARCOPHAGA PEREGRINA;
SOURCE 3 ORGANISM_TAXID: 7386
KEYWDS ANTIBACTERIAL PROTEIN, INSECT DEFENSIN, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR H.HANZAWA,H.IWAI,K.TAKEUCHI,T.KUZUHARA,H.KOMANO,D.KOHDA,F.INAGAKI,
AUTHOR 2 S.NATORI,Y.ARATA,I.SHIMADA
REVDAT 4 23-FEB-22 1L4V 1 REMARK
REVDAT 3 24-FEB-09 1L4V 1 VERSN
REVDAT 2 20-NOV-02 1L4V 1 REMARK
REVDAT 1 27-MAR-02 1L4V 0
JRNL AUTH H.HANZAWA,I.SHIMADA,T.KUZUHARA,H.KOMANO,D.KOHDA,F.INAGAKI,
JRNL AUTH 2 S.NATORI,Y.ARATA
JRNL TITL 1H NUCLEAR MAGNETIC RESONANCE STUDY OF THE SOLUTION
JRNL TITL 2 CONFORMATION OF AN ANTIBACTERIAL PROTEIN, SAPECIN.
JRNL REF FEBS LETT. V. 269 413 1990
JRNL REFN ISSN 0014-5793
JRNL PMID 2401368
JRNL DOI 10.1016/0014-5793(90)81206-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 366 RESTRAINTS, 338 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 28 DIHEDRAL ANGLE RESTRAINTS,26 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1L4V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015647.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM SAPECIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; HOHAHA; PE
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : GSX
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
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 : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
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: 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 1 HIS A 19 CG HIS A 19 ND1 -0.108
REMARK 500 2 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 2 HIS A 19 CG HIS A 19 ND1 -0.108
REMARK 500 3 HIS A 13 CG HIS A 13 ND1 -0.108
REMARK 500 3 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 4 HIS A 13 CG HIS A 13 ND1 -0.111
REMARK 500 4 HIS A 19 CG HIS A 19 ND1 -0.108
REMARK 500 5 HIS A 13 CG HIS A 13 ND1 -0.110
REMARK 500 5 HIS A 19 CG HIS A 19 ND1 -0.111
REMARK 500 6 HIS A 13 CG HIS A 13 ND1 -0.107
REMARK 500 6 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 7 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 7 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 8 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 8 HIS A 19 CG HIS A 19 ND1 -0.110
REMARK 500 9 HIS A 13 CG HIS A 13 ND1 -0.108
REMARK 500 9 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 10 HIS A 13 CG HIS A 13 ND1 -0.108
REMARK 500 10 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 11 HIS A 13 CG HIS A 13 ND1 -0.110
REMARK 500 11 HIS A 19 CG HIS A 19 ND1 -0.110
REMARK 500 12 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 12 HIS A 19 CG HIS A 19 ND1 -0.110
REMARK 500 13 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 13 HIS A 19 CG HIS A 19 ND1 -0.106
REMARK 500 14 HIS A 13 CG HIS A 13 ND1 -0.107
REMARK 500 14 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 15 HIS A 13 CG HIS A 13 ND1 -0.108
REMARK 500 15 HIS A 19 CG HIS A 19 ND1 -0.107
REMARK 500 16 HIS A 13 CG HIS A 13 ND1 -0.109
REMARK 500 16 HIS A 19 CG HIS A 19 ND1 -0.109
REMARK 500 17 HIS A 13 CG HIS A 13 ND1 -0.111
REMARK 500 17 HIS A 19 CG HIS A 19 ND1 -0.108
REMARK 500 18 HIS A 13 CG HIS A 13 ND1 -0.111
REMARK 500 18 HIS A 19 CG HIS A 19 ND1 -0.110
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 THR A 2 143.07 -173.26
REMARK 500 1 LEU A 5 -52.38 -142.96
REMARK 500 1 THR A 9 12.21 -69.01
REMARK 500 1 HIS A 13 -63.71 -108.08
REMARK 500 1 ASN A 25 -166.95 -111.15
REMARK 500 1 LYS A 33 -36.51 -172.23
REMARK 500 1 ALA A 34 43.86 -163.33
REMARK 500 2 ASP A 4 -171.93 50.28
REMARK 500 2 LEU A 6 96.46 53.84
REMARK 500 2 ILE A 11 95.90 45.77
REMARK 500 2 ASN A 12 64.48 -152.33
REMARK 500 2 ASN A 25 -168.52 -118.47
REMARK 500 2 LYS A 33 -32.62 -159.70
REMARK 500 2 ALA A 34 23.34 -167.54
REMARK 500 2 VAL A 35 74.54 -104.45
REMARK 500 2 CYS A 38 -172.14 -57.15
REMARK 500 2 ARG A 39 126.48 -170.71
REMARK 500 3 CYS A 3 -110.30 52.27
REMARK 500 3 ASP A 4 -163.39 -60.56
REMARK 500 3 LEU A 6 -32.68 -164.31
REMARK 500 3 ILE A 11 -12.47 -47.95
REMARK 500 3 ASN A 25 -168.98 -114.20
REMARK 500 3 LYS A 33 -35.26 -173.67
REMARK 500 3 ALA A 34 7.53 -151.26
REMARK 500 4 CYS A 3 30.16 -77.67
REMARK 500 4 ASP A 4 74.29 -173.58
REMARK 500 4 LEU A 6 -83.42 -132.91
REMARK 500 4 ASN A 12 -178.78 -170.52
REMARK 500 4 HIS A 13 -75.81 -153.38
REMARK 500 4 ASN A 25 -166.05 -110.21
REMARK 500 4 LYS A 33 -28.76 -170.62
REMARK 500 4 ALA A 34 25.61 -170.69
REMARK 500 4 CYS A 38 -172.34 -68.66
REMARK 500 4 ARG A 39 112.98 -172.75
REMARK 500 5 THR A 2 -167.23 -69.09
REMARK 500 5 ASP A 4 174.35 51.55
REMARK 500 5 LEU A 5 4.68 -68.16
REMARK 500 5 LEU A 6 23.94 -76.53
REMARK 500 5 ILE A 11 -178.74 -50.82
REMARK 500 5 LYS A 33 -37.29 -177.59
REMARK 500 5 ALA A 34 32.62 -147.62
REMARK 500 5 ARG A 39 132.48 -174.42
REMARK 500 6 THR A 2 155.87 -47.66
REMARK 500 6 ASP A 4 -163.53 -171.84
REMARK 500 6 LEU A 5 73.07 -119.49
REMARK 500 6 LEU A 6 -77.48 -96.30
REMARK 500 6 THR A 9 -74.80 -52.22
REMARK 500 6 ASN A 12 18.83 -170.24
REMARK 500 6 HIS A 13 -7.22 64.86
REMARK 500 6 ALA A 17 -18.40 -47.39
REMARK 500
REMARK 500 THIS ENTRY HAS 138 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 23 0.30 SIDE CHAIN
REMARK 500 1 ARG A 26 0.18 SIDE CHAIN
REMARK 500 1 ARG A 39 0.29 SIDE CHAIN
REMARK 500 2 ARG A 23 0.28 SIDE CHAIN
REMARK 500 2 ARG A 26 0.28 SIDE CHAIN
REMARK 500 3 ARG A 26 0.27 SIDE CHAIN
REMARK 500 3 ARG A 39 0.12 SIDE CHAIN
REMARK 500 4 ARG A 23 0.32 SIDE CHAIN
REMARK 500 4 ARG A 26 0.31 SIDE CHAIN
REMARK 500 4 ARG A 39 0.31 SIDE CHAIN
REMARK 500 5 ARG A 23 0.29 SIDE CHAIN
REMARK 500 5 ARG A 26 0.26 SIDE CHAIN
REMARK 500 6 ARG A 23 0.31 SIDE CHAIN
REMARK 500 6 ARG A 26 0.09 SIDE CHAIN
REMARK 500 6 ARG A 39 0.32 SIDE CHAIN
REMARK 500 7 ARG A 23 0.32 SIDE CHAIN
REMARK 500 7 ARG A 26 0.30 SIDE CHAIN
REMARK 500 7 ARG A 39 0.26 SIDE CHAIN
REMARK 500 8 ARG A 26 0.30 SIDE CHAIN
REMARK 500 8 ARG A 39 0.20 SIDE CHAIN
REMARK 500 9 ARG A 23 0.20 SIDE CHAIN
REMARK 500 9 ARG A 26 0.24 SIDE CHAIN
REMARK 500 9 ARG A 39 0.32 SIDE CHAIN
REMARK 500 10 ARG A 23 0.32 SIDE CHAIN
REMARK 500 10 ARG A 26 0.21 SIDE CHAIN
REMARK 500 10 ARG A 39 0.32 SIDE CHAIN
REMARK 500 11 ARG A 23 0.29 SIDE CHAIN
REMARK 500 11 ARG A 26 0.30 SIDE CHAIN
REMARK 500 11 ARG A 39 0.12 SIDE CHAIN
REMARK 500 12 ARG A 23 0.24 SIDE CHAIN
REMARK 500 12 ARG A 26 0.30 SIDE CHAIN
REMARK 500 12 ARG A 39 0.27 SIDE CHAIN
REMARK 500 13 ARG A 23 0.31 SIDE CHAIN
REMARK 500 13 ARG A 26 0.23 SIDE CHAIN
REMARK 500 14 ARG A 23 0.32 SIDE CHAIN
REMARK 500 14 ARG A 26 0.31 SIDE CHAIN
REMARK 500 14 ARG A 39 0.29 SIDE CHAIN
REMARK 500 15 ARG A 23 0.31 SIDE CHAIN
REMARK 500 15 ARG A 26 0.28 SIDE CHAIN
REMARK 500 15 ARG A 39 0.24 SIDE CHAIN
REMARK 500 16 ARG A 23 0.22 SIDE CHAIN
REMARK 500 16 ARG A 26 0.29 SIDE CHAIN
REMARK 500 16 ARG A 39 0.28 SIDE CHAIN
REMARK 500 17 ARG A 23 0.29 SIDE CHAIN
REMARK 500 17 ARG A 26 0.14 SIDE CHAIN
REMARK 500 17 ARG A 39 0.28 SIDE CHAIN
REMARK 500 18 ARG A 23 0.25 SIDE CHAIN
REMARK 500 18 ARG A 26 0.30 SIDE CHAIN
REMARK 500 18 ARG A 39 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1L4V A 1 40 UNP P18313 SAPE_SARPE 55 94
SEQRES 1 A 40 ALA THR CYS ASP LEU LEU SER GLY THR GLY ILE ASN HIS
SEQRES 2 A 40 SER ALA CYS ALA ALA HIS CYS LEU LEU ARG GLY ASN ARG
SEQRES 3 A 40 GLY GLY TYR CYS ASN GLY LYS ALA VAL CYS VAL CYS ARG
SEQRES 4 A 40 ASN
HELIX 1 1 HIS A 13 ASN A 25 1 13
SHEET 1 A 2 GLY A 27 ASN A 31 0
SHEET 2 A 2 VAL A 35 ARG A 39 -1 O ARG A 39 N GLY A 27
SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.02
SSBOND 2 CYS A 16 CYS A 36 1555 1555 2.02
SSBOND 3 CYS A 20 CYS A 38 1555 1555 2.02
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 - 23 20 Bytes