Header list of 1h0z.pdb file
Complete list - g 9 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 01-JUL-02 1H0Z
TITLE LEKTI DOMAIN SIX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE INHIBITOR KAZAL-TYPE 5, CONTAINS
COMPND 3 HEMOFILTRATE PEPTIDE HF6478, HEMOFILTRATE PEPTIDE HF7665;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: LEKTI DOMAIN SIX (HF7665), RESIDUES 356-423;
COMPND 6 SYNONYM: HF7665, LYMPHO-EPITHELIAL KAZAL-TYPE RELATED INHIBITOR,
COMPND 7 LEKTI;
COMPND 8 OTHER_DETAILS: DISULFIDE LINKAGE BETWEEN CYS A12 AND CYS A48, AND
COMPND 9 BETWEEN CYS A26 AND CYS A45
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BLOOD;
SOURCE 6 CELL: LYMPHO EPITHELIAL CELLS
KEYWDS SERINE PROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR T.LAUBER,P.ROESCH,U.C.MARX
REVDAT 4 14-JUN-23 1H0Z 1 SHEET
REVDAT 3 15-JAN-20 1H0Z 1 REMARK
REVDAT 2 24-FEB-09 1H0Z 1 VERSN
REVDAT 1 26-JUN-03 1H0Z 0
JRNL AUTH T.LAUBER,A.SCHULZ,K.SCHWEIMER,K.ADERMANN,U.C.MARX
JRNL TITL HOMOLOGOUS PROTEINS WITH DIFFERENT FOLDS: THE
JRNL TITL 2 THREE-DIMENSIONAL STRUCTURES OF DOMAINS 1 AND 6 OF THE
JRNL TITL 3 MULTIPLE KAZAL-TYPE INHIBITOR LEKTI
JRNL REF J.MOL.BIOL. V. 328 205 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12684009
JRNL DOI 10.1016/S0022-2836(03)00245-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1290011052.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; CLEAN-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ENERGY AND LEAST RESTRAINT
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D NMR
REMARK 210 EXPERIMENTS ON A NATIVE PROTEIN SAMPLE ISOLATED FROM HUMAN BLOOD
REMARK 210 FILTRATE
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 CYS A 12 H TYR A 15 1.57
REMARK 500 O SER A 7 H LEU A 11 1.60
REMARK 500 O ASN A 13 H ARG A 16 1.60
REMARK 500 O GLU A 57 H LYS A 60 1.60
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 6 169.86 54.57
REMARK 500 1 ARG A 20 -89.14 -82.20
REMARK 500 1 ASN A 21 44.15 -102.54
REMARK 500 1 THR A 27 -170.26 -58.45
REMARK 500 1 ARG A 28 63.24 -103.76
REMARK 500 1 ASN A 30 63.10 -102.73
REMARK 500 1 ASP A 31 83.31 -152.41
REMARK 500 1 ASN A 43 -167.62 -127.55
REMARK 500 2 ASN A 21 49.22 -140.08
REMARK 500 2 GLU A 29 -170.37 47.31
REMARK 500 2 ASN A 30 58.35 -146.72
REMARK 500 2 ASP A 31 83.25 -165.38
REMARK 500 3 THR A 6 -169.43 -60.84
REMARK 500 3 ARG A 20 -90.93 -102.40
REMARK 500 3 ASN A 21 58.12 -116.06
REMARK 500 3 ARG A 28 47.56 -84.08
REMARK 500 3 ASN A 30 55.54 -94.94
REMARK 500 4 ARG A 20 -90.77 -104.19
REMARK 500 4 ASN A 21 54.28 -119.87
REMARK 500 4 ASN A 30 60.97 -104.81
REMARK 500 4 ASN A 43 -167.89 -129.95
REMARK 500 5 ARG A 20 -81.97 -87.70
REMARK 500 5 THR A 27 -167.19 -100.24
REMARK 500 5 ASN A 30 60.20 -155.45
REMARK 500 5 ASP A 31 89.76 66.23
REMARK 500 6 THR A 6 -164.57 -71.81
REMARK 500 6 ARG A 20 -90.18 -89.88
REMARK 500 6 ARG A 28 47.03 -95.81
REMARK 500 6 GLU A 29 155.65 -48.74
REMARK 500 6 ASN A 30 58.45 -95.18
REMARK 500 7 THR A 6 -164.21 -108.65
REMARK 500 7 ASN A 21 31.11 -159.58
REMARK 500 7 LYS A 23 65.18 -100.76
REMARK 500 7 ASN A 30 58.16 -97.82
REMARK 500 8 ARG A 20 -90.08 -82.50
REMARK 500 8 ASN A 21 55.85 -116.69
REMARK 500 8 ASN A 30 59.02 -100.05
REMARK 500 8 GLU A 63 96.51 47.15
REMARK 500 9 ARG A 20 -92.02 -80.49
REMARK 500 9 ASN A 21 57.49 -119.15
REMARK 500 9 ASN A 30 61.14 -106.42
REMARK 500 10 ARG A 20 -86.82 -126.70
REMARK 500 10 ASN A 21 32.45 -98.58
REMARK 500 10 THR A 27 -167.59 -100.25
REMARK 500 10 ASN A 30 85.83 -157.28
REMARK 500 10 ASP A 31 95.92 61.35
REMARK 500 11 ARG A 20 -98.44 -110.90
REMARK 500 11 ASN A 21 51.15 -105.46
REMARK 500 11 GLU A 29 148.89 59.02
REMARK 500 11 ASN A 30 55.40 -106.40
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 16 0.20 SIDE CHAIN
REMARK 500 1 ARG A 20 0.31 SIDE CHAIN
REMARK 500 1 ARG A 28 0.27 SIDE CHAIN
REMARK 500 1 ARG A 67 0.30 SIDE CHAIN
REMARK 500 2 ARG A 16 0.12 SIDE CHAIN
REMARK 500 2 ARG A 20 0.23 SIDE CHAIN
REMARK 500 2 ARG A 28 0.30 SIDE CHAIN
REMARK 500 2 ARG A 67 0.26 SIDE CHAIN
REMARK 500 3 ARG A 16 0.31 SIDE CHAIN
REMARK 500 3 ARG A 20 0.31 SIDE CHAIN
REMARK 500 3 ARG A 28 0.31 SIDE CHAIN
REMARK 500 3 ARG A 67 0.08 SIDE CHAIN
REMARK 500 4 ARG A 16 0.29 SIDE CHAIN
REMARK 500 4 ARG A 20 0.30 SIDE CHAIN
REMARK 500 4 ARG A 28 0.22 SIDE CHAIN
REMARK 500 4 ARG A 67 0.29 SIDE CHAIN
REMARK 500 5 ARG A 16 0.28 SIDE CHAIN
REMARK 500 5 ARG A 20 0.17 SIDE CHAIN
REMARK 500 5 ARG A 28 0.30 SIDE CHAIN
REMARK 500 5 ARG A 67 0.25 SIDE CHAIN
REMARK 500 6 ARG A 16 0.27 SIDE CHAIN
REMARK 500 6 ARG A 20 0.30 SIDE CHAIN
REMARK 500 6 ARG A 28 0.32 SIDE CHAIN
REMARK 500 6 ARG A 67 0.20 SIDE CHAIN
REMARK 500 7 ARG A 16 0.27 SIDE CHAIN
REMARK 500 7 ARG A 20 0.25 SIDE CHAIN
REMARK 500 7 ARG A 28 0.27 SIDE CHAIN
REMARK 500 7 ARG A 67 0.20 SIDE CHAIN
REMARK 500 8 ARG A 16 0.15 SIDE CHAIN
REMARK 500 8 ARG A 20 0.18 SIDE CHAIN
REMARK 500 8 ARG A 28 0.32 SIDE CHAIN
REMARK 500 8 ARG A 67 0.29 SIDE CHAIN
REMARK 500 9 ARG A 16 0.32 SIDE CHAIN
REMARK 500 9 ARG A 20 0.28 SIDE CHAIN
REMARK 500 9 ARG A 28 0.21 SIDE CHAIN
REMARK 500 9 ARG A 67 0.29 SIDE CHAIN
REMARK 500 10 ARG A 16 0.20 SIDE CHAIN
REMARK 500 10 ARG A 20 0.24 SIDE CHAIN
REMARK 500 10 ARG A 28 0.26 SIDE CHAIN
REMARK 500 11 ARG A 16 0.32 SIDE CHAIN
REMARK 500 11 ARG A 20 0.20 SIDE CHAIN
REMARK 500 11 ARG A 28 0.28 SIDE CHAIN
REMARK 500 11 ARG A 67 0.27 SIDE CHAIN
REMARK 500 12 ARG A 16 0.23 SIDE CHAIN
REMARK 500 12 ARG A 20 0.32 SIDE CHAIN
REMARK 500 12 ARG A 28 0.29 SIDE CHAIN
REMARK 500 12 ARG A 67 0.31 SIDE CHAIN
REMARK 500 13 ARG A 16 0.19 SIDE CHAIN
REMARK 500 13 ARG A 20 0.31 SIDE CHAIN
REMARK 500 13 ARG A 28 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 83 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5551 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THE PROTEIN USED IN THE NMR STUDY DIFFERS
REMARK 999 FROM THAT OF THE MATCHING SWISS-PROT ENTRY AT POSITION
REMARK 999 420. RESIDUE 420 IS A GLU, NOT LYS AS IN THE SWISS-PROT
REMARK 999 ENTRY
DBREF 1H0Z A 1 68 UNP Q9NQ38 ISK5_HUMAN 356 423
SEQADV 1H0Z GLU A 65 UNP Q9NQ38 LYS 420 CONFLICT
SEQRES 1 A 68 GLU SER GLY LYS ALA THR SER TYR ALA GLU LEU CYS ASN
SEQRES 2 A 68 GLU TYR ARG LYS LEU VAL ARG ASN GLY LYS LEU ALA CYS
SEQRES 3 A 68 THR ARG GLU ASN ASP PRO ILE GLN GLY PRO ASP GLY LYS
SEQRES 4 A 68 VAL HIS GLY ASN THR CYS SER MET CYS GLU VAL PHE PHE
SEQRES 5 A 68 GLN ALA GLU GLU GLU GLU LYS LYS LYS LYS GLU GLY GLU
SEQRES 6 A 68 SER ARG ASN
HELIX 1 1 SER A 7 CYS A 12 1 6
HELIX 2 2 ASN A 13 ARG A 16 5 4
HELIX 3 3 ASN A 43 LYS A 62 1 20
SHEET 1 AA 2 ILE A 33 GLN A 34 0
SHEET 2 AA 2 VAL A 40 HIS A 41 -1 N HIS A 41 O ILE A 33
SSBOND 1 CYS A 12 CYS A 48 1555 1555 2.02
SSBOND 2 CYS A 26 CYS A 45 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 - g 9 2 Bytes