Header list of 1zfl.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE INHIBITOR 20-APR-05 1ZFL
TITLE SOLUTION STRUCTURE OF III-A, THE MAJOR INTERMEDIATE IN THE OXIDATIVE
TITLE 2 FOLDING OF LEECH CARBOXYPEPTIDASE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOCARBOXYPEPTIDASE INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LEECH CARBOXYPEPTIDASE INHIBITOR, LCI, INHIBITOR OF A/B
COMPND 5 METALLOCARBOXYPEPTIDASES;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE III-A INTERMEDIATE, CONTAINING THREE NATIVE
COMPND 8 DISULFIDE BONDS, HAS BEEN DIRECTLY ISOLATED FROM THE OXIDATIVE
COMPND 9 FOLDING REACTION OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI; FOUR
COMPND 10 DISULFIDE BONDS)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 3 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 4 ORGANISM_TAXID: 6421;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAT4
KEYWDS CARBOXYPEPTIDASE INHIBITOR, FOLDING INTERMEDIATE, OXIDATIVE FOLDING,
KEYWDS 2 FOUR-STRANDED ANTIPARALLEL BETA-SHEET, HYDROLASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.L.AROLAS,L.D'SILVA,G.M.POPOWICZ,F.X.AVILES,T.A.HOLAK,S.VENTURA
REVDAT 3 02-MAR-22 1ZFL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZFL 1 VERSN
REVDAT 1 13-SEP-05 1ZFL 0
JRNL AUTH J.L.AROLAS,L.D'SILVA,G.M.POPOWICZ,F.X.AVILES,T.A.HOLAK,
JRNL AUTH 2 S.VENTURA
JRNL TITL NMR STRUCTURAL CHARACTERIZATION AND COMPUTATIONAL
JRNL TITL 2 PREDICTIONS OF THE MAJOR INTERMEDIATE IN OXIDATIVE FOLDING
JRNL TITL 3 OF LEECH CARBOXYPEPTIDASE INHIBITOR
JRNL REF STRUCTURE V. 13 1193 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16084391
JRNL DOI 10.1016/J.STR.2005.05.008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.REVERTER,C.FERNANDEZ-CATALAN,R.BAUMGARTNER,R.PFANDER,
REMARK 1 AUTH 2 R.HUBER,W.BODE,J.VENDRELL,T.A.HOLAK,F.X.AVILES
REMARK 1 TITL STRUCTURE OF A NOVEL LEECH CARBOXYPEPTIDASE INHIBITOR
REMARK 1 TITL 2 DETERMINED FREE IN SOLUTION AND IN COMPLEX WITH HUMAN
REMARK 1 TITL 3 CARBOXYPEPTIDASE A2
REMARK 1 REF NAT.STRUCT.MOL.BIOL. V. 7 322 2000
REMARK 1 REFN ISSN 1545-9993
REMARK 1 PMID 10742178
REMARK 1 DOI 10.1038/74092
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.AROLAS,S.BRONSOMS,J.LORENZO,F.X.AVILES,J.Y.CHANG,
REMARK 1 AUTH 2 S.VENTURA
REMARK 1 TITL ROLE OF KINETIC INTERMEDIATES IN THE FOLDING OF LEECH
REMARK 1 TITL 2 CARBOXYPEPTIDASE INHIBITOR
REMARK 1 REF J.BIOL.CHEM. V. 279 37261 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15226306
REMARK 1 DOI 10.1074/JBC.M405565200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS
REMARK 3 AUTHORS : BRUKER SOFTWARE (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZFL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032662.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 15N-LABELED III-A
REMARK 210 INTERMEDIATE; 90% H2O, 10% D2O;
REMARK 210 1MM 15N-LABELED III-A
REMARK 210 INTERMEDIATE; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 1H-15N HSQC
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 : SPARKY SPARKY 3, CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: AMIDE PROTON EXCHANGE EXPERIMENTS WERE CARRIED OUT
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 ASP A 6 -28.93 -165.71
REMARK 500 1 GLU A 7 -131.84 172.43
REMARK 500 1 ASP A 15 12.88 -147.46
REMARK 500 1 CYS A 22 156.06 167.97
REMARK 500 1 ALA A 26 -63.82 -175.89
REMARK 500 1 PRO A 27 98.27 -45.90
REMARK 500 1 LEU A 28 -54.43 -168.41
REMARK 500 1 SER A 30 -57.95 -151.37
REMARK 500 1 GLU A 33 -165.57 -51.23
REMARK 500 1 CYS A 34 34.13 140.79
REMARK 500 1 PRO A 38 -56.24 -29.03
REMARK 500 1 THR A 39 -157.80 -134.99
REMARK 500 1 ALA A 40 173.42 179.43
REMARK 500 1 PRO A 41 30.62 -83.99
REMARK 500 1 TRP A 42 -38.90 -164.32
REMARK 500 1 ALA A 47 -144.43 -106.47
REMARK 500 1 VAL A 48 31.55 -92.74
REMARK 500 1 TYR A 53 -156.13 -116.19
REMARK 500 1 THR A 55 -61.80 -149.68
REMARK 500 1 GLN A 57 -156.32 -103.16
REMARK 500 1 CYS A 58 -178.14 170.22
REMARK 500 1 ARG A 59 158.86 156.25
REMARK 500 1 THR A 60 56.79 -173.14
REMARK 500 1 TYR A 65 -141.09 -109.10
REMARK 500 2 HIS A 3 -45.54 -159.50
REMARK 500 2 GLU A 7 -139.31 -32.89
REMARK 500 2 PRO A 14 -9.70 -54.31
REMARK 500 2 ASP A 15 29.82 -158.83
REMARK 500 2 CYS A 22 -172.33 -170.43
REMARK 500 2 ARG A 23 -31.23 -134.85
REMARK 500 2 ALA A 25 -74.78 -105.47
REMARK 500 2 PRO A 27 -165.84 -74.10
REMARK 500 2 PRO A 29 -166.01 -64.00
REMARK 500 2 GLU A 31 30.91 -87.17
REMARK 500 2 GLU A 33 -167.85 -53.81
REMARK 500 2 CYS A 34 29.51 137.71
REMARK 500 2 PRO A 36 103.47 -59.66
REMARK 500 2 PRO A 38 -57.55 -25.81
REMARK 500 2 ALA A 40 176.68 169.84
REMARK 500 2 VAL A 48 -79.80 -80.09
REMARK 500 2 PRO A 52 150.11 -46.60
REMARK 500 2 THR A 55 -53.18 -127.86
REMARK 500 2 GLN A 57 -142.73 -105.67
REMARK 500 2 CYS A 58 -20.82 150.42
REMARK 500 2 THR A 60 146.28 -172.81
REMARK 500 2 TYR A 65 -134.18 173.51
REMARK 500 3 THR A 4 -61.22 -168.12
REMARK 500 3 ASP A 6 -21.39 -171.05
REMARK 500 3 GLU A 7 -132.20 -177.94
REMARK 500 3 PRO A 14 -15.30 -48.76
REMARK 500
REMARK 500 THIS ENTRY HAS 441 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZFI RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR
REMARK 900 DETERMINED AT PH 3.5
REMARK 900 RELATED ID: 1DTV RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR
REMARK 900 DETERMINED AT PH 6.5
REMARK 900 RELATED ID: 1DTD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR IN
REMARK 900 COMPLEX WITH HUMAN CARBOXYPEPTIDASE A2
DBREF 1ZFL A 2 67 UNP P81511 MCPI_HIRME 16 81
SEQADV 1ZFL GLY A 1 UNP P81511 CLONING ARTIFACT
SEQRES 1 A 67 GLY SER HIS THR PRO ASP GLU SER PHE LEU CYS TYR GLN
SEQRES 2 A 67 PRO ASP GLN VAL CYS CYS PHE ILE CYS ARG GLY ALA ALA
SEQRES 3 A 67 PRO LEU PRO SER GLU GLY GLU CYS ASN PRO HIS PRO THR
SEQRES 4 A 67 ALA PRO TRP CYS ARG GLU GLY ALA VAL GLU TRP VAL PRO
SEQRES 5 A 67 TYR SER THR GLY GLN CYS ARG THR THR CYS ILE PRO TYR
SEQRES 6 A 67 VAL GLU
SHEET 1 A 4 ASN A 35 PRO A 36 0
SHEET 2 A 4 PHE A 9 GLN A 13 -1 N LEU A 10 O ASN A 35
SHEET 3 A 4 GLN A 16 PHE A 20 -1 O PHE A 20 N PHE A 9
SHEET 4 A 4 THR A 61 ILE A 63 -1 O THR A 61 N CYS A 19
SSBOND 1 CYS A 11 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 18 CYS A 62 1555 1555 2.03
SSBOND 3 CYS A 19 CYS A 43 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 - r 2 2 Bytes