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HEADER CARBOXYPEPTIDASE 12-JUN-96 1IVY
TITLE PHYSIOLOGICAL DIMER HPP PRECURSOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN PROTECTIVE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTECTIVE PROTEIN/CATHEPSIN A,
COMPND 5 CARBOXYPEPTIDASE L;
COMPND 6 EC: 3.4.16.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 BIOLOGICAL_UNIT: HETERODIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: SF21 INSECT CELLS;
SOURCE 5 EXPRESSION_SYSTEM_GENE: HUPP54;
SOURCE 6 OTHER_DETAILS: BACULOVIRUS MEDIATED OVER-EXPRESSION. SEE
SOURCE 7 BONTEN ET AL. 1995, J.B.C. 270, P. 26441-26445
KEYWDS CARBOXYPEPTIDASE, SERINE CARBOXYPEPTIDASE,
KEYWDS 2 PROTECTIVE PROTEIN, GLYCOPROTEIN, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.RUDENKO,E.BONTEN,A.D'AZZO,W.G.J.HOL
REVDAT 1 21-APR-97 1IVY 0
JRNL AUTH G.RUDENKO,E.BONTEN,A.D'AZZO,W.G.HOL
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE HUMAN
JRNL TITL 2 'PROTECTIVE PROTEIN': STRUCTURE OF THE PRECURSOR
JRNL TITL 3 FORM SUGGESTS A COMPLEX ACTIVATION MECHANISM
JRNL REF STRUCTURE (LONDON) V. 3 1249 1995
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.RUDENKO,E.BONTEN,A.D'AZZO,W.G.J.HOL
REMARK 1 TITL STRUCTURE DETERMINATION OF THE HUMAN PROTECTIVE
REMARK 1 TITL 2 PROTEIN: TWOFOLD AVERAGING REVEALS THE
REMARK 1 TITL 3 THREE-DIMENSIONAL STRUCTURE OF A DOMAIN WHICH WAS
REMARK 1 TITL 4 ENTIRELY ABSENT IN THE INITIAL MODEL
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 923 1996
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 0766
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.J.GALJART,N.GILLEMANS,A.HARRIS,
REMARK 1 AUTH 2 G.T.VAN DER HORST,F.W.VERHEIJEN,H.GALJAARD,A.D'AZZO
REMARK 1 TITL EXPRESSION OF CDNA ENCODING THE HUMAN 'PROTECTIVE
REMARK 1 TITL 2 PROTEIN' ASSOCIATED WITH LYSOSOMAL
REMARK 1 TITL 3 BETA-GALACTOSIDASE AND NEURAMINIDASE: HOMOLOGY TO
REMARK 1 TITL 4 YEAST PROTEASES
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 54 755 1988
REMARK 1 REFN ASTM CELLB5 US ISSN 0092-8674 0998
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.2
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.9
REMARK 3 NUMBER OF REFLECTIONS : 57704
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.2
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.3
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.9
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.240
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7173
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.282
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.72
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ESTIMATED COORD. ERROR 0.282 ANGSTROMS
REMARK 3 MEAN B (A**2) (MAIN CHAIN): 16.6
REMARK 3 MEAN B (A**2) (SIDE CHAIN): 18.3
REMARK 4
REMARK 4 1IVY COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 BECAUSE OF SIGNIFICANT DIFFERENCES BETWEEN THE TWO
REMARK 6 MONOMERS DUE TO A CRYSTAL CONTACT, THE COORDINATES OF A
REMARK 6 DIMER HAVE BEEN SUBMITTED.
REMARK 7
REMARK 7 RESIDUES ASN B 216 AND LEU B 217 ARE IN AN AREA OF POOR
REMARK 7 ELECTRON DENSITY. THE EXACT GEOMETRY OF THESE RESIDUES
REMARK 7 IS NOT CLEAR FROM THE ELECTRON DENSITY MAP, BUT THEIR
REMARK 7 GENERAL POSITION IS. IN ADDITION, THE RESTRAINING
REMARK 7 DISULFIDE CYS 213 - CYS 218 SUPPORTS THE DEPOSITORS'
REMARK 7 MODEL IN THIS AREA.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-1994
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : 7.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 5.2
REMARK 200 DATA SCALING SOFTWARE : ROTAVATA, AGROVATA,
REMARK 200 TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67740
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.2
REMARK 200 RESOLUTION RANGE LOW (A) : 32.3
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : ~6.
REMARK 200 R MERGE (I) : 0.051
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : ~6.
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.130
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.7
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT AND TWO-FOLD AVERAGING
REMARK 200 SOFTWARE USED: X-PLOR, RAVE, CCCP4 SUITE
REMARK 200 STARTING MODEL: SERINE CARBOXYPEPTIDASE FROM WHEAT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 8.0 - 8.3 AT
REMARK 280 4 - 12 DEGREES CELSIUS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 57.51754
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.05213
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.51754
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.05213
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 8 CG CD OE1 NE2
REMARK 470 ARG A 9 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 ASN A 47 CG OD1 ND2
REMARK 470 PHE A 113 CG CD1 CE1 CZ CE2 CD2
REMARK 470 GLU A 326 CG CD OE1 OE2
REMARK 470 VAL A 393 CG1 CG2
REMARK 470 GLU B 46 CG CD OE1 OE2
REMARK 470 GLN B 215 CG CD OE1 NE2
REMARK 470 LYS B 217 CG CD CE NZ
REMARK 470 PHE B 261 CG CD1 CE1 CZ CE2 CD2
REMARK 470 TYR B 263 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 LYS B 283 CG CD CE NZ
REMARK 470 LYS B 296 CG CD CE NZ
REMARK 470 GLU B 326 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 216 LYS B 217 0 124.19
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD SERINE CARBOXYPEPTIDASE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1IVY A SWS P10619 1 - 28 NOT IN ATOMS LIST
REMARK 999 1IVY B SWS P10619 1 - 28 NOT IN ATOMS LIST
DBREF 1IVY A 1 452 SWS P10619 PRTP_HUMAN 29 480
DBREF 1IVY B 1 258 SWS P10619 PRTP_HUMAN 29 286
DBREF 1IVY B 261 452 SWS P10619 PRTP_HUMAN 289 480
SEQADV 1IVY B SWS P10619 SER 287 GAP IN PDB ENTRY
SEQADV 1IVY B SWS P10619 HIS 288 GAP IN PDB ENTRY
SEQRES 1 A 452 ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU
SEQRES 2 A 452 ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU
SEQRES 3 A 452 LYS SER SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL
SEQRES 4 A 452 GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU
SEQRES 5 A 452 TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY
SEQRES 6 A 452 LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP
SEQRES 7 A 452 GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU
SEQRES 8 A 452 ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL
SEQRES 9 A 452 GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN
SEQRES 10 A 452 ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN
SEQRES 11 A 452 ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS
SEQRES 12 A 452 LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE
SEQRES 13 A 452 PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET
SEQRES 14 A 452 ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER
SEQRES 15 A 452 TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR
SEQRES 16 A 452 TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU
SEQRES 17 A 452 GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR
SEQRES 18 A 452 ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU
SEQRES 19 A 452 VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR
SEQRES 20 A 452 ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS
SEQRES 21 A 452 PHE ARG TYR GLU LYS ASP THR VAL VAL VAL GLN ASP LEU
SEQRES 22 A 452 GLY ASN ILE PHE THR ARG LEU PRO LEU LYS ARG MET TRP
SEQRES 23 A 452 HIS GLN ALA LEU LEU ARG SER GLY ASP LYS VAL ARG MET
SEQRES 24 A 452 ASP PRO PRO CYS THR ASN THR THR ALA ALA SER THR TYR
SEQRES 25 A 452 LEU ASN ASN PRO TYR VAL ARG LYS ALA LEU ASN ILE PRO
SEQRES 26 A 452 GLU GLN LEU PRO GLN TRP ASP MET CYS ASN PHE LEU VAL
SEQRES 27 A 452 ASN LEU GLN TYR ARG ARG LEU TYR ARG SER MET ASN SER
SEQRES 28 A 452 GLN TYR LEU LYS LEU LEU SER SER GLN LYS TYR GLN ILE
SEQRES 29 A 452 LEU LEU TYR ASN GLY ASP VAL ASP MET ALA CYS ASN PHE
SEQRES 30 A 452 MET GLY ASP GLU TRP PHE VAL ASP SER LEU ASN GLN LYS
SEQRES 31 A 452 MET GLU VAL GLN ARG ARG PRO TRP LEU VAL LYS TYR GLY
SEQRES 32 A 452 ASP SER GLY GLU GLN ILE ALA GLY PHE VAL LYS GLU PHE
SEQRES 33 A 452 SER HIS ILE ALA PHE LEU THR ILE LYS GLY ALA GLY HIS
SEQRES 34 A 452 MET VAL PRO THR ASP LYS PRO LEU ALA ALA PHE THR MET
SEQRES 35 A 452 PHE SER ARG PHE LEU ASN LYS GLN PRO TYR
SEQRES 1 B 452 ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU
SEQRES 2 B 452 ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU
SEQRES 3 B 452 LYS SER SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL
SEQRES 4 B 452 GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU
SEQRES 5 B 452 TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY
SEQRES 6 B 452 LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP
SEQRES 7 B 452 GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU
SEQRES 8 B 452 ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL
SEQRES 9 B 452 GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN
SEQRES 10 B 452 ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN
SEQRES 11 B 452 ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS
SEQRES 12 B 452 LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE
SEQRES 13 B 452 PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET
SEQRES 14 B 452 ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER
SEQRES 15 B 452 TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR
SEQRES 16 B 452 TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU
SEQRES 17 B 452 GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR
SEQRES 18 B 452 ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU
SEQRES 19 B 452 VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR
SEQRES 20 B 452 ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS
SEQRES 21 B 452 PHE ARG TYR GLU LYS ASP THR VAL VAL VAL GLN ASP LEU
SEQRES 22 B 452 GLY ASN ILE PHE THR ARG LEU PRO LEU LYS ARG MET TRP
SEQRES 23 B 452 HIS GLN ALA LEU LEU ARG SER GLY ASP LYS VAL ARG MET
SEQRES 24 B 452 ASP PRO PRO CYS THR ASN THR THR ALA ALA SER THR TYR
SEQRES 25 B 452 LEU ASN ASN PRO TYR VAL ARG LYS ALA LEU ASN ILE PRO
SEQRES 26 B 452 GLU GLN LEU PRO GLN TRP ASP MET CYS ASN PHE LEU VAL
SEQRES 27 B 452 ASN LEU GLN TYR ARG ARG LEU TYR ARG SER MET ASN SER
SEQRES 28 B 452 GLN TYR LEU LYS LEU LEU SER SER GLN LYS TYR GLN ILE
SEQRES 29 B 452 LEU LEU TYR ASN GLY ASP VAL ASP MET ALA CYS ASN PHE
SEQRES 30 B 452 MET GLY ASP GLU TRP PHE VAL ASP SER LEU ASN GLN LYS
SEQRES 31 B 452 MET GLU VAL GLN ARG ARG PRO TRP LEU VAL LYS TYR GLY
SEQRES 32 B 452 ASP SER GLY GLU GLN ILE ALA GLY PHE VAL LYS GLU PHE
SEQRES 33 B 452 SER HIS ILE ALA PHE LEU THR ILE LYS GLY ALA GLY HIS
SEQRES 34 B 452 MET VAL PRO THR ASP LYS PRO LEU ALA ALA PHE THR MET
SEQRES 35 B 452 PHE SER ARG PHE LEU ASN LYS GLN PRO TYR
HET NAG A3010 14
HET NAG A3011 14
HET NAG A3020 14
HET NAG B3030 14
HET NAG B3031 14
HET NAG B3040 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 6(C8 H15 N1 O6)
FORMUL 4 HOH *296(H2 O1)
HELIX 1 1 LEU A 63 LEU A 67 1 5
HELIX 2 2 ASP A 118 LEU A 135 1 18
HELIX 3 3 ALA A 152 VAL A 163 5 12
HELIX 4 4 TYR A 183 TYR A 196 1 14
HELIX 5 5 ASN A 202 CYS A 212 1 11
HELIX 6 6 LEU A 226 GLY A 240 1 15
HELIX 7 7 LEU A 290 SER A 293 5 4
HELIX 8 8 THR A 307 LEU A 313 1 7
HELIX 9 9 PRO A 316 ALA A 321 1 6
HELIX 10 10 PHE A 336 GLN A 341 1 6
HELIX 11 11 ASN A 350 SER A 359 1 10
HELIX 12 12 PHE A 377 SER A 386 1 10
HELIX 13 13 VAL A 431 ASP A 434 1 4
HELIX 14 14 PRO A 436 LEU A 447 1 12
HELIX 15 15 LEU B 63 LEU B 67 1 5
HELIX 16 16 ASP B 118 LEU B 135 1 18
HELIX 17 17 ALA B 152 VAL B 163 5 12
HELIX 18 18 TYR B 183 TYR B 196 1 14
HELIX 19 19 ASN B 202 CYS B 212 1 11
HELIX 20 20 LEU B 226 GLY B 240 1 15
HELIX 21 21 THR B 307 LEU B 313 1 7
HELIX 22 22 PRO B 316 ALA B 321 1 6
HELIX 23 23 PHE B 336 GLN B 341 1 6
HELIX 24 24 ASN B 350 SER B 359 1 10
HELIX 25 25 PHE B 377 SER B 386 1 10
HELIX 26 26 VAL B 431 ASP B 434 1 4
HELIX 27 27 PRO B 436 LEU B 447 1 12
SHEET 1 A10 GLN A 21 LYS A 27 0
SHEET 2 A10 LYS A 32 VAL A 39 -1 N PHE A 38 O TYR A 22
SHEET 3 A10 ASN A 94 LEU A 98 -1 N TYR A 97 O TRP A 37
SHEET 4 A10 VAL A 50 LEU A 54 1 N VAL A 51 O ASN A 94
SHEET 5 A10 LEU A 144 GLU A 149 1 N PHE A 145 O VAL A 50
SHEET 6 A10 LEU A 171 GLY A 177 1 N GLN A 172 O LEU A 144
SHEET 7 A10 GLN A 363 GLY A 369 1 N GLN A 363 O LEU A 174
SHEET 8 A10 ILE A 419 ILE A 424 1 N ALA A 420 O ILE A 364
SHEET 9 A10 GLU A 407 PHE A 416 -1 N LYS A 414 O PHE A 421
SHEET 10 A10 MET A 391 LYS A 401 -1 N VAL A 400 O GLN A 408
SHEET 1 B 2 PHE A 73 VAL A 75 0
SHEET 2 B 2 LEU A 82 TYR A 84 -1 N GLU A 83 O LEU A 74
SHEET 1 C 3 PHE A 261 GLU A 264 0
SHEET 2 C 3 THR A 267 VAL A 270 -1 N VAL A 269 O ARG A 262
SHEET 3 C 3 LYS A 296 MET A 299 1 N LYS A 296 O VAL A 268
SHEET 1 D10 GLN B 21 LYS B 27 0
SHEET 2 D10 LYS B 32 VAL B 39 -1 N PHE B 38 O TYR B 22
SHEET 3 D10 ASN B 94 LEU B 98 -1 N TYR B 97 O TRP B 37
SHEET 4 D10 VAL B 50 LEU B 54 1 N VAL B 51 O ASN B 94
SHEET 5 D10 LEU B 144 GLU B 149 1 N PHE B 145 O VAL B 50
SHEET 6 D10 LEU B 171 GLY B 177 1 N GLN B 172 O LEU B 144
SHEET 7 D10 GLN B 363 GLY B 369 1 N GLN B 363 O LEU B 174
SHEET 8 D10 ILE B 419 ILE B 424 1 N ALA B 420 O ILE B 364
SHEET 9 D10 GLU B 407 PHE B 416 -1 N PHE B 416 O ILE B 419
SHEET 10 D10 MET B 391 LYS B 401 -1 N VAL B 400 O GLN B 408
SHEET 1 E 2 PHE B 73 VAL B 75 0
SHEET 2 E 2 LEU B 82 TYR B 84 -1 N GLU B 83 O LEU B 74
SHEET 1 F 2 THR B 267 VAL B 270 0
SHEET 2 F 2 LYS B 296 MET B 299 1 N LYS B 296 O VAL B 268
SSBOND 1 CYS A 60 CYS A 334
SSBOND 2 CYS A 212 CYS A 228
SSBOND 3 CYS A 213 CYS A 218
SSBOND 4 CYS A 253 CYS A 303
SSBOND 5 CYS B 60 CYS B 334
SSBOND 6 CYS B 212 CYS B 228
SSBOND 7 CYS B 213 CYS B 218
SSBOND 8 CYS B 253 CYS B 303
LINK C1 NAG A3010 ND2 ASN A 117
LINK O4 NAG A3010 C1 NAG A3011
LINK C1 NAG A3020 ND2 ASN A 305
LINK C1 NAG B3030 ND2 ASN B 117
LINK O4 NAG B3030 C1 NAG B3031
LINK C1 NAG B3040 ND2 ASN B 305
CISPEP 1 GLY A 57 PRO A 58 0 1.29
CISPEP 2 SER A 100 PRO A 101 0 0.52
CISPEP 3 GLY B 57 PRO B 58 0 -0.46
CISPEP 4 SER B 100 PRO B 101 0 -0.63
SITE 1 CAT 6 SER A 150 ASP A 372 HIS A 429 SER B 150
SITE 2 CAT 6 ASP B 372 HIS B 429
CRYST1 115.040 148.110 80.970 90.00 90.00 90.00 P 21 21 2 8
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 0.008693 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012350 0.00000 |