HEADER HYDROLASE 23-APR-04 1T31
TITLE A DUAL INHIBITOR OF THE LEUKOCYTE PROTEASES CATHEPSIN G AND CHYMASE
TITLE 2 WITH THERAPEUTIC EFFICACY IN ANIMALS MODELS OF INFLAMMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAST CELL PROTEASE I;
COMPND 5 EC: 3.4.21.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CMA1, CYM, CYH;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HUMAN CHYMASE, SERINE PROTEINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.DE GARAVILLA,M.N.GRECO,E.C.GIARDINO,G.I.WELLS,B.J.HAERTLEIN,
AUTHOR 2 J.A.KAUFFMAN,T.W.CORCORAN,C.K.DERIAN,A.J.ECKARDT,W.M.ABRAHAM,
AUTHOR 3 N.SUKUMAR,Z.CHEN,A.O.PINEDA,F.S.MATHEWS,E.DI CERA,P.ANDRADE-GORDON,
AUTHOR 4 B.P.DAMIANO,B.E.MARYANOFF,P.J.B.PEREIRA,Z.M.WANG,H.RUBIN,R.HUBER,
AUTHOR 5 W.BODE,N.M.SCHECHTER,S.STROBL
REVDAT 7 23-AUG-23 1T31 1 REMARK
REVDAT 6 27-OCT-21 1T31 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 1T31 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 13-JUL-11 1T31 1 VERSN
REVDAT 3 24-FEB-09 1T31 1 VERSN
REVDAT 2 10-MAY-05 1T31 1 JRNL
REVDAT 1 01-MAR-05 1T31 0
JRNL AUTH L.DE GARAVILLA,M.N.GRECO,N.SUKUMAR,Z.W.CHEN,A.O.PINEDA,
JRNL AUTH 2 F.S.MATHEWS,E.DI CERA,E.C.GIARDINO,G.I.WELLS,B.J.HAERTLEIN,
JRNL AUTH 3 J.A.KAUFFMAN,T.W.CORCORAN,C.K.DERIAN,A.J.ECKARDT,
JRNL AUTH 4 B.P.DAMIANO,P.ANDRADE-GORDON,B.E.MARYANOFF
JRNL TITL A NOVEL, POTENT DUAL INHIBITOR OF THE LEUKOCYTE PROTEASES
JRNL TITL 2 CATHEPSIN G AND CHYMASE: MOLECULAR MECHANISMS AND
JRNL TITL 3 ANTI-INFLAMMATORY ACTIVITY IN VIVO.
JRNL REF J.BIOL.CHEM. V. 280 18001 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15741158
JRNL DOI 10.1074/JBC.M501302200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.0
REMARK 3 NUMBER OF REFLECTIONS : 19651
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 947
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2329
REMARK 3 BIN FREE R VALUE : 0.3374
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 80
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 : 1755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.10
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20258
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 52.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.26500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1PJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, COBALT
REMARK 280 CHLORIDE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 296.0K
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-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 23.20850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.86650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.20850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.86650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 131.73300
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 902 LIES ON A SPECIAL POSITION.
REMARK 375 O2 SO4 A 902 LIES ON A SPECIAL POSITION.
REMARK 375 CO CO A 909 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1002 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 ND2 ASN A 72 O5 NAG B 1 2.19
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 SER A 36B 14.14 -50.87
REMARK 500 ASN A 36C -25.94 -167.72
REMARK 500 HIS A 71 -66.64 -134.78
REMARK 500 SER A 189 160.63 178.94
REMARK 500 SER A 214 -64.78 -108.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 909 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 25 NE2
REMARK 620 2 HIS A 25 NE2 101.9
REMARK 620 3 GLU A 78 OE2 94.0 92.0
REMARK 620 4 GLU A 78 OE2 92.0 93.9 170.5
REMARK 620 5 HOH A1002 O 129.5 128.6 85.4 85.1
REMARK 620 6 HOH A1002 O 128.6 129.5 85.2 85.4 1.0
REMARK 620 7 HOH A1005 O 79.7 177.9 86.6 87.3 49.8 48.9
REMARK 620 8 HOH A1005 O 177.9 79.7 87.3 86.5 48.9 49.8 98.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PJP RELATED DB: PDB
REMARK 900 THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH
REMARK 900 SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE: STRUCTURAL EXPLANATION
REMARK 900 FOR ITS DIPEPTIDYL CARBOXYPEPTIDASE SPECIFICITY.
DBREF 1T31 A 16 245 UNP P23946 MCT1_HUMAN 22 247
SEQADV 1T31 PHE A 129 UNP P23946 LYS 135 ENGINEERED MUTATION
SEQADV 1T31 ALA A 208 UNP P23946 VAL 212 ENGINEERED MUTATION
SEQADV 1T31 GLN A 235 UNP P23946 ARG 237 ENGINEERED MUTATION
SEQRES 1 A 226 ILE ILE GLY GLY THR GLU CYS LYS PRO HIS SER ARG PRO
SEQRES 2 A 226 TYR MET ALA TYR LEU GLU ILE VAL THR SER ASN GLY PRO
SEQRES 3 A 226 SER LYS PHE CYS GLY GLY PHE LEU ILE ARG ARG ASN PHE
SEQRES 4 A 226 VAL LEU THR ALA ALA HIS CYS ALA GLY ARG SER ILE THR
SEQRES 5 A 226 VAL THR LEU GLY ALA HIS ASN ILE THR GLU GLU GLU ASP
SEQRES 6 A 226 THR TRP GLN LYS LEU GLU VAL ILE LYS GLN PHE ARG HIS
SEQRES 7 A 226 PRO LYS TYR ASN THR SER THR LEU HIS HIS ASP ILE MET
SEQRES 8 A 226 LEU LEU LYS LEU LYS GLU LYS ALA SER LEU THR LEU ALA
SEQRES 9 A 226 VAL GLY THR LEU PRO PHE PRO SER GLN LYS ASN PHE VAL
SEQRES 10 A 226 PRO PRO GLY ARG MET CYS ARG VAL ALA GLY TRP GLY ARG
SEQRES 11 A 226 THR GLY VAL LEU LYS PRO GLY SER ASP THR LEU GLN GLU
SEQRES 12 A 226 VAL LYS LEU ARG LEU MET ASP PRO GLN ALA CYS SER HIS
SEQRES 13 A 226 PHE ARG ASP PHE ASP HIS ASN LEU GLN LEU CYS VAL GLY
SEQRES 14 A 226 ASN PRO ARG LYS THR LYS SER ALA PHE LYS GLY ASP SER
SEQRES 15 A 226 GLY GLY PRO LEU LEU CYS ALA GLY ALA ALA GLN GLY ILE
SEQRES 16 A 226 VAL SER TYR GLY ARG SER ASP ALA LYS PRO PRO ALA VAL
SEQRES 17 A 226 PHE THR ARG ILE SER HIS TYR GLN PRO TRP ILE ASN GLN
SEQRES 18 A 226 ILE LEU GLN ALA ASN
MODRES 1T31 ASN A 72 ASN GLYCOSYLATION SITE
MODRES 1T31 ASN A 95 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG A 302 14
HET SO4 A 902 5
HET SO4 A 903 5
HET SO4 A 904 5
HET SO4 A 905 5
HET SO4 A 906 5
HET SO4 A 907 5
HET SO4 A 908 5
HET CO A 909 1
HET OHH A 901 49
HET MES A 910 12
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM CO COBALT (II) ION
HETNAM OHH 2-[3-({METHYL[1-(2-NAPHTHOYL)PIPERIDIN-4-
HETNAM 2 OHH YL]AMINO}CARBONYL)-2-NAPHTHYL]-1-(1-NAPHTHYL)-2-
HETNAM 3 OHH OXOETHYLPHOSPHONIC ACID
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 4 SO4 7(O4 S 2-)
FORMUL 11 CO CO 2+
FORMUL 12 OHH C40 H35 N2 O6 P
FORMUL 13 MES C6 H13 N O4 S
FORMUL 14 HOH *219(H2 O)
HELIX 1 1 ALA A 55 ALA A 59 5 5
HELIX 2 2 ASP A 164 SER A 169 5 6
HELIX 3 3 TYR A 234 ASN A 245 1 12
SHEET 1 A 8 THR A 20 GLU A 21 0
SHEET 2 A 8 GLN A 156 MET A 163 -1 O GLU A 157 N THR A 20
SHEET 3 A 8 GLN A 180 VAL A 183 -1 O CYS A 182 N MET A 163
SHEET 4 A 8 ALA A 226 ARG A 230 -1 O PHE A 228 N LEU A 181
SHEET 5 A 8 ALA A 208 TYR A 215 -1 N TYR A 215 O VAL A 227
SHEET 6 A 8 PRO A 198 CYS A 201 -1 N LEU A 199 O GLN A 210
SHEET 7 A 8 MET A 135 GLY A 140 -1 N ARG A 137 O LEU A 200
SHEET 8 A 8 GLN A 156 MET A 163 -1 O LEU A 160 N CYS A 136
SHEET 1 B 7 MET A 30 VAL A 36 0
SHEET 2 B 7 LYS A 40 ARG A 48 -1 O LYS A 40 N ILE A 35
SHEET 3 B 7 PHE A 51 THR A 54 -1 O LEU A 53 N PHE A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N THR A 54
SHEET 5 B 7 GLN A 81 ARG A 90 -1 N PHE A 89 O LEU A 105
SHEET 6 B 7 SER A 63 LEU A 68 -1 N VAL A 66 O LEU A 83
SHEET 7 B 7 MET A 30 VAL A 36 -1 N VAL A 36 O SER A 63
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
LINK ND2 ASN A 72 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 95 C1 NAG A 302 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.47
LINK NE2 HIS A 25 CO CO A 909 1555 1555 2.07
LINK NE2 HIS A 25 CO CO A 909 2565 1555 2.07
LINK OE2 GLU A 78 CO CO A 909 1555 1555 2.09
LINK OE2 GLU A 78 CO CO A 909 2565 1555 2.09
LINK CO CO A 909 O HOH A1002 1555 1555 2.75
LINK CO CO A 909 O HOH A1002 1555 2565 2.75
LINK CO CO A 909 O HOH A1005 1555 1555 2.03
LINK CO CO A 909 O HOH A1005 1555 2565 2.03
CISPEP 1 PRO A 224 PRO A 225 0 0.00
CRYST1 46.417 131.733 49.219 90.00 90.00 90.00 P 21 21 2 4
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 0.021544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007591 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020317 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
