HEADER HYDROLASE/HYDROLASE INHIBITOR 18-NOV-11 3UPE
TITLE BOVINE TRYPSIN VARIANT X(TRIPLEPHE227) IN COMPLEX WITH SMALL MOLECULE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN, ALPHA-TRYPSIN CHAIN 1, ALPHA-TRYPSIN CHAIN 2;
COMPND 5 EC: 3.4.21.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS TRYPSIN-LIKE SERINE PROTEASE, HYDROLASE, PROTEIN BINDING, DUODENUM,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TZIRIDIS,P.NEUMANN,P.KOLENKO,M.T.STUBBS
REVDAT 3 13-SEP-23 3UPE 1 REMARK SEQADV LINK
REVDAT 2 16-JUL-14 3UPE 1 JRNL
REVDAT 1 21-NOV-12 3UPE 0
JRNL AUTH A.TZIRIDIS,D.RAUH,P.NEUMANN,P.KOLENKO,A.MENZEL,U.BRAUER,
JRNL AUTH 2 C.URSEL,P.STEINMETZER,J.STURZEBECHER,A.SCHWEINITZ,
JRNL AUTH 3 T.STEINMETZER,M.T.STUBBS
JRNL TITL CORRELATING STRUCTURE AND LIGAND AFFINITY IN DRUG DISCOVERY:
JRNL TITL 2 A CAUTIONARY TALE INVOLVING SECOND SHELL RESIDUES.
JRNL REF BIOL.CHEM. V. 395 891 2014
JRNL REFN ISSN 1431-6730
JRNL PMID 25003390
JRNL DOI 10.1515/HSZ-2014-0158
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 3 NUMBER OF REFLECTIONS : 32852
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 + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1694
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 602
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 20.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.5480
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.6100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1790 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2450 ; 1.430 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 241 ; 6.512 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 62 ;38.856 ;25.645
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 283 ;11.203 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;15.301 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 266 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1350 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1134 ; 0.775 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1828 ; 1.348 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 656 ; 2.075 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 614 ; 3.190 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3UPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32874
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 22.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.56
REMARK 200 R MERGE FOR SHELL (I) : 0.19500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1V2K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 0.1M AMMONIUM SULPHATE,
REMARK 280 0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.25800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.62900
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.62900
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 103.25800
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 O HOH A 1350 O HOH A 1363 2.16
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 ASP A 71 -79.90 -117.42
REMARK 500 ASN A 115 -169.84 -164.70
REMARK 500 SER A 195 131.67 -34.38
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 CA A 480 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 91.2
REMARK 620 3 VAL A 75 O 164.6 83.2
REMARK 620 4 GLU A 80 OE2 102.5 160.3 86.7
REMARK 620 5 HOH A1001 O 88.8 91.4 105.6 75.1
REMARK 620 6 HOH A1090 O 77.5 104.0 89.9 92.8 159.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0CA A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V2K RELATED DB: PDB
REMARK 900 RELATED ID: 3UNQ RELATED DB: PDB
REMARK 900 RELATED ID: 3UNS RELATED DB: PDB
REMARK 900 RELATED ID: 3UNP RELATED DB: PDB
REMARK 900 RELATED ID: 3UQO RELATED DB: PDB
REMARK 900 RELATED ID: 3UQV RELATED DB: PDB
REMARK 900 RELATED ID: 3UQZ RELATED DB: PDB
DBREF 3UPE A 16 245 UNP P00760 TRY1_BOVIN 24 246
SEQADV 3UPE GLU A 97 UNP P00760 ASN 102 ENGINEERED MUTATION
SEQADV 3UPE TYR A 99 UNP P00760 LEU 104 ENGINEERED MUTATION
SEQADV 3UPE SER A 172 UNP P00760 TYR 175 ENGINEERED MUTATION
SEQADV 3UPE SER A 173 UNP P00760 PRO 176 ENGINEERED MUTATION
SEQADV 3UPE PHE A 174 UNP P00760 GLY 177 ENGINEERED MUTATION
SEQADV 3UPE ILE A 175 UNP P00760 GLN 178 ENGINEERED MUTATION
SEQADV 3UPE ALA A 190 UNP P00760 SER 195 ENGINEERED MUTATION
SEQADV 3UPE PHE A 227 UNP P00760 VAL 228 ENGINEERED MUTATION
SEQADV 3UPE LEU A 231 UNP P00760 VAL 232 ENGINEERED MUTATION
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 GLU THR TYR ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA SER SER PHE ILE ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP ALA CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY PHE TYR THR LYS
SEQRES 17 A 223 LEU CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 480 1
HET 0CA A 481 39
HET SO4 A 483 5
HET SO4 A 484 5
HET GOL A 485 6
HETNAM CA CALCIUM ION
HETNAM 0CA 1-[(7-CARBAMIMIDOYLNAPHTHALEN-2-YL)METHYL]-6-({1-[(1Z)-
HETNAM 2 0CA ETHANIMIDOYL]PIPERIDIN-4-YL}OXY)-2-(PROPAN-2-YL)-1H-
HETNAM 3 0CA INDOLE-4-CARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA CA 2+
FORMUL 3 0CA C31 H35 N5 O3
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *379(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 SER A 172 1 9
HELIX 3 3 TYR A 234 SER A 244 1 11
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 A 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 A 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 O PHE A 227 N TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N SER A 54
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.06
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.05
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.05
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.02
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.02
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.05
LINK OE1 GLU A 70 CA CA A 480 1555 1555 2.30
LINK O ASN A 72 CA CA A 480 1555 1555 2.22
LINK O VAL A 75 CA CA A 480 1555 1555 2.25
LINK OE2 GLU A 80 CA CA A 480 1555 1555 2.33
LINK CA CA A 480 O HOH A1001 1555 1555 2.30
LINK CA CA A 480 O HOH A1090 1555 1555 2.35
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A1001 HOH A1090
SITE 1 AC2 20 GLU A 97 TYR A 99 PHE A 174 ASP A 189
SITE 2 AC2 20 ALA A 190 GLN A 192 SER A 195 TRP A 215
SITE 3 AC2 20 GLY A 216 SER A 217 GLY A 219 CYS A 220
SITE 4 AC2 20 GLY A 226 HOH A1011 HOH A1024 HOH A1118
SITE 5 AC2 20 HOH A1121 HOH A1126 HOH A1151 HOH A1202
SITE 1 AC3 4 THR A 177 SER A 178 LYS A 188A HOH A1139
SITE 1 AC4 5 ASN A 95 ASN A 100 HOH A1124 HOH A1226
SITE 2 AC4 5 HOH A1289
SITE 1 AC5 5 GLU A 80 PHE A 82 HOH A1164 HOH A1188
SITE 2 AC5 5 HOH A1229
CRYST1 54.644 54.644 154.887 90.00 90.00 120.00 P 32 2 1 6
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 0.018300 0.010566 0.000000 0.00000
SCALE2 0.000000 0.021131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006456 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
