HEADER HYDROLASE/HYDROLASE INHIBITOR 17-NOV-11 3UOU
TITLE CRYSTAL STRUCTURE OF THE KUNITZ-TYPE PROTEASE INHIBITOR SHPI-1
TITLE 2 LYS13LEU MUTANT IN COMPLEX WITH PANCREATIC ELASTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PEPTIDASE S1 DOMAIN;
COMPND 5 SYNONYM: ELASTASE-1;
COMPND 6 EC: 3.4.21.36;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: KUNITZ-TYPE PROTEINASE INHIBITOR SHPI-1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: KUNITZ-TYPE PROTEINASE INHIBITOR SHPI-1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 OTHER_DETAILS: PANCREAS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: STICHODACTYLA HELIANTHUS;
SOURCE 8 ORGANISM_COMMON: CARRIBEAN SEA ANEMONE;
SOURCE 9 ORGANISM_TAXID: 6123;
SOURCE 10 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAC
KEYWDS PROTEIN-PROTEIN INTERACTION, HYDROLASE (SERINE PROTEASE), KUNITZ-TYPE
KEYWDS 2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GARCIA-FERNANDEZ,M.PERBANDT,D.REHDERS,Y.GONZALEZ-GONZALEZ,
AUTHOR 2 M.A.CHAVEZ,C.BETZEL,L.REDECKE
REVDAT 4 13-SEP-23 3UOU 1 REMARK SEQADV
REVDAT 3 17-JUN-15 3UOU 1 JRNL
REVDAT 2 29-APR-15 3UOU 1 JRNL
REVDAT 1 21-NOV-12 3UOU 0
JRNL AUTH R.GARCIA-FERNANDEZ,M.PERBANDT,D.REHDERS,P.ZIEGELMULLER,
JRNL AUTH 2 N.PIGANEAU,U.HAHN,C.BETZEL,M.A.CHAVEZ,L.REDECKE
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF A KUNITZ-TYPE INHIBITOR IN
JRNL TITL 2 COMPLEX WITH AN ELASTASE-LIKE ENZYME.
JRNL REF J.BIOL.CHEM. V. 290 14154 2015
JRNL REFN ISSN 0021-9258
JRNL PMID 25878249
JRNL DOI 10.1074/JBC.M115.647586
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 17474
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 892
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6501 - 3.6301 1.00 2859 172 0.1474 0.1767
REMARK 3 2 3.6301 - 2.8821 1.00 2824 143 0.1614 0.1884
REMARK 3 3 2.8821 - 2.5180 1.00 2790 133 0.1681 0.2309
REMARK 3 4 2.5180 - 2.2879 0.99 2795 157 0.1765 0.2517
REMARK 3 5 2.2879 - 2.1239 0.99 2746 150 0.1820 0.2495
REMARK 3 6 2.1239 - 2.0000 0.91 2568 137 0.2072 0.2692
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 42.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.48630
REMARK 3 B22 (A**2) : 13.20110
REMARK 3 B33 (A**2) : -1.44170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.62440
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2444
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : 0.072 366
REMARK 3 PLANARITY : 0.004 423
REMARK 3 DIHEDRAL : 13.321 861
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1250 3.2727 9.9495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0615 T22: 0.0698
REMARK 3 T33: 0.0617 T12: 0.0159
REMARK 3 T13: 0.0004 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.8243 L22: 0.6213
REMARK 3 L33: 1.0128 L12: 0.0305
REMARK 3 L13: -0.1520 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: 0.1055 S13: 0.0248
REMARK 3 S21: -0.0476 S22: 0.0202 S23: -0.0042
REMARK 3 S31: -0.0946 S32: -0.0007 S33: -0.0321
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000069023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.81
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17481
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.647
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 1QNJ, PDB ENTRY 3OFW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.425M AMMONIUM SULFATE, 0.085M TRI
REMARK 280 -SODIUM CITRATE, 0.85M LITHIUM SULFATE, 15% GLYCEROL, PH 5.6,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 66.37500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.37500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.59000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 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 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 HOH A 428 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA B 55
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 142 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 27 CG CD CE NZ
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 SG CYS B 3 CB CYS B 53 1.89
REMARK 500 O GLN A 90 O HOH A 436 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 347 O HOH A 347 2556 2.09
REMARK 500 O HOH A 427 O HOH A 427 2556 2.12
REMARK 500 O HOH A 434 O HOH B 217 1545 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 SER A 51 -156.64 -108.61
REMARK 500 HIS A 86 -58.59 -134.39
REMARK 500 ASP A 113 75.95 -154.67
REMARK 500 TYR A 189 -110.70 -95.64
REMARK 500 ASN B 39 -156.64 -108.05
REMARK 500 CYS B 53 77.79 -156.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 58
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 271
DBREF 3UOU A 27 266 UNP P00772 CELA1_PIG 27 266
DBREF 3UOU B 1 55 UNP P31713 ISH1_STOHE 1 55
SEQADV 3UOU LEU B 13 UNP P31713 LYS 13 ENGINEERED MUTATION
SEQRES 1 A 240 VAL VAL GLY GLY THR GLU ALA GLN ARG ASN SER TRP PRO
SEQRES 2 A 240 SER GLN ILE SER LEU GLN TYR ARG SER GLY SER SER TRP
SEQRES 3 A 240 ALA HIS THR CYS GLY GLY THR LEU ILE ARG GLN ASN TRP
SEQRES 4 A 240 VAL MET THR ALA ALA HIS CYS VAL ASP ARG GLU LEU THR
SEQRES 5 A 240 PHE ARG VAL VAL VAL GLY GLU HIS ASN LEU ASN GLN ASN
SEQRES 6 A 240 ASP GLY THR GLU GLN TYR VAL GLY VAL GLN LYS ILE VAL
SEQRES 7 A 240 VAL HIS PRO TYR TRP ASN THR ASP ASP VAL ALA ALA GLY
SEQRES 8 A 240 TYR ASP ILE ALA LEU LEU ARG LEU ALA GLN SER VAL THR
SEQRES 9 A 240 LEU ASN SER TYR VAL GLN LEU GLY VAL LEU PRO ARG ALA
SEQRES 10 A 240 GLY THR ILE LEU ALA ASN ASN SER PRO CYS TYR ILE THR
SEQRES 11 A 240 GLY TRP GLY LEU THR ARG THR ASN GLY GLN LEU ALA GLN
SEQRES 12 A 240 THR LEU GLN GLN ALA TYR LEU PRO THR VAL ASP TYR ALA
SEQRES 13 A 240 ILE CYS SER SER SER SER TYR TRP GLY SER THR VAL LYS
SEQRES 14 A 240 ASN SER MET VAL CYS ALA GLY GLY ASP GLY VAL ARG SER
SEQRES 15 A 240 GLY CYS GLN GLY ASP SER GLY GLY PRO LEU HIS CYS LEU
SEQRES 16 A 240 VAL ASN GLY GLN TYR ALA VAL HIS GLY VAL THR SER PHE
SEQRES 17 A 240 VAL SER ARG LEU GLY CYS ASN VAL THR ARG LYS PRO THR
SEQRES 18 A 240 VAL PHE THR ARG VAL SER ALA TYR ILE SER TRP ILE ASN
SEQRES 19 A 240 ASN VAL ILE ALA SER ASN
SEQRES 1 B 55 SER ILE CYS SER GLU PRO LYS LYS VAL GLY ARG CYS LEU
SEQRES 2 B 55 GLY TYR PHE PRO ARG PHE TYR PHE ASP SER GLU THR GLY
SEQRES 3 B 55 LYS CYS THR PRO PHE ILE TYR GLY GLY CYS GLY GLY ASN
SEQRES 4 B 55 GLY ASN ASN PHE GLU THR LEU HIS GLN CYS ARG ALA ILE
SEQRES 5 B 55 CYS ARG ALA
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 3 5
HET SO4 A 4 5
HET SO4 A 6 5
HET SO4 A 7 5
HET GOL A 267 6
HET GOL A 268 6
HET GOL A 269 6
HET GOL A 5 6
HET GOL A 270 6
HET GOL A 271 6
HET SO4 B 56 5
HET SO4 B 57 5
HET GOL B 58 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 9 GOL 7(C3 H8 O3)
FORMUL 18 HOH *206(H2 O)
HELIX 1 1 ALA A 69 ASP A 74 1 6
HELIX 2 2 ASP A 113 GLY A 117 5 5
HELIX 3 3 ASP A 180 SER A 185 1 6
HELIX 4 4 TRP A 190 VAL A 194 5 5
HELIX 5 5 TYR A 255 ASN A 266 1 12
HELIX 6 6 THR B 45 CYS B 53 1 9
SHEET 1 A 8 THR A 31 GLU A 32 0
SHEET 2 A 8 GLN A 172 TYR A 175 -1 O GLN A 173 N THR A 31
SHEET 3 A 8 CYS A 153 GLY A 157 -1 N ILE A 155 O ALA A 174
SHEET 4 A 8 PRO A 217 VAL A 222 -1 O HIS A 219 N TYR A 154
SHEET 5 A 8 GLN A 225 PHE A 234 -1 O ALA A 227 N CYS A 220
SHEET 6 A 8 THR A 247 ARG A 251 -1 O THR A 250 N VAL A 231
SHEET 7 A 8 MET A 198 ALA A 201 -1 N VAL A 199 O PHE A 249
SHEET 8 A 8 THR A 178 VAL A 179 -1 N VAL A 179 O CYS A 200
SHEET 1 B 7 GLN A 41 SER A 48 0
SHEET 2 B 7 SER A 51 ARG A 62 -1 O CYS A 56 N LEU A 44
SHEET 3 B 7 TRP A 65 THR A 68 -1 O MET A 67 N THR A 59
SHEET 4 B 7 ALA A 121 LEU A 125 -1 O LEU A 123 N VAL A 66
SHEET 5 B 7 GLN A 96 VAL A 105 -1 N VAL A 104 O LEU A 122
SHEET 6 B 7 PHE A 79 VAL A 83 -1 N VAL A 81 O VAL A 98
SHEET 7 B 7 GLN A 41 SER A 48 -1 N GLN A 45 O ARG A 80
SHEET 1 C 2 PHE B 16 PHE B 21 0
SHEET 2 C 2 CYS B 28 TYR B 33 -1 O TYR B 33 N PHE B 16
SSBOND 1 CYS A 56 CYS A 72 1555 1555 2.04
SSBOND 2 CYS A 153 CYS A 220 1555 1555 2.05
SSBOND 3 CYS A 184 CYS A 200 1555 1555 2.04
SSBOND 4 CYS A 210 CYS A 240 1555 1555 2.03
SSBOND 5 CYS B 3 CYS B 53 1555 1555 2.03
SSBOND 6 CYS B 12 CYS B 36 1555 1555 2.03
SSBOND 7 CYS B 28 CYS B 49 1555 1555 2.02
SITE 1 AC1 5 ARG A 62 SER A 236 ARG A 237 HOH A 398
SITE 2 AC1 5 ARG B 11
SITE 1 AC2 5 GLY A 144 ARG A 251 SER A 253 ALA A 254
SITE 2 AC2 5 HOH A 350
SITE 1 AC3 4 ARG A 75 ARG B 18 TYR B 33 GLY B 35
SITE 1 AC4 3 ALA A 115 THR A 193 ARG B 11
SITE 1 AC5 6 LYS B 8 ARG B 11 HOH B 59 HOH B 72
SITE 2 AC5 6 HOH B 101 HOH B 178
SITE 1 AC6 9 HOH A 24 GLN A 63 SER A 128 ARG A 237
SITE 2 AC6 9 HOH A 279 HOH A 306 LYS B 8 VAL B 9
SITE 3 AC6 9 GLY B 10
SITE 1 AC7 4 ARG A 162 GLN A 166 ARG A 207 HOH A 372
SITE 1 AC8 3 ARG A 237 LYS B 8 HOH B 206
SITE 1 AC9 4 TYR A 46 PHE B 16 PRO B 17 ARG B 18
SITE 1 BC1 4 SER A 186 SER A 187 SER A 188 ARG B 50
SITE 1 BC2 4 LYS A 195 ASN A 196 SER A 197 HOH A 337
SITE 1 BC3 5 GLU A 32 ALA A 33 GLN A 34 ARG A 35
SITE 2 BC3 5 ARG A 244
SITE 1 BC4 7 LEU A 88 ASN A 89 LEU A 167 ALA A 168
SITE 2 BC4 7 GLN A 169 HOH A 284 HOH A 357
SITE 1 BC5 3 ARG A 80 TYR A 97 HOH A 326
SITE 1 BC6 3 SER A 187 GLY A 191 SER A 192
CRYST1 132.750 47.180 42.680 90.00 100.07 90.00 C 1 2 1 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 0.007533 0.000000 0.001338 0.00000
SCALE2 0.000000 0.021195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023797 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
