HEADER HYDROLASE 17-MAR-10 3M7U
TITLE CRYSTAL STRUCTURE OF ALPHA-LYTIC PROTEASE SB1+2 R64A/E182Q MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-LYTIC PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MATURE PROTEASE DOMAIN (RESIDUES 1-198);
COMPND 5 SYNONYM: ALPHA-LYTIC ENDOPEPTIDASE;
COMPND 6 EC: 3.4.21.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SELF-PROTEOLYSIS PRODUCT (RESIDUES 184-187);
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYSOBACTER ENZYMOGENES;
SOURCE 3 ORGANISM_TAXID: 69;
SOURCE 4 GENE: ALPHA-LP, LYSOBACTER;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PALP12;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES
KEYWDS HYDROLASE, DISULFIDE BOND, PROTEASE, SERINE PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.AGARD,F.P.ERCIYAS BAILEY,C.A.WADDLING
REVDAT 3 06-SEP-23 3M7U 1 REMARK
REVDAT 2 06-OCT-21 3M7U 1 REMARK SEQADV
REVDAT 1 09-FEB-11 3M7U 0
JRNL AUTH F.P.ERCIYAS BAILEY,C.A.WADDLING,D.A.AGARD
JRNL TITL QUANTIFYING PROTEIN UNFOLDING COOPERATIVITY WITH ACID
JRNL TITL 2 SENSITIVE PROBES: INTERDOMAIN SALT BRIDGE CONTRIBUTIONS TO
JRNL TITL 3 UNFOLDING COOPERATIVITY ARE COMBINED EFFICIENTLY IN
JRNL TITL 4 ALPHA-LYTIC PROTEASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.N.FUHRMANN,B.A.KELCH,N.OTA,D.A.AGARD
REMARK 1 TITL THE 0.83 A RESOLUTION CRYSTAL STRUCTURE OF ALPHA-LYTIC
REMARK 1 TITL 2 PROTEASE REVEALS THE DETAILED STRUCTURE OF THE ACTIVE SITE
REMARK 1 TITL 3 AND IDENTIFIES A SOURCE OF CONFORMATIONAL STRAIN.
REMARK 1 REF J.MOL.BIOL. V. 338 999 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15111063
REMARK 1 DOI 10.1016/J.JMB.2004.03.018
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.D.RADER,D.A.AGARD
REMARK 1 TITL CONFORMATIONAL SUBSTATES IN ENZYME MECHANISM: THE 120 K
REMARK 1 TITL 2 STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.5 A RESOLUTION.
REMARK 1 REF PROTEIN SCI. V. 6 1375 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9232638
REMARK 1 DOI 10.1002/PRO.5560060701
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_328)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 91149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.220
REMARK 3 FREE R VALUE TEST SET COUNT : 2022
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 14.6012 - 2.5273 0.98 6750 153 0.0983 0.1322
REMARK 3 2 2.5273 - 2.0076 0.98 6536 148 0.1061 0.1288
REMARK 3 3 2.0076 - 1.7543 0.98 6496 145 0.1215 0.1580
REMARK 3 4 1.7543 - 1.5942 0.98 6430 148 0.1357 0.1544
REMARK 3 5 1.5942 - 1.4800 0.98 6467 143 0.1430 0.1496
REMARK 3 6 1.4800 - 1.3928 0.98 6410 142 0.1502 0.1621
REMARK 3 7 1.3928 - 1.3231 0.97 6384 147 0.1565 0.1873
REMARK 3 8 1.3231 - 1.2656 0.97 6383 145 0.1696 0.1913
REMARK 3 9 1.2656 - 1.2169 0.97 6332 140 0.1783 0.2156
REMARK 3 10 1.2169 - 1.1749 0.97 6330 142 0.1964 0.2088
REMARK 3 11 1.1749 - 1.1382 0.97 6328 138 0.2193 0.2290
REMARK 3 12 1.1382 - 1.1056 0.95 6235 142 0.2542 0.2495
REMARK 3 13 1.1056 - 1.0766 0.93 6064 138 0.3224 0.3210
REMARK 3 14 1.0766 - 1.0500 0.90 5876 135 0.3919 0.4479
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.42
REMARK 3 B_SOL : 63.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47050
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.47050
REMARK 3 B13 (A**2) : -0.99330
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 : 0.006 1562
REMARK 3 ANGLE : 1.109 2133
REMARK 3 CHIRALITY : 0.066 241
REMARK 3 PLANARITY : 0.004 288
REMARK 3 DIHEDRAL : 13.513 541
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3M7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11588
REMARK 200 MONOCHROMATOR : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91149
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.030
REMARK 200 RESOLUTION RANGE LOW (A) : 46.196
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 33.10
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 118.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 18.10
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
REMARK 200 R SYM FOR SHELL (I) : 0.64400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX DEV_328
REMARK 200 STARTING MODEL: PDB ENTRY 1SSX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M LITHIUM SULFATE, 20 MM TRIS
REMARK 280 SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 53.23733
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 26.61867
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 26.61867
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 53.23733
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: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 211 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 643 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 O HOH A 295 O HOH A 374 2.01
REMARK 500 O HOH A 258 O HOH A 304 2.08
REMARK 500 O HOH A 335 O HOH A 512 2.11
REMARK 500 O HOH A 382 O HOH A 392 2.12
REMARK 500 O HOH A 319 O HOH A 555 2.12
REMARK 500 O HOH A 430 O HOH A 712 2.16
REMARK 500 O HOH A 310 O HOH A 409 2.18
REMARK 500 O HOH A 292 O HOH A 686 2.18
REMARK 500 O HOH A 268 O HOH A 501 2.19
REMARK 500 O HOH A 296 O HOH A 341 2.19
REMARK 500 O HOH A 303 O HOH A 356 2.19
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 456 O HOH A 633 6444 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 ALA A 14 -91.30 -127.88
REMARK 500 ASN A 41 -5.57 85.39
REMARK 500 PRO A 60 -152.73 -77.69
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M7T RELATED DB: PDB
REMARK 900 SB2+3 ALPHA-LYTIC PROTEASE MUTANT AT 1.55A RESOLUTION
REMARK 900 RELATED ID: 1SSX RELATED DB: PDB
REMARK 900 WT ALPHA-LYTIC PROTEASE TO 0.83A RESOLUTION
REMARK 900 RELATED ID: 1TAL RELATED DB: PDB
REMARK 900 WT ALPHA-LYTIC PROTEASE TO 1.5A RESOLUTION
DBREF 3M7U A 1 198 UNP P00778 PRLA_LYSEN 200 397
DBREF 3M7U B 2184 2187 PDB 3M7U 3M7U 2184 2187
SEQADV 3M7U ALA A 64 UNP P00778 ARG 263 ENGINEERED MUTATION
SEQADV 3M7U GLN A 182 UNP P00778 GLU 381 ENGINEERED MUTATION
SEQRES 1 A 198 ALA ASN ILE VAL GLY GLY ILE GLU TYR SER ILE ASN ASN
SEQRES 2 A 198 ALA SER LEU CYS SER VAL GLY PHE SER VAL THR ARG GLY
SEQRES 3 A 198 ALA THR LYS GLY PHE VAL THR ALA GLY HIS CYS GLY THR
SEQRES 4 A 198 VAL ASN ALA THR ALA ARG ILE GLY GLY ALA VAL VAL GLY
SEQRES 5 A 198 THR PHE ALA ALA ARG VAL PHE PRO GLY ASN ASP ALA ALA
SEQRES 6 A 198 TRP VAL SER LEU THR SER ALA GLN THR LEU LEU PRO ARG
SEQRES 7 A 198 VAL ALA ASN GLY SER SER PHE VAL THR VAL ARG GLY SER
SEQRES 8 A 198 THR GLU ALA ALA VAL GLY ALA ALA VAL CYS ARG SER GLY
SEQRES 9 A 198 ARG THR THR GLY TYR GLN CYS GLY THR ILE THR ALA LYS
SEQRES 10 A 198 ASN VAL THR ALA ASN TYR ALA GLU GLY ALA VAL ARG GLY
SEQRES 11 A 198 LEU THR GLN GLY ASN ALA CYS MET GLY ARG GLY ASP SER
SEQRES 12 A 198 GLY GLY SER TRP ILE THR SER ALA GLY GLN ALA GLN GLY
SEQRES 13 A 198 VAL MET SER GLY GLY ASN VAL GLN SER ASN GLY ASN ASN
SEQRES 14 A 198 CYS GLY ILE PRO ALA SER GLN ARG SER SER LEU PHE GLN
SEQRES 15 A 198 ARG LEU GLN PRO ILE LEU SER GLN TYR GLY LEU SER LEU
SEQRES 16 A 198 VAL THR GLY
SEQRES 1 B 4 LEU GLN PRO ILE
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET SO4 A1004 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *527(H2 O)
HELIX 1 1 ALA A 34 GLY A 38 5 5
HELIX 2 2 PRO A 173 ARG A 177 5 5
HELIX 3 3 LEU A 184 GLY A 192 1 9
SHEET 1 A 3 ASN A 2 GLY A 5 0
SHEET 2 A 3 THR A 74 ASN A 81 1 O THR A 74 N ILE A 3
SHEET 3 A 3 SER A 84 THR A 87 -1 O SER A 84 N ASN A 81
SHEET 1 B 8 SER A 15 SER A 18 0
SHEET 2 B 8 GLU A 8 ILE A 11 -1 N TYR A 9 O CYS A 17
SHEET 3 B 8 THR A 43 ILE A 46 -1 O ARG A 45 N SER A 10
SHEET 4 B 8 ALA A 49 VAL A 58 -1 O VAL A 51 N ALA A 44
SHEET 5 B 8 ALA A 64 LEU A 69 -1 O ALA A 64 N VAL A 58
SHEET 6 B 8 THR A 28 THR A 33 -1 N PHE A 31 O VAL A 67
SHEET 7 B 8 PHE A 21 ARG A 25 -1 N ARG A 25 O THR A 28
SHEET 8 B 8 SER A 194 LEU A 195 -1 O SER A 194 N THR A 24
SHEET 1 C 7 ALA A 99 GLY A 104 0
SHEET 2 C 7 GLY A 108 TYR A 123 -1 O GLY A 112 N VAL A 100
SHEET 3 C 7 GLY A 126 GLY A 134 -1 O LEU A 131 N VAL A 119
SHEET 4 C 7 SER A 179 ARG A 183 -1 O SER A 179 N GLY A 134
SHEET 5 C 7 ALA A 154 GLY A 161 -1 N GLY A 160 O LEU A 180
SHEET 6 C 7 SER A 146 ILE A 148 -1 N TRP A 147 O GLN A 155
SHEET 7 C 7 ALA A 99 GLY A 104 -1 N CYS A 101 O ILE A 148
SSBOND 1 CYS A 17 CYS A 37 1555 1555 2.03
SSBOND 2 CYS A 101 CYS A 111 1555 1555 2.04
SSBOND 3 CYS A 137 CYS A 170 1555 1555 2.03
CISPEP 1 PHE A 59 PRO A 60 0 -3.96
SITE 1 AC1 10 ALA A 1 ASN A 2 ARG A 183 PRO A 186
SITE 2 AC1 10 HOH A 240 HOH A 245 HOH A 518 HOH A 553
SITE 3 AC1 10 HOH A 566 HOH A 574
SITE 1 AC2 11 HIS A 36 ARG A 140 GLY A 141 SER A 143
SITE 2 AC2 11 HOH A 218 HOH A 253 HOH A 503 HOH A 541
SITE 3 AC2 11 HOH A 595 HOH A 717 LEU B2184
SITE 1 AC3 10 ALA A 27 THR A 28 ALA A 127 ARG A 129
SITE 2 AC3 10 HOH A 308 HOH A 336 HOH A 543 HOH A 551
SITE 3 AC3 10 HOH A 709 HOH A 714
SITE 1 AC4 10 ALA A 95 VAL A 96 LYS A 117 HOH A 230
SITE 2 AC4 10 HOH A 296 HOH A 341 HOH A 438 HOH A 461
SITE 3 AC4 10 HOH A 470 HOH A 593
CRYST1 65.396 65.396 79.856 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 0.015291 0.008829 0.000000 0.00000
SCALE2 0.000000 0.017657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012523 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
