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HEADER HYDROLASE 09-MAR-11 3R0V
TITLE THE CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE FROM SPHAEROBACTER
TITLE 2 THERMOPHILUS DSM 20745.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHAEROBACTER THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 479434;
SOURCE 4 STRAIN: DSM 20745 / S 6022;
SOURCE 5 GENE: SPHAEROBACTER THERMOPHILUS, STHE_2971;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE, MCSG,
KEYWDS 2 ALPHA/BETA HYDROLASE, MIDWEST CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,R.WU,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 06-APR-11 3R0V 0
JRNL AUTH K.TAN,R.WU,S.CLANCY,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE FROM
JRNL TITL 2 SPHAEROBACTER THERMOPHILUS DSM 20745.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 42410
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2141
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 37.0892 - 2.9791 1.00 4430 228 0.1495 0.1706
REMARK 3 2 2.9791 - 2.3647 1.00 4252 213 0.1688 0.1901
REMARK 3 3 2.3647 - 2.0658 1.00 4209 226 0.1596 0.1664
REMARK 3 4 2.0658 - 1.8770 1.00 4138 240 0.1565 0.1799
REMARK 3 5 1.8770 - 1.7424 0.99 4141 215 0.1622 0.1744
REMARK 3 6 1.7424 - 1.6397 0.98 4063 221 0.1614 0.2024
REMARK 3 7 1.6397 - 1.5576 0.96 3961 220 0.1637 0.1879
REMARK 3 8 1.5576 - 1.4898 0.94 3899 209 0.1904 0.2369
REMARK 3 9 1.4898 - 1.4324 0.90 3743 192 0.2226 0.2695
REMARK 3 10 1.4324 - 1.3830 0.83 3433 177 0.2570 0.2782
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.61
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 60.23
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.800
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) : 3.49190
REMARK 3 B22 (A**2) : 0.31510
REMARK 3 B33 (A**2) : -3.80700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
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 2043
REMARK 3 ANGLE : 1.178 2815
REMARK 3 CHIRALITY : 0.073 317
REMARK 3 PLANARITY : 0.009 380
REMARK 3 DIHEDRAL : 11.945 762
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8165 10.1777 5.0956
REMARK 3 T TENSOR
REMARK 3 T11: 0.1088 T22: 0.1148
REMARK 3 T33: 0.1128 T12: -0.0034
REMARK 3 T13: 0.0003 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.1188 L22: 0.2175
REMARK 3 L33: 0.0361 L12: 0.0398
REMARK 3 L13: -0.0017 L23: 0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: -0.0054 S13: 0.0086
REMARK 3 S21: 0.0023 S22: -0.0082 S23: 0.0049
REMARK 3 S31: -0.0002 S32: 0.0024 S33: -0.0043
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 3R0V COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44078
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380
REMARK 200 RESOLUTION RANGE LOW (A) : 38.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.72300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1M HEPES:NAOH, 30% (W/V)
REMARK 280 PEG 4000, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 32.61000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.61000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08100
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: 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 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 489 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ARG A 259
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 92 -125.72 53.74
REMARK 500 PRO A 117 45.90 -85.59
REMARK 500 ASN A 231 60.30 -108.94
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 CL A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLT A 264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC100708 RELATED DB: TARGETDB
DBREF 3R0V A 1 259 UNP D1C982 D1C982_SPHTD 1 259
SEQADV 3R0V SER A -2 UNP D1C982 EXPRESSION TAG
SEQADV 3R0V ASN A -1 UNP D1C982 EXPRESSION TAG
SEQADV 3R0V ALA A 0 UNP D1C982 EXPRESSION TAG
SEQRES 1 A 262 SER ASN ALA MSE GLN THR VAL PRO SER SER ASP GLY THR
SEQRES 2 A 262 PRO ILE ALA PHE GLU ARG SER GLY SER GLY PRO PRO VAL
SEQRES 3 A 262 VAL LEU VAL GLY GLY ALA LEU SER THR ARG ALA GLY GLY
SEQRES 4 A 262 ALA PRO LEU ALA GLU ARG LEU ALA PRO HIS PHE THR VAL
SEQRES 5 A 262 ILE OCS TYR ASP ARG ARG GLY ARG GLY ASP SER GLY ASP
SEQRES 6 A 262 THR PRO PRO TYR ALA VAL GLU ARG GLU ILE GLU ASP LEU
SEQRES 7 A 262 ALA ALA ILE ILE ASP ALA ALA GLY GLY ALA ALA PHE VAL
SEQRES 8 A 262 PHE GLY MSE SER SER GLY ALA GLY LEU SER LEU LEU ALA
SEQRES 9 A 262 ALA ALA SER GLY LEU PRO ILE THR ARG LEU ALA VAL PHE
SEQRES 10 A 262 GLU PRO PRO TYR ALA VAL ASP ASP SER ARG PRO PRO VAL
SEQRES 11 A 262 PRO PRO ASP TYR GLN THR ARG LEU ASP ALA LEU LEU ALA
SEQRES 12 A 262 GLU GLY ARG ARG GLY ASP ALA VAL THR TYR PHE MSE THR
SEQRES 13 A 262 GLU GLY VAL GLY VAL PRO PRO ASP LEU VAL ALA GLN MSE
SEQRES 14 A 262 GLN GLN ALA PRO MSE TRP PRO GLY MSE GLU ALA VAL ALA
SEQRES 15 A 262 HIS THR LEU PRO TYR ASP HIS ALA VAL MSE GLY ASP ASN
SEQRES 16 A 262 THR ILE PRO THR ALA ARG PHE ALA SER ILE SER ILE PRO
SEQRES 17 A 262 THR LEU VAL MSE ASP GLY GLY ALA SER PRO ALA TRP ILE
SEQRES 18 A 262 ARG HIS THR ALA GLN GLU LEU ALA ASP THR ILE PRO ASN
SEQRES 19 A 262 ALA ARG TYR VAL THR LEU GLU ASN GLN THR HIS THR VAL
SEQRES 20 A 262 ALA PRO ASP ALA ILE ALA PRO VAL LEU VAL GLU PHE PHE
SEQRES 21 A 262 THR ARG
MODRES 3R0V OCS A 51 CYS CYSTEINESULFONIC ACID
MODRES 3R0V MSE A 91 MET SELENOMETHIONINE
MODRES 3R0V MSE A 152 MET SELENOMETHIONINE
MODRES 3R0V MSE A 166 MET SELENOMETHIONINE
MODRES 3R0V MSE A 171 MET SELENOMETHIONINE
MODRES 3R0V MSE A 175 MET SELENOMETHIONINE
MODRES 3R0V MSE A 189 MET SELENOMETHIONINE
MODRES 3R0V MSE A 209 MET SELENOMETHIONINE
HET OCS A 51 9
HET MSE A 91 13
HET MSE A 152 13
HET MSE A 166 8
HET MSE A 171 8
HET MSE A 175 8
HET MSE A 189 8
HET MSE A 209 8
HET CL A 260 1
HET GOL A 261 6
HET BME A 262 4
HET BME A 263 4
HET MLT A 264 9
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM MLT MALATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 OCS C3 H7 N O5 S
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 CL CL 1-
FORMUL 3 GOL C3 H8 O3
FORMUL 4 BME 2(C2 H6 O S)
FORMUL 6 MLT C4 H5 O5 1-
FORMUL 7 HOH *299(H2 O)
HELIX 1 1 THR A 32 GLY A 35 5 4
HELIX 2 2 GLY A 36 ALA A 44 1 9
HELIX 3 3 ALA A 67 ALA A 82 1 16
HELIX 4 4 SER A 92 SER A 104 1 13
HELIX 5 5 ASP A 130 GLU A 141 1 12
HELIX 6 6 ARG A 143 GLY A 155 1 13
HELIX 7 7 PRO A 159 GLN A 168 1 10
HELIX 8 8 MSE A 171 VAL A 178 1 8
HELIX 9 9 THR A 181 GLY A 190 1 10
HELIX 10 10 PRO A 195 ALA A 200 1 6
HELIX 11 11 PRO A 215 ILE A 229 1 15
HELIX 12 12 ALA A 245 THR A 258 1 14
SHEET 1 A 8 THR A 3 PRO A 5 0
SHEET 2 A 8 PRO A 11 GLY A 18 -1 O ILE A 12 N VAL A 4
SHEET 3 A 8 THR A 48 TYR A 52 -1 O VAL A 49 N SER A 17
SHEET 4 A 8 PRO A 22 VAL A 26 1 N VAL A 23 O THR A 48
SHEET 5 A 8 ALA A 86 MSE A 91 1 O PHE A 89 N VAL A 26
SHEET 6 A 8 ILE A 108 PHE A 114 1 O ALA A 112 N VAL A 88
SHEET 7 A 8 THR A 206 ASP A 210 1 O MSE A 209 N VAL A 113
SHEET 8 A 8 ALA A 232 THR A 236 1 O ARG A 233 N VAL A 208
LINK C ILE A 50 N OCS A 51 1555 1555 1.33
LINK C OCS A 51 N TYR A 52 1555 1555 1.33
LINK C GLY A 90 N MSE A 91 1555 1555 1.33
LINK C MSE A 91 N SER A 92 1555 1555 1.33
LINK C PHE A 151 N MSE A 152 1555 1555 1.33
LINK C MSE A 152 N THR A 153 1555 1555 1.33
LINK C GLN A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N GLN A 167 1555 1555 1.33
LINK C PRO A 170 N MSE A 171 1555 1555 1.33
LINK C MSE A 171 N TRP A 172 1555 1555 1.33
LINK C GLY A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N GLU A 176 1555 1555 1.33
LINK C VAL A 188 N MSE A 189 1555 1555 1.33
LINK C MSE A 189 N GLY A 190 1555 1555 1.33
LINK C VAL A 208 N MSE A 209 1555 1555 1.32
LINK C MSE A 209 N ASP A 210 1555 1555 1.33
CISPEP 1 PRO A 64 PRO A 65 0 1.70
SITE 1 AC1 5 ARG A 143 ARG A 144 GLY A 145 ASP A 146
SITE 2 AC1 5 HOH A 330
SITE 1 AC2 10 ARG A 124 VAL A 127 TYR A 131 PHE A 151
SITE 2 AC2 10 GLY A 155 HIS A 186 ASN A 192 HOH A 291
SITE 3 AC2 10 HOH A 293 HOH A 377
SITE 1 AC3 3 GLN A 2 PHE A 14 ARG A 33
SITE 1 AC4 7 PRO A 195 THR A 196 ALA A 197 HIS A 242
SITE 2 AC4 7 HOH A 406 HOH A 466 HOH A 523
SITE 1 AC5 6 ALA A 29 SER A 92 SER A 93 PRO A 117
SITE 2 AC5 6 PHE A 151 HOH A 437
CRYST1 65.220 72.162 45.066 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 0.015333 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022190 0.00000
TER 1962 THR A 258
MASTER 278 0 13 12 8 0 10 6 2220 1 114 21
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