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HEADER HYDROLASE 26-APR-16 5JKF
TITLE CRYSTAL STRUCTURE OF ESTERASE E22
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE E22;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ESTERASE E32, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,P.WANG,Q.YAO
REVDAT 1 26-APR-17 5JKF 0
JRNL AUTH Y.ZHANG,Q.YAO,P.WANG
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION AND CATALYSIS OF
JRNL TITL 2 A NOVEL ESTERASE E22 WITH A HOMOSERINE TRANSACETYLASE-LIKE
JRNL TITL 3 FOLD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 24105
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1173
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 42.7554 - 4.7838 0.92 3089 151 0.1476 0.1808
REMARK 3 2 4.7838 - 3.7978 0.88 2817 153 0.1352 0.2100
REMARK 3 3 3.7978 - 3.3179 0.89 2805 164 0.1683 0.2430
REMARK 3 4 3.3179 - 3.0146 0.90 2842 132 0.1918 0.3353
REMARK 3 5 3.0146 - 2.7986 0.92 2859 144 0.1997 0.2936
REMARK 3 6 2.7986 - 2.6336 0.92 2843 145 0.2056 0.2760
REMARK 3 7 2.6336 - 2.5018 0.91 2849 147 0.2118 0.2875
REMARK 3 8 2.5018 - 2.3929 0.90 2828 137 0.2213 0.3619
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.550
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) : 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 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 : 0.008 5826
REMARK 3 ANGLE : 0.954 7939
REMARK 3 CHIRALITY : 0.054 893
REMARK 3 PLANARITY : 0.006 1026
REMARK 3 DIHEDRAL : 13.387 3437
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 5JKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24115
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.393
REMARK 200 RESOLUTION RANGE LOW (A) : 42.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 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: 3I1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES (PH 9.5), 16% (W/V) PEG
REMARK 280 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.14750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.70850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.84100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.70850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.14750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.84100
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: 5200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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 ASP A 394
REMARK 465 ASN B 393
REMARK 465 ASP B 394
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 OG SER B 175 O HOH B 401 1.84
REMARK 500 O HOH A 463 O HOH A 481 1.96
REMARK 500 NH2 ARG A 150 O GLY A 316 2.08
REMARK 500 O HOH A 466 O HOH B 476 2.11
REMARK 500 CB MET B 25 O HOH B 482 2.12
REMARK 500 O SER A 166 O HOH A 401 2.12
REMARK 500 O LEU B 221 O HOH B 402 2.13
REMARK 500 NZ LYS B 42 O HOH B 403 2.15
REMARK 500 OD2 ASP B 151 O HOH B 404 2.16
REMARK 500 O ALA A 100 O HOH A 402 2.17
REMARK 500 O HOH A 456 O HOH B 476 2.19
REMARK 500 O HOH A 468 O HOH B 474 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 175 -120.80 67.75
REMARK 500 ILE A 199 48.47 36.28
REMARK 500 LEU A 252 -157.84 -121.10
REMARK 500 VAL A 269 73.46 -101.78
REMARK 500 HIS A 317 42.85 75.03
REMARK 500 GLN A 318 -158.68 -95.36
REMARK 500 ASP A 361 96.65 -61.55
REMARK 500 PRO B 88 -169.21 -79.95
REMARK 500 SER B 175 -118.17 57.70
REMARK 500 ILE B 199 56.16 30.92
REMARK 500 LEU B 252 -153.46 -116.95
REMARK 500 GLN B 318 -159.37 -110.46
REMARK 500 ASP B 361 92.01 -64.13
REMARK 500 VAL B 377 -69.11 -102.62
REMARK 500 ASN B 379 52.73 -142.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JKJ RELATED DB: PDB
DBREF 5JKF A 25 394 PDB 5JKF 5JKF 25 394
DBREF 5JKF B 25 394 PDB 5JKF 5JKF 25 394
SEQRES 1 A 370 MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR
SEQRES 2 A 370 THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY
SEQRES 3 A 370 TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN
SEQRES 4 A 370 VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS
SEQRES 5 A 370 ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY
SEQRES 6 A 370 TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP
SEQRES 7 A 370 THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA
SEQRES 8 A 370 ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY
SEQRES 9 A 370 PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY
SEQRES 10 A 370 LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN
SEQRES 11 A 370 VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS
SEQRES 12 A 370 LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN
SEQRES 13 A 370 ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU
SEQRES 14 A 370 ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA
SEQRES 15 A 370 TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE
SEQRES 16 A 370 THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS
SEQRES 17 A 370 GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET
SEQRES 18 A 370 LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN
SEQRES 19 A 370 GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER
SEQRES 20 A 370 ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL
SEQRES 21 A 370 ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER
SEQRES 22 A 370 MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS
SEQRES 23 A 370 GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN
SEQRES 24 A 370 GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO
SEQRES 25 A 370 ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN
SEQRES 26 A 370 SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER
SEQRES 27 A 370 THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS LEU GLU
SEQRES 28 A 370 GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG
SEQRES 29 A 370 GLN PHE LEU GLU ASN ASP
SEQRES 1 B 370 MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR
SEQRES 2 B 370 THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY
SEQRES 3 B 370 TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN
SEQRES 4 B 370 VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS
SEQRES 5 B 370 ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY
SEQRES 6 B 370 TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP
SEQRES 7 B 370 THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA
SEQRES 8 B 370 ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY
SEQRES 9 B 370 PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY
SEQRES 10 B 370 LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN
SEQRES 11 B 370 VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS
SEQRES 12 B 370 LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN
SEQRES 13 B 370 ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU
SEQRES 14 B 370 ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA
SEQRES 15 B 370 TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE
SEQRES 16 B 370 THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS
SEQRES 17 B 370 GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET
SEQRES 18 B 370 LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN
SEQRES 19 B 370 GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER
SEQRES 20 B 370 ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL
SEQRES 21 B 370 ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER
SEQRES 22 B 370 MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS
SEQRES 23 B 370 GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN
SEQRES 24 B 370 GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO
SEQRES 25 B 370 ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN
SEQRES 26 B 370 SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER
SEQRES 27 B 370 THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS LEU GLU
SEQRES 28 B 370 GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG
SEQRES 29 B 370 GLN PHE LEU GLU ASN ASP
FORMUL 3 HOH *170(H2 O)
HELIX 1 AA1 TYR A 140 PHE A 144 5 5
HELIX 2 AA2 THR A 148 LEU A 163 1 16
HELIX 3 AA3 SER A 175 TYR A 188 1 14
HELIX 4 AA4 PRO A 189 VAL A 192 5 4
HELIX 5 AA5 ASP A 205 ASP A 222 1 18
HELIX 6 AA6 LYS A 223 ALA A 229 5 7
HELIX 7 AA7 SER A 231 ALA A 235 5 5
HELIX 8 AA8 PRO A 236 ALA A 251 1 16
HELIX 9 AA9 THR A 253 LEU A 264 1 12
HELIX 10 AB1 GLU A 270 ASP A 276 1 7
HELIX 11 AB2 HIS A 281 ALA A 295 1 15
HELIX 12 AB3 ASP A 299 LEU A 312 1 14
HELIX 13 AB4 ASN A 320 SER A 327 1 8
HELIX 14 AB5 MET A 344 MET A 358 1 15
HELIX 15 AB6 LEU A 371 HIS A 373 5 3
HELIX 16 AB7 LEU A 374 ASN A 379 1 6
HELIX 17 AB8 VAL A 380 ALA A 382 5 3
HELIX 18 AB9 GLN A 383 GLU A 392 1 10
HELIX 19 AC1 TRP B 91 SER B 93 5 3
HELIX 20 AC2 TYR B 140 PHE B 144 5 5
HELIX 21 AC3 THR B 148 SER B 162 1 15
HELIX 22 AC4 SER B 175 TYR B 188 1 14
HELIX 23 AC5 PRO B 189 VAL B 192 5 4
HELIX 24 AC6 ASP B 205 ASP B 222 1 18
HELIX 25 AC7 LYS B 223 ALA B 229 5 7
HELIX 26 AC8 PRO B 236 ALA B 251 1 16
HELIX 27 AC9 THR B 253 GLY B 265 1 13
HELIX 28 AD1 GLU B 270 ASP B 276 1 7
HELIX 29 AD2 HIS B 281 ALA B 295 1 15
HELIX 30 AD3 ASP B 299 LEU B 312 1 14
HELIX 31 AD4 VAL B 314 GLN B 318 5 5
HELIX 32 AD5 ASN B 320 SER B 327 1 8
HELIX 33 AD6 MET B 344 MET B 358 1 15
HELIX 34 AD7 LEU B 371 HIS B 373 5 3
HELIX 35 AD8 LEU B 374 ASN B 379 1 6
HELIX 36 AD9 VAL B 380 ALA B 382 5 3
HELIX 37 AE1 GLN B 383 GLU B 392 1 10
SHEET 1 AA1 8 ARG A 29 THR A 37 0
SHEET 2 AA1 8 GLN A 43 TYR A 54 -1 O TRP A 51 N ARG A 29
SHEET 3 AA1 8 TYR A 107 VAL A 111 -1 O VAL A 108 N TYR A 54
SHEET 4 AA1 8 VAL A 64 ILE A 67 1 N ILE A 65 O TYR A 107
SHEET 5 AA1 8 ALA A 170 PRO A 174 1 O ILE A 172 N LEU A 66
SHEET 6 AA1 8 ARG A 194 VAL A 198 1 O ILE A 196 N VAL A 171
SHEET 7 AA1 8 LYS A 331 ILE A 335 1 O LEU A 333 N SER A 197
SHEET 8 AA1 8 SER A 362 LEU A 364 1 O THR A 363 N THR A 332
SHEET 1 AA2 2 ILE A 95 GLY A 96 0
SHEET 2 AA2 2 ILE A 101 ASP A 102 1 O ILE A 101 N GLY A 96
SHEET 1 AA3 8 ARG B 29 THR B 37 0
SHEET 2 AA3 8 GLN B 43 TYR B 54 -1 O VAL B 49 N PHE B 31
SHEET 3 AA3 8 TYR B 107 VAL B 111 -1 O VAL B 108 N TYR B 54
SHEET 4 AA3 8 VAL B 64 ILE B 67 1 N ILE B 67 O ILE B 109
SHEET 5 AA3 8 ALA B 170 PRO B 174 1 O ILE B 172 N LEU B 66
SHEET 6 AA3 8 ARG B 194 VAL B 198 1 O ILE B 196 N VAL B 171
SHEET 7 AA3 8 LYS B 331 ILE B 335 1 O ILE B 335 N SER B 197
SHEET 8 AA3 8 SER B 362 LEU B 364 1 O THR B 363 N PHE B 334
SHEET 1 AA4 2 ILE B 95 GLY B 96 0
SHEET 2 AA4 2 ILE B 101 ASP B 102 1 O ILE B 101 N GLY B 96
CRYST1 58.295 67.682 165.417 90.00 90.00 90.00 P 21 21 21 8
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 0.017154 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006045 0.00000
TER 2850 ASN A 393
TER 5684 GLU B 392
MASTER 265 0 0 37 20 0 0 6 5844 2 0 58
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