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HEADER HYDROLASE 09-NOV-21 7Q6Y
TITLE THE X-RAY CRYSTAL STRUCTURE OF CBTAN2, A TANNASE ENZYME FROM
TITLE 2 CLOSTRIDIUM BUTYRICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CBTAN2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BUTYRICUM;
SOURCE 3 ORGANISM_TAXID: 1492;
SOURCE 4 GENE: CBLFYP62_01769, FF104_18625;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS TANNASE, SERINE HYDROLASE, GALLATE, TANNIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.COLEMAN,S.MAZURKEWICH,J.LARSBRINK
REVDAT 1 02-MAR-22 7Q6Y 0
JRNL AUTH T.COLEMAN,S.MAZURKEWICH
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF CBTAN2, A TANNASE ENZYME FROM
JRNL TITL 2 CLOSTRIDIUM BUTYRICUM
JRNL REF J.BIOL.CHEM. 2022
JRNL REFN ESSN 1083-351X
JRNL DOI S0021-9258(22)00198-3
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.510
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
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 46.4500 - 5.3500 1.00 4155 151 0.1805 0.2250
REMARK 3 2 5.3500 - 4.2500 1.00 3992 146 0.1501 0.1965
REMARK 3 3 4.2500 - 3.7100 1.00 3956 143 0.1635 0.2123
REMARK 3 4 3.7100 - 3.3700 1.00 3915 143 0.1836 0.2695
REMARK 3 5 3.3700 - 3.1300 1.00 3905 141 0.1875 0.2484
REMARK 3 6 3.1300 - 2.9400 1.00 3917 146 0.2199 0.2808
REMARK 3 7 2.9400 - 2.8000 1.00 3880 138 0.2260 0.2875
REMARK 3 8 2.8000 - 2.6800 1.00 3890 144 0.2448 0.3346
REMARK 3 9 2.6800 - 2.5700 1.00 3861 146 0.2399 0.2941
REMARK 3 10 2.5700 - 2.4800 1.00 3893 136 0.2597 0.3112
REMARK 3 11 2.4800 - 2.4100 1.00 3883 147 0.2757 0.3138
REMARK 3 12 2.4100 - 2.3400 1.00 3855 131 0.3027 0.3977
REMARK 3 13 2.3400 - 2.2800 1.00 3847 142 0.3289 0.3734
REMARK 3 14 2.2800 - 2.2200 1.00 3843 139 0.3578 0.4015
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.334
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.825
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.34
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 7593
REMARK 3 ANGLE : 0.916 10226
REMARK 3 CHIRALITY : 0.057 1098
REMARK 3 PLANARITY : 0.007 1323
REMARK 3 DIHEDRAL : 17.399 2833
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 7Q6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1292119040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.75-5.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8731
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56815
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 46.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.19600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 2.46300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
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: 4J0C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE DIHYDRATE 0.1 M
REMARK 280 SODIUM ACETATE, PH 5.0 20 % PEG 6,000 25 MG/ML PROTEIN, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298.15K
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 45.33750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.79300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.50150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.79300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.33750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.50150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 VAL A 116
REMARK 465 LYS A 117
REMARK 465 THR A 118
REMARK 465 ASN A 119
REMARK 465 GLU A 120
REMARK 465 PHE A 121
REMARK 465 PHE A 122
REMARK 465 VAL A 123
REMARK 465 GLY A 124
REMARK 465 SER A 125
REMARK 465 LYS A 126
REMARK 465 ALA A 127
REMARK 465 GLY A 128
REMARK 465 GLU A 129
REMARK 465 ILE A 130
REMARK 465 SER A 131
REMARK 465 ASN A 132
REMARK 465 GLU A 133
REMARK 465 ASN A 134
REMARK 465 GLY A 135
REMARK 465 VAL B 116
REMARK 465 LYS B 117
REMARK 465 THR B 118
REMARK 465 ASN B 119
REMARK 465 GLU B 120
REMARK 465 PHE B 121
REMARK 465 PHE B 122
REMARK 465 VAL B 123
REMARK 465 GLY B 124
REMARK 465 SER B 125
REMARK 465 LYS B 126
REMARK 465 ALA B 127
REMARK 465 GLY B 128
REMARK 465 GLU B 129
REMARK 465 ILE B 130
REMARK 465 SER B 131
REMARK 465 ASN B 132
REMARK 465 GLU B 133
REMARK 465 ASN B 134
REMARK 465 GLY B 135
REMARK 465 SER B 321
REMARK 465 THR B 322
REMARK 465 TYR B 323
REMARK 465 LYS B 324
REMARK 465 ILE B 325
REMARK 465 ILE B 326
REMARK 465 ASP B 327
REMARK 465 ASN B 328
REMARK 465 ALA B 329
REMARK 465 ALA B 330
REMARK 465 VAL B 331
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 -123.94 68.65
REMARK 500 CYS A 216 58.35 28.73
REMARK 500 ASP A 327 -64.93 73.32
REMARK 500 ASN A 328 -28.59 71.89
REMARK 500 LYS A 335 47.92 38.95
REMARK 500 ASP A 346 61.93 64.09
REMARK 500 GLU A 347 15.34 50.29
REMARK 500 ASN A 353 99.91 -66.86
REMARK 500 THR A 362 149.33 67.66
REMARK 500 PHE A 393 18.78 -146.02
REMARK 500 ASN A 423 4.24 102.78
REMARK 500 ASN A 424 15.19 -147.60
REMARK 500 THR B 113 71.42 -105.98
REMARK 500 PRO B 142 37.67 -98.58
REMARK 500 SER B 175 -126.76 70.49
REMARK 500 ASP B 204 79.22 -108.66
REMARK 500 CYS B 216 55.97 33.00
REMARK 500 SER B 246 147.45 -175.06
REMARK 500 LYS B 335 -35.68 73.57
REMARK 500 THR B 362 154.59 59.25
REMARK 500 PHE B 370 -45.94 -138.80
REMARK 500 LYS B 376 66.41 -103.22
REMARK 500 THR B 385 -164.54 -120.31
REMARK 500 PHE B 393 16.92 -145.50
REMARK 500 ASN B 424 47.38 -150.36
REMARK 500 PRO B 470 -157.27 -83.12
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7Q6Y A 1 490 UNP A0A6M0U600_CLOBU
DBREF2 7Q6Y A A0A6M0U600 1 490
DBREF1 7Q6Y B 1 490 UNP A0A6M0U600_CLOBU
DBREF2 7Q6Y B A0A6M0U600 1 490
SEQRES 1 A 490 MET LEU ILE PHE ASP ASP LYS ASN TYR LYS VAL ASP THR
SEQRES 2 A 490 CYS ASN ILE ASP GLY ILE SER ILE LYS PHE ARG SER PHE
SEQRES 3 A 490 LYS GLU ILE LEU TYR CYS GLU LYS PRO VAL ASP SER ILE
SEQRES 4 A 490 GLN LYS MET ASN ILE PHE VAL PRO GLU VAL TYR TYR GLU
SEQRES 5 A 490 GLY ASN THR ILE ASN GLY TYR SER LEU HIS THR ALA PRO
SEQRES 6 A 490 ILE PHE MET PRO ASN THR VAL GLY GLY TYR MET PRO GLY
SEQRES 7 A 490 PRO ALA ASP GLU PRO GLY LYS ASP PHE LYS GLY ARG ILE
SEQRES 8 A 490 ASN SER ILE PHE ARG ALA LEU LYS HIS GLY TYR ILE VAL
SEQRES 9 A 490 VAL SER ALA GLY VAL ARG GLY ARG THR SER GLY VAL LYS
SEQRES 10 A 490 THR ASN GLU PHE PHE VAL GLY SER LYS ALA GLY GLU ILE
SEQRES 11 A 490 SER ASN GLU ASN GLY LYS MET VAL GLY ARG ALA PRO ALA
SEQRES 12 A 490 LEU VAL VAL ASP MET LYS ALA ALA ILE ARG TYR LEU ARG
SEQRES 13 A 490 TYR ASN LYS GLY ARG ILE PRO GLY ASN THR GLU CYS ILE
SEQRES 14 A 490 VAL THR ASN GLY THR SER ALA GLY GLY ALA LEU SER ALA
SEQRES 15 A 490 ILE ILE GLY ALA SER GLY ASN SER GLU ASP TYR ASN PRO
SEQRES 16 A 490 TYR LEU LYS GLU ILE GLY ALA ALA ASP GLU ARG ASP ASP
SEQRES 17 A 490 ILE PHE ALA ALA SER CYS TYR CYS PRO ILE HIS ASN LEU
SEQRES 18 A 490 GLU ASN ALA ASP ALA ALA TYR GLU TRP GLN PHE CYS GLY
SEQRES 19 A 490 TYR ASN ASP TYR HIS ARG ILE LYS HIS VAL ARG SER GLU
SEQRES 20 A 490 SER GLY VAL LYS ASN ILE GLN ILE ASP GLY ILE LEU THR
SEQRES 21 A 490 GLU LYS GLN ILE LYS ILE SER GLU GLU LEU LYS ARG LEU
SEQRES 22 A 490 PHE PRO LYS TYR LEU ASN SER LEU LYS LEU LYS ASP SER
SEQRES 23 A 490 SER ASN ASN GLU LEU LEU LEU ASP GLU ASN GLY GLU GLY
SEQRES 24 A 490 SER PHE LYS GLU TYR ILE LYS LYS LEU VAL ILE ASN SER
SEQRES 25 A 490 ALA GLN LYS GLU LEU ASP LEU CYS SER THR TYR LYS ILE
SEQRES 26 A 490 ILE ASP ASN ALA ALA VAL CYS GLY SER LYS ILE ASP GLU
SEQRES 27 A 490 GLN GLU TYR LEU SER ILE GLU ASP GLU LYS VAL VAL ASP
SEQRES 28 A 490 ILE ASN TRP ASP GLY PHE ILE LYS LYS ILE THR ARG MET
SEQRES 29 A 490 LYS VAL ALA PRO ALA PHE ASP ALA LEU ASP LEU LYS SER
SEQRES 30 A 490 PRO GLU ASN GLU GLU PHE GLY THR GLU ALA ILE LYS ALA
SEQRES 31 A 490 LYS HIS PHE THR ALA TYR SER GLN GLU HIS SER GLU VAL
SEQRES 32 A 490 GLU GLY THR LEU ALA ASP PRO LYS ILE ILE LYS LEU LEU
SEQRES 33 A 490 ASN PRO ILE GLU TYR ILE ASN ASN SER ASP THR ALA LYS
SEQRES 34 A 490 TYR TRP ARG VAL ARG HIS GLY ALA PHE ASP ARG ASP ILE
SEQRES 35 A 490 SER LEU ALA MET PRO SER ILE LEU SER LEU THR LEU GLU
SEQRES 36 A 490 ASN ASN GLY TYR VAL VAL ASP PHE SER LEU PRO TRP GLY
SEQRES 37 A 490 ILE PRO HIS SER GLY ASP TYR ASP LEU ASP ASP LEU PHE
SEQRES 38 A 490 ALA TRP ILE ASP GLU ILE TYR THR LYS
SEQRES 1 B 490 MET LEU ILE PHE ASP ASP LYS ASN TYR LYS VAL ASP THR
SEQRES 2 B 490 CYS ASN ILE ASP GLY ILE SER ILE LYS PHE ARG SER PHE
SEQRES 3 B 490 LYS GLU ILE LEU TYR CYS GLU LYS PRO VAL ASP SER ILE
SEQRES 4 B 490 GLN LYS MET ASN ILE PHE VAL PRO GLU VAL TYR TYR GLU
SEQRES 5 B 490 GLY ASN THR ILE ASN GLY TYR SER LEU HIS THR ALA PRO
SEQRES 6 B 490 ILE PHE MET PRO ASN THR VAL GLY GLY TYR MET PRO GLY
SEQRES 7 B 490 PRO ALA ASP GLU PRO GLY LYS ASP PHE LYS GLY ARG ILE
SEQRES 8 B 490 ASN SER ILE PHE ARG ALA LEU LYS HIS GLY TYR ILE VAL
SEQRES 9 B 490 VAL SER ALA GLY VAL ARG GLY ARG THR SER GLY VAL LYS
SEQRES 10 B 490 THR ASN GLU PHE PHE VAL GLY SER LYS ALA GLY GLU ILE
SEQRES 11 B 490 SER ASN GLU ASN GLY LYS MET VAL GLY ARG ALA PRO ALA
SEQRES 12 B 490 LEU VAL VAL ASP MET LYS ALA ALA ILE ARG TYR LEU ARG
SEQRES 13 B 490 TYR ASN LYS GLY ARG ILE PRO GLY ASN THR GLU CYS ILE
SEQRES 14 B 490 VAL THR ASN GLY THR SER ALA GLY GLY ALA LEU SER ALA
SEQRES 15 B 490 ILE ILE GLY ALA SER GLY ASN SER GLU ASP TYR ASN PRO
SEQRES 16 B 490 TYR LEU LYS GLU ILE GLY ALA ALA ASP GLU ARG ASP ASP
SEQRES 17 B 490 ILE PHE ALA ALA SER CYS TYR CYS PRO ILE HIS ASN LEU
SEQRES 18 B 490 GLU ASN ALA ASP ALA ALA TYR GLU TRP GLN PHE CYS GLY
SEQRES 19 B 490 TYR ASN ASP TYR HIS ARG ILE LYS HIS VAL ARG SER GLU
SEQRES 20 B 490 SER GLY VAL LYS ASN ILE GLN ILE ASP GLY ILE LEU THR
SEQRES 21 B 490 GLU LYS GLN ILE LYS ILE SER GLU GLU LEU LYS ARG LEU
SEQRES 22 B 490 PHE PRO LYS TYR LEU ASN SER LEU LYS LEU LYS ASP SER
SEQRES 23 B 490 SER ASN ASN GLU LEU LEU LEU ASP GLU ASN GLY GLU GLY
SEQRES 24 B 490 SER PHE LYS GLU TYR ILE LYS LYS LEU VAL ILE ASN SER
SEQRES 25 B 490 ALA GLN LYS GLU LEU ASP LEU CYS SER THR TYR LYS ILE
SEQRES 26 B 490 ILE ASP ASN ALA ALA VAL CYS GLY SER LYS ILE ASP GLU
SEQRES 27 B 490 GLN GLU TYR LEU SER ILE GLU ASP GLU LYS VAL VAL ASP
SEQRES 28 B 490 ILE ASN TRP ASP GLY PHE ILE LYS LYS ILE THR ARG MET
SEQRES 29 B 490 LYS VAL ALA PRO ALA PHE ASP ALA LEU ASP LEU LYS SER
SEQRES 30 B 490 PRO GLU ASN GLU GLU PHE GLY THR GLU ALA ILE LYS ALA
SEQRES 31 B 490 LYS HIS PHE THR ALA TYR SER GLN GLU HIS SER GLU VAL
SEQRES 32 B 490 GLU GLY THR LEU ALA ASP PRO LYS ILE ILE LYS LEU LEU
SEQRES 33 B 490 ASN PRO ILE GLU TYR ILE ASN ASN SER ASP THR ALA LYS
SEQRES 34 B 490 TYR TRP ARG VAL ARG HIS GLY ALA PHE ASP ARG ASP ILE
SEQRES 35 B 490 SER LEU ALA MET PRO SER ILE LEU SER LEU THR LEU GLU
SEQRES 36 B 490 ASN ASN GLY TYR VAL VAL ASP PHE SER LEU PRO TRP GLY
SEQRES 37 B 490 ILE PRO HIS SER GLY ASP TYR ASP LEU ASP ASP LEU PHE
SEQRES 38 B 490 ALA TRP ILE ASP GLU ILE TYR THR LYS
HET PEG A 501 7
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET PEG A 506 7
HET PEG A 507 7
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 4
HET PEG A 511 7
HET EDO B 501 4
HET EDO B 502 4
HET PEG B 503 7
HET EDO B 504 4
HET EDO B 505 4
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PEG 5(C4 H10 O3)
FORMUL 4 EDO 11(C2 H6 O2)
FORMUL 19 HOH *228(H2 O)
HELIX 1 AA1 VAL A 49 GLY A 53 5 5
HELIX 2 AA2 ASN A 92 GLY A 101 1 10
HELIX 3 AA3 PRO A 142 ASN A 158 1 17
HELIX 4 AA4 SER A 175 SER A 187 1 13
HELIX 5 AA5 SER A 190 ASP A 192 5 3
HELIX 6 AA6 TYR A 193 ILE A 200 1 8
HELIX 7 AA7 ASN A 220 GLU A 222 5 3
HELIX 8 AA8 ASN A 223 CYS A 233 1 11
HELIX 9 AA9 THR A 260 LEU A 281 1 22
HELIX 10 AB1 GLY A 299 ILE A 326 1 28
HELIX 11 AB2 CYS A 332 GLN A 339 5 8
HELIX 12 AB3 ASN A 353 THR A 362 1 10
HELIX 13 AB4 SER A 377 PHE A 383 1 7
HELIX 14 AB5 THR A 394 HIS A 400 1 7
HELIX 15 AB6 ASP A 409 LEU A 415 1 7
HELIX 16 AB7 LEU A 416 TYR A 421 5 6
HELIX 17 AB8 LEU A 444 ASN A 457 1 14
HELIX 18 AB9 ASP A 476 LYS A 490 1 15
HELIX 19 AC1 VAL B 49 GLY B 53 5 5
HELIX 20 AC2 ASN B 92 GLY B 101 1 10
HELIX 21 AC3 PRO B 142 ASN B 158 1 17
HELIX 22 AC4 ASN B 165 GLU B 167 5 3
HELIX 23 AC5 SER B 175 SER B 187 1 13
HELIX 24 AC6 SER B 190 ASP B 192 5 3
HELIX 25 AC7 TYR B 193 ILE B 200 1 8
HELIX 26 AC8 ASN B 220 GLU B 222 5 3
HELIX 27 AC9 ASN B 223 CYS B 233 1 11
HELIX 28 AD1 THR B 260 LEU B 281 1 22
HELIX 29 AD2 GLY B 299 ASP B 318 1 20
HELIX 30 AD3 LYS B 335 GLN B 339 5 5
HELIX 31 AD4 ASN B 353 THR B 362 1 10
HELIX 32 AD5 SER B 377 PHE B 383 1 7
HELIX 33 AD6 THR B 394 HIS B 400 1 7
HELIX 34 AD7 ASP B 409 LEU B 416 1 8
HELIX 35 AD8 ASN B 417 ILE B 422 5 6
HELIX 36 AD9 LEU B 444 ASN B 457 1 14
HELIX 37 AE1 ASP B 476 THR B 489 1 14
SHEET 1 AA1 9 LYS A 10 ILE A 16 0
SHEET 2 AA1 9 ILE A 19 LEU A 30 -1 O PHE A 23 N ASP A 12
SHEET 3 AA1 9 LYS A 41 PRO A 47 -1 O MET A 42 N ILE A 29
SHEET 4 AA1 9 ILE A 103 ALA A 107 -1 O VAL A 104 N PHE A 45
SHEET 5 AA1 9 PRO A 65 PRO A 69 1 N PHE A 67 O ILE A 103
SHEET 6 AA1 9 ASN A 165 THR A 174 1 O VAL A 170 N MET A 68
SHEET 7 AA1 9 ALA A 211 TYR A 215 1 O TYR A 215 N GLY A 173
SHEET 8 AA1 9 TYR A 430 ARG A 434 1 O ARG A 432 N CYS A 214
SHEET 9 AA1 9 VAL A 460 SER A 464 1 O ASP A 462 N TRP A 431
SHEET 1 AA2 2 ASP A 237 ARG A 245 0
SHEET 2 AA2 2 VAL A 250 ILE A 258 -1 O ILE A 253 N LYS A 242
SHEET 1 AA3 2 LEU A 342 GLU A 345 0
SHEET 2 AA3 2 LYS A 348 ILE A 352 -1 O VAL A 350 N SER A 343
SHEET 1 AA4 9 LYS B 10 ILE B 16 0
SHEET 2 AA4 9 ILE B 19 LEU B 30 -1 O SER B 25 N LYS B 10
SHEET 3 AA4 9 LYS B 41 PRO B 47 -1 O MET B 42 N ILE B 29
SHEET 4 AA4 9 ILE B 103 ALA B 107 -1 O VAL B 104 N PHE B 45
SHEET 5 AA4 9 ILE B 66 PRO B 69 1 N PHE B 67 O ILE B 103
SHEET 6 AA4 9 ILE B 169 ASN B 172 1 O VAL B 170 N MET B 68
SHEET 7 AA4 9 ALA B 211 TYR B 215 1 O SER B 213 N THR B 171
SHEET 8 AA4 9 TYR B 430 ARG B 434 1 O ARG B 432 N CYS B 214
SHEET 9 AA4 9 VAL B 460 SER B 464 1 O ASP B 462 N TRP B 431
SHEET 1 AA5 2 ASP B 237 VAL B 244 0
SHEET 2 AA5 2 LYS B 251 ILE B 258 -1 O ILE B 255 N ARG B 240
SHEET 1 AA6 2 LEU B 283 LYS B 284 0
SHEET 2 AA6 2 GLU B 290 LEU B 291 -1 O LEU B 291 N LEU B 283
SHEET 1 AA7 2 LEU B 342 ILE B 344 0
SHEET 2 AA7 2 VAL B 349 ILE B 352 -1 O VAL B 350 N SER B 343
SSBOND 1 CYS A 320 CYS A 332 1555 1555 2.01
SSBOND 2 CYS B 320 CYS B 332 1555 1555 2.01
CISPEP 1 ALA A 141 PRO A 142 0 4.40
CISPEP 2 ALA A 367 PRO A 368 0 -6.60
CISPEP 3 ALA B 141 PRO B 142 0 5.09
CISPEP 4 ALA B 367 PRO B 368 0 -8.28
CRYST1 90.675 95.003 131.586 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 0.011028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010526 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007600 0.00000
TER 3731 LYS A 490
TER 7373 LYS B 490
MASTER 309 0 16 37 28 0 0 6 7660 2 83 76
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