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HEADER HYDROLASE 23-JUL-22 7YKQ
TITLE CRYSTAL STRUCTURE OF A NOVEL ALPHA/BETA HYDROLASE MUTANT FROM
TITLE 2 THERMOMONOSPORA CURVATA IN APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMONOSPORA CURVATA DSM 43183;
SOURCE 3 ORGANISM_TAXID: 471852;
SOURCE 4 GENE: TCUR_1278;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC, PET, DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,G.JIAN,U.T.BORNSCHEUER,R.WEI,W.LIU
REVDAT 1 26-JUL-23 7YKQ 0
JRNL AUTH X.HAN,G.JIAN,U.T.BORNSCHEUER,R.WEI,W.LIU
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL ALPHA/BETA HYDROLASE MUTANT
JRNL TITL 2 FROM THERMOMONOSPORA CURVATA IN APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 40088
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2009
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 45.3400 - 5.0900 0.98 3932 214 0.2062 0.2355
REMARK 3 2 5.0900 - 4.0400 1.00 3923 203 0.1830 0.2186
REMARK 3 3 4.0400 - 3.5300 1.00 3912 205 0.1943 0.2250
REMARK 3 4 3.5300 - 3.2100 1.00 3883 205 0.2001 0.2487
REMARK 3 5 3.2100 - 2.9800 1.00 3910 203 0.2200 0.2682
REMARK 3 6 2.9800 - 2.8000 1.00 3861 203 0.2181 0.2380
REMARK 3 7 2.8000 - 2.6600 1.00 3872 197 0.2239 0.2562
REMARK 3 8 2.6600 - 2.5500 1.00 3866 204 0.2414 0.2929
REMARK 3 9 2.5500 - 2.4500 1.00 3842 203 0.2440 0.2964
REMARK 3 10 2.4500 - 2.3600 0.80 3078 172 0.2542 0.3094
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 : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.28
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 3172
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 3172
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 3172
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7YKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1300031085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40804
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.00
REMARK 200 R MERGE (I) : 0.30900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 1.19400
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: 1JFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1M HEPES PH 7.5, 10%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.79650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ASN A -8
REMARK 465 SER A -7
REMARK 465 MET A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 1
REMARK 465 ASN B -8
REMARK 465 SER B -7
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 ALA B 1
REMARK 465 ASN C -8
REMARK 465 SER C -7
REMARK 465 MET C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 ALA C 1
REMARK 465 ASN D -8
REMARK 465 SER D -7
REMARK 465 MET D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 ALA D 1
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 130 -123.00 62.56
REMARK 500 HIS A 184 -70.91 -121.72
REMARK 500 PRO A 242 155.11 -48.33
REMARK 500 SER A 247 -154.69 -140.65
REMARK 500 ASP B 93 126.98 -31.64
REMARK 500 SER B 130 -121.18 61.26
REMARK 500 HIS B 184 -69.92 -124.06
REMARK 500 THR B 196 -44.07 72.26
REMARK 500 SER C 130 -122.68 62.61
REMARK 500 HIS C 184 -70.89 -123.51
REMARK 500 SER C 247 -154.95 -143.15
REMARK 500 SER D 130 -121.98 61.91
REMARK 500 HIS D 184 -72.20 -122.61
REMARK 500 ARG D 228 -78.29 -55.29
REMARK 500 SER D 247 -151.96 -143.83
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7YKQ A 1 260 UNP D1A9G5 D1A9G5_THECD 30 289
DBREF 7YKQ B 1 260 UNP D1A9G5 D1A9G5_THECD 30 289
DBREF 7YKQ C 1 260 UNP D1A9G5 D1A9G5_THECD 30 289
DBREF 7YKQ D 1 260 UNP D1A9G5 D1A9G5_THECD 30 289
SEQADV 7YKQ ASN A -8 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ SER A -7 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ MET A -6 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A -5 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A -4 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A -3 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A -2 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A -1 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS A 0 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ ALA A 13 UNP D1A9G5 SER 42 ENGINEERED MUTATION
SEQADV 7YKQ SER A 14 UNP D1A9G5 LEU 43 ENGINEERED MUTATION
SEQADV 7YKQ PRO A 18 UNP D1A9G5 ALA 47 ENGINEERED MUTATION
SEQADV 7YKQ THR A 41 UNP D1A9G5 ARG 70 ENGINEERED MUTATION
SEQADV 7YKQ ASP A 47 UNP D1A9G5 THR 76 ENGINEERED MUTATION
SEQADV 7YKQ TYR A 92 UNP D1A9G5 LEU 121 ENGINEERED MUTATION
SEQADV 7YKQ ASP A 117 UNP D1A9G5 ASN 146 ENGINEERED MUTATION
SEQADV 7YKQ ARG A 141 UNP D1A9G5 LYS 170 ENGINEERED MUTATION
SEQADV 7YKQ ARG A 142 UNP D1A9G5 SER 171 ENGINEERED MUTATION
SEQADV 7YKQ PRO A 144 UNP D1A9G5 THR 173 ENGINEERED MUTATION
SEQADV 7YKQ THR A 165 UNP D1A9G5 ARG 194 ENGINEERED MUTATION
SEQADV 7YKQ ASN A 175 UNP D1A9G5 LEU 204 ENGINEERED MUTATION
SEQADV 7YKQ ALA A 185 UNP D1A9G5 SER 214 ENGINEERED MUTATION
SEQADV 7YKQ THR A 196 UNP D1A9G5 ARG 225 ENGINEERED MUTATION
SEQADV 7YKQ GLY A 205 UNP D1A9G5 ASN 234 ENGINEERED MUTATION
SEQADV 7YKQ THR A 213 UNP D1A9G5 PHE 242 ENGINEERED MUTATION
SEQADV 7YKQ PRO A 214 UNP D1A9G5 SER 243 ENGINEERED MUTATION
SEQADV 7YKQ ALA A 224 UNP D1A9G5 SER 253 ENGINEERED MUTATION
SEQADV 7YKQ PRO A 246 UNP D1A9G5 ALA 275 ENGINEERED MUTATION
SEQADV 7YKQ SER A 247 UNP D1A9G5 ILE 276 ENGINEERED MUTATION
SEQADV 7YKQ GLU A 252 UNP D1A9G5 ASP 281 ENGINEERED MUTATION
SEQADV 7YKQ ASN B -8 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ SER B -7 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ MET B -6 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B -5 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B -4 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B -3 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B -2 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B -1 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS B 0 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ ALA B 13 UNP D1A9G5 SER 42 ENGINEERED MUTATION
SEQADV 7YKQ SER B 14 UNP D1A9G5 LEU 43 ENGINEERED MUTATION
SEQADV 7YKQ PRO B 18 UNP D1A9G5 ALA 47 ENGINEERED MUTATION
SEQADV 7YKQ THR B 41 UNP D1A9G5 ARG 70 ENGINEERED MUTATION
SEQADV 7YKQ ASP B 47 UNP D1A9G5 THR 76 ENGINEERED MUTATION
SEQADV 7YKQ TYR B 92 UNP D1A9G5 LEU 121 ENGINEERED MUTATION
SEQADV 7YKQ ASP B 117 UNP D1A9G5 ASN 146 ENGINEERED MUTATION
SEQADV 7YKQ ARG B 141 UNP D1A9G5 LYS 170 ENGINEERED MUTATION
SEQADV 7YKQ ARG B 142 UNP D1A9G5 SER 171 ENGINEERED MUTATION
SEQADV 7YKQ PRO B 144 UNP D1A9G5 THR 173 ENGINEERED MUTATION
SEQADV 7YKQ THR B 165 UNP D1A9G5 ARG 194 ENGINEERED MUTATION
SEQADV 7YKQ ASN B 175 UNP D1A9G5 LEU 204 ENGINEERED MUTATION
SEQADV 7YKQ ALA B 185 UNP D1A9G5 SER 214 ENGINEERED MUTATION
SEQADV 7YKQ THR B 196 UNP D1A9G5 ARG 225 ENGINEERED MUTATION
SEQADV 7YKQ GLY B 205 UNP D1A9G5 ASN 234 ENGINEERED MUTATION
SEQADV 7YKQ THR B 213 UNP D1A9G5 PHE 242 ENGINEERED MUTATION
SEQADV 7YKQ PRO B 214 UNP D1A9G5 SER 243 ENGINEERED MUTATION
SEQADV 7YKQ ALA B 224 UNP D1A9G5 SER 253 ENGINEERED MUTATION
SEQADV 7YKQ PRO B 246 UNP D1A9G5 ALA 275 ENGINEERED MUTATION
SEQADV 7YKQ SER B 247 UNP D1A9G5 ILE 276 ENGINEERED MUTATION
SEQADV 7YKQ GLU B 252 UNP D1A9G5 ASP 281 ENGINEERED MUTATION
SEQADV 7YKQ ASN C -8 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ SER C -7 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ MET C -6 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C -5 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C -4 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C -3 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C -2 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C -1 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS C 0 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ ALA C 13 UNP D1A9G5 SER 42 ENGINEERED MUTATION
SEQADV 7YKQ SER C 14 UNP D1A9G5 LEU 43 ENGINEERED MUTATION
SEQADV 7YKQ PRO C 18 UNP D1A9G5 ALA 47 ENGINEERED MUTATION
SEQADV 7YKQ THR C 41 UNP D1A9G5 ARG 70 ENGINEERED MUTATION
SEQADV 7YKQ ASP C 47 UNP D1A9G5 THR 76 ENGINEERED MUTATION
SEQADV 7YKQ TYR C 92 UNP D1A9G5 LEU 121 ENGINEERED MUTATION
SEQADV 7YKQ ASP C 117 UNP D1A9G5 ASN 146 ENGINEERED MUTATION
SEQADV 7YKQ ARG C 141 UNP D1A9G5 LYS 170 ENGINEERED MUTATION
SEQADV 7YKQ ARG C 142 UNP D1A9G5 SER 171 ENGINEERED MUTATION
SEQADV 7YKQ PRO C 144 UNP D1A9G5 THR 173 ENGINEERED MUTATION
SEQADV 7YKQ THR C 165 UNP D1A9G5 ARG 194 ENGINEERED MUTATION
SEQADV 7YKQ ASN C 175 UNP D1A9G5 LEU 204 ENGINEERED MUTATION
SEQADV 7YKQ ALA C 185 UNP D1A9G5 SER 214 ENGINEERED MUTATION
SEQADV 7YKQ THR C 196 UNP D1A9G5 ARG 225 ENGINEERED MUTATION
SEQADV 7YKQ GLY C 205 UNP D1A9G5 ASN 234 ENGINEERED MUTATION
SEQADV 7YKQ THR C 213 UNP D1A9G5 PHE 242 ENGINEERED MUTATION
SEQADV 7YKQ PRO C 214 UNP D1A9G5 SER 243 ENGINEERED MUTATION
SEQADV 7YKQ ALA C 224 UNP D1A9G5 SER 253 ENGINEERED MUTATION
SEQADV 7YKQ PRO C 246 UNP D1A9G5 ALA 275 ENGINEERED MUTATION
SEQADV 7YKQ SER C 247 UNP D1A9G5 ILE 276 ENGINEERED MUTATION
SEQADV 7YKQ GLU C 252 UNP D1A9G5 ASP 281 ENGINEERED MUTATION
SEQADV 7YKQ ASN D -8 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ SER D -7 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ MET D -6 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D -5 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D -4 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D -3 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D -2 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D -1 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ HIS D 0 UNP D1A9G5 EXPRESSION TAG
SEQADV 7YKQ ALA D 13 UNP D1A9G5 SER 42 ENGINEERED MUTATION
SEQADV 7YKQ SER D 14 UNP D1A9G5 LEU 43 ENGINEERED MUTATION
SEQADV 7YKQ PRO D 18 UNP D1A9G5 ALA 47 ENGINEERED MUTATION
SEQADV 7YKQ THR D 41 UNP D1A9G5 ARG 70 ENGINEERED MUTATION
SEQADV 7YKQ ASP D 47 UNP D1A9G5 THR 76 ENGINEERED MUTATION
SEQADV 7YKQ TYR D 92 UNP D1A9G5 LEU 121 ENGINEERED MUTATION
SEQADV 7YKQ ASP D 117 UNP D1A9G5 ASN 146 ENGINEERED MUTATION
SEQADV 7YKQ ARG D 141 UNP D1A9G5 LYS 170 ENGINEERED MUTATION
SEQADV 7YKQ ARG D 142 UNP D1A9G5 SER 171 ENGINEERED MUTATION
SEQADV 7YKQ PRO D 144 UNP D1A9G5 THR 173 ENGINEERED MUTATION
SEQADV 7YKQ THR D 165 UNP D1A9G5 ARG 194 ENGINEERED MUTATION
SEQADV 7YKQ ASN D 175 UNP D1A9G5 LEU 204 ENGINEERED MUTATION
SEQADV 7YKQ ALA D 185 UNP D1A9G5 SER 214 ENGINEERED MUTATION
SEQADV 7YKQ THR D 196 UNP D1A9G5 ARG 225 ENGINEERED MUTATION
SEQADV 7YKQ GLY D 205 UNP D1A9G5 ASN 234 ENGINEERED MUTATION
SEQADV 7YKQ THR D 213 UNP D1A9G5 PHE 242 ENGINEERED MUTATION
SEQADV 7YKQ PRO D 214 UNP D1A9G5 SER 243 ENGINEERED MUTATION
SEQADV 7YKQ ALA D 224 UNP D1A9G5 SER 253 ENGINEERED MUTATION
SEQADV 7YKQ PRO D 246 UNP D1A9G5 ALA 275 ENGINEERED MUTATION
SEQADV 7YKQ SER D 247 UNP D1A9G5 ILE 276 ENGINEERED MUTATION
SEQADV 7YKQ GLU D 252 UNP D1A9G5 ASP 281 ENGINEERED MUTATION
SEQRES 1 A 269 ASN SER MET HIS HIS HIS HIS HIS HIS ALA ASN PRO TYR
SEQRES 2 A 269 GLN ARG GLY PRO ASP PRO THR GLU ALA SER LEU ARG ALA
SEQRES 3 A 269 PRO ARG GLY PRO PHE ALA VAL SER GLU GLN SER VAL SER
SEQRES 4 A 269 ARG LEU SER VAL SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 5 A 269 TYR PRO THR ASP THR SER GLN GLY THR PHE GLY ALA ILE
SEQRES 6 A 269 ALA ILE SER PRO GLY PHE THR ALA SER TRP SER SER LEU
SEQRES 7 A 269 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 8 A 269 VAL ILE GLY ILE GLU THR ASN THR ARG TYR ASP GLN PRO
SEQRES 9 A 269 ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU ASP TYR
SEQRES 10 A 269 LEU THR GLN ARG SER SER VAL ARG ASP ARG VAL ASP ALA
SEQRES 11 A 269 SER ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 12 A 269 GLY THR LEU GLU ALA ALA ARG ARG ARG PRO SER LEU LYS
SEQRES 13 A 269 ALA ALA ILE PRO ILE ALA PRO TRP ASN LEU ASP LYS THR
SEQRES 14 A 269 TRP PRO GLU VAL THR THR PRO THR LEU ILE ILE GLY GLY
SEQRES 15 A 269 GLU ASN ASP SER ILE ALA PRO VAL ALA THR HIS ALA ILE
SEQRES 16 A 269 PRO PHE TYR ASN SER LEU THR ASN ALA THR GLU LYS ALA
SEQRES 17 A 269 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE PHE PRO GLN
SEQRES 18 A 269 THR PRO ASN ASP THR MET ALA LYS PHE MET ILE ALA TRP
SEQRES 19 A 269 MET LYS ARG PHE ILE ASP ASP ASP THR ARG TYR ASP GLN
SEQRES 20 A 269 PHE LEU CYS PRO PRO PRO ARG PRO SER GLY ASP ILE SER
SEQRES 21 A 269 GLU TYR ARG ASP THR CYS PRO HIS THR
SEQRES 1 B 269 ASN SER MET HIS HIS HIS HIS HIS HIS ALA ASN PRO TYR
SEQRES 2 B 269 GLN ARG GLY PRO ASP PRO THR GLU ALA SER LEU ARG ALA
SEQRES 3 B 269 PRO ARG GLY PRO PHE ALA VAL SER GLU GLN SER VAL SER
SEQRES 4 B 269 ARG LEU SER VAL SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 5 B 269 TYR PRO THR ASP THR SER GLN GLY THR PHE GLY ALA ILE
SEQRES 6 B 269 ALA ILE SER PRO GLY PHE THR ALA SER TRP SER SER LEU
SEQRES 7 B 269 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 8 B 269 VAL ILE GLY ILE GLU THR ASN THR ARG TYR ASP GLN PRO
SEQRES 9 B 269 ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU ASP TYR
SEQRES 10 B 269 LEU THR GLN ARG SER SER VAL ARG ASP ARG VAL ASP ALA
SEQRES 11 B 269 SER ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 12 B 269 GLY THR LEU GLU ALA ALA ARG ARG ARG PRO SER LEU LYS
SEQRES 13 B 269 ALA ALA ILE PRO ILE ALA PRO TRP ASN LEU ASP LYS THR
SEQRES 14 B 269 TRP PRO GLU VAL THR THR PRO THR LEU ILE ILE GLY GLY
SEQRES 15 B 269 GLU ASN ASP SER ILE ALA PRO VAL ALA THR HIS ALA ILE
SEQRES 16 B 269 PRO PHE TYR ASN SER LEU THR ASN ALA THR GLU LYS ALA
SEQRES 17 B 269 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE PHE PRO GLN
SEQRES 18 B 269 THR PRO ASN ASP THR MET ALA LYS PHE MET ILE ALA TRP
SEQRES 19 B 269 MET LYS ARG PHE ILE ASP ASP ASP THR ARG TYR ASP GLN
SEQRES 20 B 269 PHE LEU CYS PRO PRO PRO ARG PRO SER GLY ASP ILE SER
SEQRES 21 B 269 GLU TYR ARG ASP THR CYS PRO HIS THR
SEQRES 1 C 269 ASN SER MET HIS HIS HIS HIS HIS HIS ALA ASN PRO TYR
SEQRES 2 C 269 GLN ARG GLY PRO ASP PRO THR GLU ALA SER LEU ARG ALA
SEQRES 3 C 269 PRO ARG GLY PRO PHE ALA VAL SER GLU GLN SER VAL SER
SEQRES 4 C 269 ARG LEU SER VAL SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 5 C 269 TYR PRO THR ASP THR SER GLN GLY THR PHE GLY ALA ILE
SEQRES 6 C 269 ALA ILE SER PRO GLY PHE THR ALA SER TRP SER SER LEU
SEQRES 7 C 269 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 8 C 269 VAL ILE GLY ILE GLU THR ASN THR ARG TYR ASP GLN PRO
SEQRES 9 C 269 ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU ASP TYR
SEQRES 10 C 269 LEU THR GLN ARG SER SER VAL ARG ASP ARG VAL ASP ALA
SEQRES 11 C 269 SER ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 12 C 269 GLY THR LEU GLU ALA ALA ARG ARG ARG PRO SER LEU LYS
SEQRES 13 C 269 ALA ALA ILE PRO ILE ALA PRO TRP ASN LEU ASP LYS THR
SEQRES 14 C 269 TRP PRO GLU VAL THR THR PRO THR LEU ILE ILE GLY GLY
SEQRES 15 C 269 GLU ASN ASP SER ILE ALA PRO VAL ALA THR HIS ALA ILE
SEQRES 16 C 269 PRO PHE TYR ASN SER LEU THR ASN ALA THR GLU LYS ALA
SEQRES 17 C 269 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE PHE PRO GLN
SEQRES 18 C 269 THR PRO ASN ASP THR MET ALA LYS PHE MET ILE ALA TRP
SEQRES 19 C 269 MET LYS ARG PHE ILE ASP ASP ASP THR ARG TYR ASP GLN
SEQRES 20 C 269 PHE LEU CYS PRO PRO PRO ARG PRO SER GLY ASP ILE SER
SEQRES 21 C 269 GLU TYR ARG ASP THR CYS PRO HIS THR
SEQRES 1 D 269 ASN SER MET HIS HIS HIS HIS HIS HIS ALA ASN PRO TYR
SEQRES 2 D 269 GLN ARG GLY PRO ASP PRO THR GLU ALA SER LEU ARG ALA
SEQRES 3 D 269 PRO ARG GLY PRO PHE ALA VAL SER GLU GLN SER VAL SER
SEQRES 4 D 269 ARG LEU SER VAL SER GLY PHE GLY GLY GLY THR ILE TYR
SEQRES 5 D 269 TYR PRO THR ASP THR SER GLN GLY THR PHE GLY ALA ILE
SEQRES 6 D 269 ALA ILE SER PRO GLY PHE THR ALA SER TRP SER SER LEU
SEQRES 7 D 269 ALA TRP LEU GLY PRO ARG LEU ALA SER HIS GLY PHE VAL
SEQRES 8 D 269 VAL ILE GLY ILE GLU THR ASN THR ARG TYR ASP GLN PRO
SEQRES 9 D 269 ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU ASP TYR
SEQRES 10 D 269 LEU THR GLN ARG SER SER VAL ARG ASP ARG VAL ASP ALA
SEQRES 11 D 269 SER ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 12 D 269 GLY THR LEU GLU ALA ALA ARG ARG ARG PRO SER LEU LYS
SEQRES 13 D 269 ALA ALA ILE PRO ILE ALA PRO TRP ASN LEU ASP LYS THR
SEQRES 14 D 269 TRP PRO GLU VAL THR THR PRO THR LEU ILE ILE GLY GLY
SEQRES 15 D 269 GLU ASN ASP SER ILE ALA PRO VAL ALA THR HIS ALA ILE
SEQRES 16 D 269 PRO PHE TYR ASN SER LEU THR ASN ALA THR GLU LYS ALA
SEQRES 17 D 269 TYR LEU GLU LEU ASN GLY ALA SER HIS PHE PHE PRO GLN
SEQRES 18 D 269 THR PRO ASN ASP THR MET ALA LYS PHE MET ILE ALA TRP
SEQRES 19 D 269 MET LYS ARG PHE ILE ASP ASP ASP THR ARG TYR ASP GLN
SEQRES 20 D 269 PHE LEU CYS PRO PRO PRO ARG PRO SER GLY ASP ILE SER
SEQRES 21 D 269 GLU TYR ARG ASP THR CYS PRO HIS THR
FORMUL 5 HOH *275(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 SER A 65 ALA A 70 5 6
HELIX 3 AA3 TRP A 71 SER A 78 1 8
HELIX 4 AA4 GLN A 94 ARG A 112 1 19
HELIX 5 AA5 VAL A 115 ASP A 117 5 3
HELIX 6 AA6 SER A 130 ARG A 143 1 14
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 PHE A 209 THR A 213 5 5
HELIX 9 AA9 ASN A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 ARG A 235 5 3
HELIX 11 AB2 TYR A 236 CYS A 241 1 6
HELIX 12 AB3 THR B 11 ALA B 17 1 7
HELIX 13 AB4 SER B 65 ALA B 70 5 6
HELIX 14 AB5 TRP B 71 SER B 78 1 8
HELIX 15 AB6 GLN B 94 ARG B 112 1 19
HELIX 16 AB7 VAL B 115 ASP B 117 5 3
HELIX 17 AB8 SER B 130 ARG B 143 1 14
HELIX 18 AB9 HIS B 184 LEU B 192 1 9
HELIX 19 AC1 PHE B 209 THR B 213 5 5
HELIX 20 AC2 ASN B 215 ASP B 231 1 17
HELIX 21 AC3 ASP B 233 ARG B 235 5 3
HELIX 22 AC4 TYR B 236 CYS B 241 1 6
HELIX 23 AC5 THR C 11 ALA C 17 1 7
HELIX 24 AC6 SER C 65 ALA C 70 5 6
HELIX 25 AC7 TRP C 71 SER C 78 1 8
HELIX 26 AC8 GLN C 94 ARG C 112 1 19
HELIX 27 AC9 SER C 130 ARG C 143 1 14
HELIX 28 AD1 HIS C 184 LEU C 192 1 9
HELIX 29 AD2 PHE C 209 THR C 213 5 5
HELIX 30 AD3 ASN C 215 ASP C 231 1 17
HELIX 31 AD4 ASP C 233 LEU C 240 5 8
HELIX 32 AD5 THR D 11 ALA D 17 1 7
HELIX 33 AD6 SER D 65 ALA D 70 5 6
HELIX 34 AD7 TRP D 71 SER D 78 1 8
HELIX 35 AD8 GLN D 94 ARG D 112 1 19
HELIX 36 AD9 VAL D 115 ASP D 117 5 3
HELIX 37 AE1 SER D 130 ARG D 143 1 14
HELIX 38 AE2 HIS D 184 LEU D 192 1 9
HELIX 39 AE3 PHE D 209 THR D 213 5 5
HELIX 40 AE4 ASN D 215 ASP D 232 1 18
HELIX 41 AE5 ASP D 233 LEU D 240 5 8
SHEET 1 AA1 6 VAL A 24 VAL A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O ILE A 42 N GLN A 27
SHEET 3 AA1 6 VAL A 82 ILE A 86 -1 O VAL A 83 N TYR A 43
SHEET 4 AA1 6 PHE A 53 SER A 59 1 N GLY A 54 O VAL A 82
SHEET 5 AA1 6 VAL A 119 HIS A 129 1 O ALA A 127 N ALA A 57
SHEET 6 AA1 6 ALA A 148 ILE A 152 1 O ILE A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 GLY A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O LEU A 201 N ILE A 170
SHEET 3 AA2 3 ILE A 250 ASP A 255 -1 O ARG A 254 N TYR A 200
SHEET 1 AA3 6 VAL B 24 VAL B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O GLY B 40 N VAL B 29
SHEET 3 AA3 6 VAL B 82 ILE B 86 -1 O VAL B 83 N TYR B 43
SHEET 4 AA3 6 PHE B 53 SER B 59 1 N ILE B 58 O ILE B 86
SHEET 5 AA3 6 VAL B 119 HIS B 129 1 O ASP B 120 N PHE B 53
SHEET 6 AA3 6 ALA B 148 ILE B 152 1 O ILE B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 GLY B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O ALA B 199 N ILE B 170
SHEET 3 AA4 3 ILE B 250 ASP B 255 -1 O GLU B 252 N GLU B 202
SHEET 1 AA5 6 VAL C 24 VAL C 29 0
SHEET 2 AA5 6 GLY C 40 PRO C 45 -1 O GLY C 40 N VAL C 29
SHEET 3 AA5 6 VAL C 82 ILE C 86 -1 O VAL C 83 N TYR C 43
SHEET 4 AA5 6 PHE C 53 SER C 59 1 N GLY C 54 O VAL C 82
SHEET 5 AA5 6 VAL C 119 HIS C 129 1 O ALA C 127 N ALA C 57
SHEET 6 AA5 6 ALA C 148 ILE C 152 1 O ILE C 152 N GLY C 128
SHEET 1 AA6 3 THR C 168 GLY C 173 0
SHEET 2 AA6 3 LYS C 198 LEU C 203 1 O LEU C 201 N GLY C 172
SHEET 3 AA6 3 ILE C 250 ASP C 255 -1 O ARG C 254 N TYR C 200
SHEET 1 AA7 6 VAL D 24 VAL D 29 0
SHEET 2 AA7 6 GLY D 40 PRO D 45 -1 O GLY D 40 N VAL D 29
SHEET 3 AA7 6 VAL D 82 ILE D 86 -1 O VAL D 83 N TYR D 43
SHEET 4 AA7 6 PHE D 53 SER D 59 1 N ILE D 56 O VAL D 82
SHEET 5 AA7 6 VAL D 119 HIS D 129 1 O ASP D 120 N PHE D 53
SHEET 6 AA7 6 ALA D 148 ILE D 152 1 O ILE D 152 N GLY D 128
SHEET 1 AA8 3 THR D 168 GLY D 173 0
SHEET 2 AA8 3 LYS D 198 LEU D 203 1 O LEU D 201 N ILE D 170
SHEET 3 AA8 3 ILE D 250 ASP D 255 -1 O GLU D 252 N GLU D 202
SSBOND 1 CYS A 241 CYS A 257 1555 1555 2.04
SSBOND 2 CYS B 241 CYS B 257 1555 1555 2.02
SSBOND 3 CYS C 241 CYS C 257 1555 1555 2.03
SSBOND 4 CYS D 241 CYS D 257 1555 1555 2.03
CISPEP 1 CYS A 241 PRO A 242 0 -17.38
CISPEP 2 CYS A 257 PRO A 258 0 4.24
CISPEP 3 CYS B 241 PRO B 242 0 -13.32
CISPEP 4 CYS B 257 PRO B 258 0 4.17
CISPEP 5 CYS C 241 PRO C 242 0 -9.84
CISPEP 6 CYS C 257 PRO C 258 0 4.18
CISPEP 7 CYS D 241 PRO D 242 0 -8.14
CISPEP 8 CYS D 257 PRO D 258 0 2.14
CRYST1 87.251 63.593 91.537 90.00 97.80 90.00 P 1 21 1 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 0.011461 0.000000 0.001570 0.00000
SCALE2 0.000000 0.015725 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011027 0.00000
TER 1990 THR A 260
TER 3980 THR B 260
TER 5970 THR C 260
TER 7960 THR D 260
MASTER 304 0 0 41 36 0 0 6 8231 4 8 84
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