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HEADER HYDROLASE 11-JAN-26 10BV
TITLE LOOP MUTANT OF A CHLOROGENIC ACID ESTERASE FROM LACTOBACILLUS
TITLE 2 HELVETICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROGENIC ACID ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: CINNAMOYL ESTERASE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS HELVETICUS;
SOURCE 3 ORGANISM_TAXID: 1587;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, CHLOROGENIC ACID ESTERASE, FERULIC ACID ESTERASE,
KEYWDS 2 CHLOROGENIC ACID, FERULIC ACID, LACTOBACILLUS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.P.OWENS,K.K.OMORI,N.CARL
REVDAT 1 12-AUG-26 10BV 0
JRNL AUTH N.CARL,Y.TSIGARIS,D.JI,N.K.ANPREE,K.K.OMORI,C.P.OWENS
JRNL TITL ANALYSIS OF THE ATYPICAL TEMPERATURE DEPENDENCE AND
JRNL TITL 2 CONFORMATIONAL CHANGES DURING TURNOVER OF A LACTOBACILLUS
JRNL TITL 3 CHLOROGENIC ACID ESTERASE.
JRNL REF BIOCHEMISTRY 2026
JRNL REFN ISSN 0006-2960
JRNL PMID 42531162
JRNL DOI 10.1021/ACS.BIOCHEM.6C00440
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 2.0_5936
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) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.320
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 32306
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1604
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 51.7800 - 6.7800 0.94 2771 165 0.1471 0.1962
REMARK 3 2 6.7800 - 5.3800 0.99 2873 164 0.2122 0.2824
REMARK 3 3 5.3800 - 4.7000 0.99 2868 139 0.2141 0.2682
REMARK 3 4 4.7000 - 4.2700 0.97 2774 144 0.2050 0.2909
REMARK 3 5 4.2700 - 3.9700 0.92 2645 119 0.2537 0.3309
REMARK 3 6 3.9700 - 3.7300 0.95 2714 148 0.3159 0.3652
REMARK 3 7 3.7300 - 3.5500 0.97 2791 133 0.3145 0.3536
REMARK 3 8 3.5500 - 3.3900 0.97 2775 142 0.3504 0.3829
REMARK 3 9 3.3900 - 3.2600 0.99 2826 158 0.3403 0.4703
REMARK 3 10 3.2600 - 3.1500 0.99 2804 156 0.3556 0.3911
REMARK 3 11 3.1500 - 3.0500 0.99 2861 136 0.3580 0.3975
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) : 0.612
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.527
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.53
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 : 0.013 11608
REMARK 3 ANGLE : 1.692 15761
REMARK 3 CHIRALITY : 0.092 1763
REMARK 3 PLANARITY : 0.013 2102
REMARK 3 DIHEDRAL : 13.358 4248
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 10BV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-26.
REMARK 100 THE DEPOSITION ID IS D_1000304077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-24
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32377
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 54.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.24900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 1.08100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM CHLORIDE, CITRIC ACID, PEG
REMARK 280 6000, SPERMINE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
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 43.04231
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.75250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.59345
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.04231
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.75250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 80.59345
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 SER C 0
REMARK 465 ALA C 246
REMARK 465 PHE C 247
REMARK 465 ALA D 246
REMARK 465 PHE D 247
REMARK 465 ALA E 246
REMARK 465 PHE E 247
REMARK 465 SER F 0
REMARK 465 ALA F 246
REMARK 465 PHE F 247
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 247 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE B 247 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE C 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 23 CG CD OE1 OE2
REMARK 470 ASP C 48 CG OD1 OD2
REMARK 470 GLU C 67 CG CD OE1 OE2
REMARK 470 LYS C 206 CG CD CE NZ
REMARK 470 ASP C 237 CG OD1 OD2
REMARK 470 GLN C 241 CG CD OE1 NE2
REMARK 470 ILE D 24 CG1 CG2 CD1
REMARK 470 ARG D 51 CG CD NE CZ NH1 NH2
REMARK 470 THR D 195 OG1 CG2
REMARK 470 ASP D 197 CG OD1 OD2
REMARK 470 MET E 1 CG SD CE
REMARK 470 ASP E 156 CG OD1 OD2
REMARK 470 GLN E 198 CG CD OE1 NE2
REMARK 470 GLU F 23 CG CD OE1 OE2
REMARK 470 TYR F 25 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN F 45 CG CD OE1 NE2
REMARK 470 GLU F 53 CG CD OE1 OE2
REMARK 470 HIS F 96 CG ND1 CD2 CE1 NE2
REMARK 470 LYS F 124 CG CD CE NZ
REMARK 470 LYS F 203 CG CD CE NZ
REMARK 470 MET F 219 CG SD CE
REMARK 470 PHE F 227 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS F 232 CG CD CE NZ
REMARK 470 ASP F 237 CG OD1 OD2
REMARK 470 PHE F 242 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU F 243 CG CD1 CD2
REMARK 470 LYS F 244 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 78 CB CYS C 78 SG -0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 129 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU A 176 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU E 118 CA - CB - CG ANGL. DEV. = -15.0 DEGREES
REMARK 500 LEU E 176 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU F 43 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
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 THR A 35 -8.12 80.59
REMARK 500 SER A 106 -121.78 54.78
REMARK 500 GLN A 145 -170.57 54.68
REMARK 500 VAL A 161 105.88 -48.64
REMARK 500 ASN A 222 -2.73 78.67
REMARK 500 THR B 35 -7.60 80.34
REMARK 500 SER B 106 -123.64 55.32
REMARK 500 GLN B 145 -95.47 56.78
REMARK 500 ASN B 222 -3.00 78.91
REMARK 500 PRO B 245 -174.17 -63.85
REMARK 500 PHE C 21 49.02 -91.92
REMARK 500 THR C 35 -6.98 80.78
REMARK 500 SER C 106 -123.14 54.64
REMARK 500 GLN C 145 -124.23 51.47
REMARK 500 LEU C 160 -139.50 -132.80
REMARK 500 ASN C 222 -3.35 77.61
REMARK 500 PRO D 20 -168.78 -79.92
REMARK 500 THR D 35 -7.29 79.77
REMARK 500 SER D 106 -122.12 54.93
REMARK 500 ASN D 222 -3.92 77.37
REMARK 500 PHE E 21 59.17 -92.23
REMARK 500 THR E 35 -6.79 80.72
REMARK 500 SER E 106 -122.87 54.39
REMARK 500 VAL E 161 107.31 -50.15
REMARK 500 ASN E 222 -2.55 78.55
REMARK 500 THR F 35 -6.68 80.45
REMARK 500 SER F 106 -121.74 53.54
REMARK 500 ASN F 222 -3.35 78.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8SKM RELATED DB: PDB
REMARK 900 WILD TYPE PROTEIN
DBREF1 10BV A 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV A A0A060IEI9 1 250
DBREF1 10BV B 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV B A0A060IEI9 1 250
DBREF1 10BV C 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV C A0A060IEI9 1 250
DBREF1 10BV D 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV D A0A060IEI9 1 250
DBREF1 10BV E 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV E A0A060IEI9 1 250
DBREF1 10BV F 1 246 UNP A0A060IEI9_LACHE
DBREF2 10BV F A0A060IEI9 1 250
SEQADV 10BV SER A 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV A UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV A UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV A UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV A UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL A 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE A 247 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV SER B 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV B UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV B UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV B UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV B UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL B 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE B 247 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV SER C 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV C UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV C UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV C UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV C UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL C 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE C 247 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV SER D 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV D UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV D UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV D UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV D UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL D 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE D 247 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV SER E 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV E UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV E UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV E UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV E UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL E 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE E 247 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV SER F 0 UNP A0A060IEI EXPRESSION TAG
SEQADV 10BV F UNP A0A060IEI GLY 162 DELETION
SEQADV 10BV F UNP A0A060IEI ASN 163 DELETION
SEQADV 10BV F UNP A0A060IEI LYS 164 DELETION
SEQADV 10BV F UNP A0A060IEI LEU 165 DELETION
SEQADV 10BV VAL F 181 UNP A0A060IEI ILE 185 CONFLICT
SEQADV 10BV PHE F 247 UNP A0A060IEI EXPRESSION TAG
SEQRES 1 A 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 A 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 A 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 A 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 A 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 A 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 A 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 A 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 A 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 A 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 A 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 A 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 A 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 A 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 A 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 A 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 A 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 A 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 A 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 A 248 PHE
SEQRES 1 B 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 B 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 B 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 B 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 B 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 B 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 B 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 B 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 B 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 B 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 B 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 B 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 B 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 B 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 B 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 B 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 B 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 B 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 B 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 B 248 PHE
SEQRES 1 C 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 C 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 C 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 C 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 C 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 C 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 C 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 C 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 C 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 C 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 C 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 C 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 C 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 C 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 C 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 C 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 C 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 C 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 C 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 C 248 PHE
SEQRES 1 D 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 D 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 D 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 D 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 D 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 D 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 D 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 D 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 D 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 D 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 D 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 D 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 D 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 D 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 D 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 D 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 D 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 D 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 D 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 D 248 PHE
SEQRES 1 E 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 E 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 E 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 E 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 E 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 E 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 E 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 E 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 E 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 E 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 E 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 E 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 E 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 E 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 E 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 E 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 E 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 E 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 E 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 E 248 PHE
SEQRES 1 F 248 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 F 248 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 F 248 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 F 248 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 F 248 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 F 248 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 F 248 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 F 248 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 F 248 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 F 248 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 F 248 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 F 248 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 F 248 ASP VAL VAL PRO LEU VAL GLY MET LYS VAL GLY GLY PHE
SEQRES 14 F 248 TYR LEU ARG THR ALA GLN VAL LEU PRO ILE TYR GLU VAL
SEQRES 15 F 248 SER GLN ARG PHE THR ARG PRO VAL SER VAL ILE ALA GLY
SEQRES 16 F 248 THR ASN ASP GLN VAL VAL ASP PRO LYS TYR ALA LYS LYS
SEQRES 17 F 248 TYR ASP GLU VAL TYR GLU ASN SER GLU LEU HIS MET ILE
SEQRES 18 F 248 PRO ASN ALA ASP HIS ARG PHE SER GLY GLY TYR LYS ASP
SEQRES 19 F 248 MET ALA ALA ASP LEU THR ALA GLN PHE LEU LYS PRO ALA
SEQRES 20 F 248 PHE
HELIX 1 AA1 THR A 40 GLU A 53 1 14
HELIX 2 AA2 LYS A 71 MET A 75 5 5
HELIX 3 AA3 THR A 76 THR A 93 1 18
HELIX 4 AA4 SER A 106 TYR A 119 1 14
HELIX 5 AA5 ALA A 133 GLY A 142 1 10
HELIX 6 AA6 GLY A 167 VAL A 175 1 9
HELIX 7 AA7 PRO A 177 GLN A 183 1 7
HELIX 8 AA8 ASP A 201 TYR A 212 1 12
HELIX 9 AA9 GLY A 229 LYS A 244 1 16
HELIX 10 AB1 THR B 40 GLU B 53 1 14
HELIX 11 AB2 LYS B 71 MET B 75 5 5
HELIX 12 AB3 THR B 76 ASP B 94 1 19
HELIX 13 AB4 SER B 106 TYR B 119 1 14
HELIX 14 AB5 ALA B 133 GLY B 142 1 10
HELIX 15 AB6 GLY B 167 GLN B 174 1 8
HELIX 16 AB7 PRO B 177 GLN B 183 1 7
HELIX 17 AB8 ASP B 201 TYR B 212 1 12
HELIX 18 AB9 GLY B 229 LYS B 244 1 16
HELIX 19 AC1 THR C 40 GLU C 53 1 14
HELIX 20 AC2 LYS C 71 MET C 75 5 5
HELIX 21 AC3 THR C 76 THR C 93 1 18
HELIX 22 AC4 SER C 106 TYR C 119 1 14
HELIX 23 AC5 ALA C 133 GLY C 142 1 10
HELIX 24 AC6 GLY C 167 GLN C 174 1 8
HELIX 25 AC7 PRO C 177 GLN C 183 1 7
HELIX 26 AC8 ASP C 201 TYR C 212 1 12
HELIX 27 AC9 GLY C 229 LYS C 244 1 16
HELIX 28 AD1 THR D 40 GLU D 53 1 14
HELIX 29 AD2 LYS D 71 MET D 75 5 5
HELIX 30 AD3 THR D 76 THR D 93 1 18
HELIX 31 AD4 SER D 106 TYR D 119 1 14
HELIX 32 AD5 ALA D 133 GLY D 142 1 10
HELIX 33 AD6 GLY D 167 GLN D 174 1 8
HELIX 34 AD7 PRO D 177 GLN D 183 1 7
HELIX 35 AD8 ASP D 201 TYR D 212 1 12
HELIX 36 AD9 GLY D 229 LYS D 244 1 16
HELIX 37 AE1 THR E 40 GLU E 53 1 14
HELIX 38 AE2 LYS E 71 MET E 75 5 5
HELIX 39 AE3 THR E 76 ASP E 94 1 19
HELIX 40 AE4 SER E 106 TYR E 119 1 14
HELIX 41 AE5 GLN E 134 GLY E 142 1 9
HELIX 42 AE6 GLY E 167 GLN E 174 1 8
HELIX 43 AE7 PRO E 177 GLN E 183 1 7
HELIX 44 AE8 ASP E 201 TYR E 212 1 12
HELIX 45 AE9 GLY E 229 LYS E 244 1 16
HELIX 46 AF1 THR F 40 GLU F 53 1 14
HELIX 47 AF2 LYS F 71 MET F 75 5 5
HELIX 48 AF3 THR F 76 THR F 93 1 18
HELIX 49 AF4 SER F 106 TYR F 119 1 14
HELIX 50 AF5 ALA F 133 GLY F 142 1 10
HELIX 51 AF6 GLY F 167 GLN F 174 1 8
HELIX 52 AF7 PRO F 177 GLN F 183 1 7
HELIX 53 AF8 ASP F 201 TYR F 212 1 12
HELIX 54 AF9 GLY F 229 LYS F 244 1 16
SHEET 1 AA1 8 MET A 1 ARG A 8 0
SHEET 2 AA1 8 LEU A 11 GLU A 18 -1 O GLY A 15 N ILE A 4
SHEET 3 AA1 8 VAL A 55 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 AA1 8 TYR A 25 MET A 31 1 N ILE A 30 O VAL A 58
SHEET 5 AA1 8 VAL A 97 HIS A 105 1 O ARG A 98 N TYR A 25
SHEET 6 AA1 8 VAL A 123 LEU A 129 1 O LEU A 129 N GLY A 104
SHEET 7 AA1 8 VAL A 189 GLY A 194 1 O ILE A 192 N LEU A 128
SHEET 8 AA1 8 SER A 215 ILE A 220 1 O HIS A 218 N VAL A 191
SHEET 1 AA2 2 ASN A 143 THR A 144 0
SHEET 2 AA2 2 ALA A 147 THR A 148 -1 O ALA A 147 N THR A 144
SHEET 1 AA3 2 VAL A 157 LEU A 160 0
SHEET 2 AA3 2 MET A 163 GLY A 166 -1 O VAL A 165 N VAL A 158
SHEET 1 AA4 8 MET B 1 ARG B 8 0
SHEET 2 AA4 8 LEU B 11 GLU B 18 -1 O LEU B 13 N ILE B 6
SHEET 3 AA4 8 VAL B 55 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 AA4 8 TYR B 25 MET B 31 1 N ASP B 26 O ALA B 56
SHEET 5 AA4 8 VAL B 97 HIS B 105 1 O ASP B 99 N MET B 27
SHEET 6 AA4 8 LYS B 125 LEU B 129 1 O LEU B 129 N GLY B 104
SHEET 7 AA4 8 VAL B 189 GLY B 194 1 O ILE B 192 N LEU B 128
SHEET 8 AA4 8 SER B 215 ILE B 220 1 O HIS B 218 N VAL B 191
SHEET 1 AA5 2 ASN B 143 THR B 144 0
SHEET 2 AA5 2 ALA B 147 THR B 148 -1 O ALA B 147 N THR B 144
SHEET 1 AA6 2 VAL B 157 PRO B 159 0
SHEET 2 AA6 2 LYS B 164 GLY B 166 -1 O VAL B 165 N VAL B 158
SHEET 1 AA7 8 SER C 2 ARG C 8 0
SHEET 2 AA7 8 LEU C 11 GLU C 18 -1 O ARG C 17 N SER C 2
SHEET 3 AA7 8 VAL C 55 PHE C 60 -1 O SER C 57 N GLU C 18
SHEET 4 AA7 8 TYR C 25 MET C 31 1 N ASP C 26 O ALA C 56
SHEET 5 AA7 8 VAL C 97 HIS C 105 1 O VAL C 103 N MET C 31
SHEET 6 AA7 8 VAL C 123 LEU C 129 1 O LEU C 129 N GLY C 104
SHEET 7 AA7 8 VAL C 189 GLY C 194 1 O SER C 190 N VAL C 126
SHEET 8 AA7 8 SER C 215 ILE C 220 1 O GLU C 216 N VAL C 191
SHEET 1 AA8 2 ASN C 143 THR C 144 0
SHEET 2 AA8 2 ALA C 147 THR C 148 -1 O ALA C 147 N THR C 144
SHEET 1 AA9 2 VAL C 157 PRO C 159 0
SHEET 2 AA9 2 LYS C 164 GLY C 166 -1 O VAL C 165 N VAL C 158
SHEET 1 AB1 8 MET D 1 ARG D 8 0
SHEET 2 AB1 8 LEU D 11 GLU D 18 -1 O LEU D 13 N ILE D 6
SHEET 3 AB1 8 VAL D 55 PHE D 60 -1 O SER D 57 N GLU D 18
SHEET 4 AB1 8 TYR D 25 MET D 31 1 N ASP D 26 O ALA D 56
SHEET 5 AB1 8 VAL D 97 HIS D 105 1 O VAL D 103 N ILE D 29
SHEET 6 AB1 8 VAL D 123 LEU D 129 1 O VAL D 127 N GLY D 104
SHEET 7 AB1 8 VAL D 189 GLY D 194 1 O ILE D 192 N LEU D 128
SHEET 8 AB1 8 SER D 215 ILE D 220 1 O HIS D 218 N VAL D 191
SHEET 1 AB2 2 ASN D 143 THR D 144 0
SHEET 2 AB2 2 ALA D 147 THR D 148 -1 O ALA D 147 N THR D 144
SHEET 1 AB3 2 VAL D 157 PRO D 159 0
SHEET 2 AB3 2 LYS D 164 GLY D 166 -1 O VAL D 165 N VAL D 158
SHEET 1 AB4 8 MET E 1 ARG E 8 0
SHEET 2 AB4 8 LEU E 11 GLU E 18 -1 O ARG E 17 N SER E 2
SHEET 3 AB4 8 VAL E 55 PHE E 60 -1 O ARG E 59 N ASP E 16
SHEET 4 AB4 8 TYR E 25 MET E 31 1 N ILE E 30 O VAL E 58
SHEET 5 AB4 8 VAL E 97 HIS E 105 1 O ASP E 99 N MET E 27
SHEET 6 AB4 8 LYS E 125 LEU E 129 1 O LEU E 129 N GLY E 104
SHEET 7 AB4 8 VAL E 189 GLY E 194 1 O SER E 190 N VAL E 126
SHEET 8 AB4 8 SER E 215 ILE E 220 1 O HIS E 218 N VAL E 191
SHEET 1 AB5 2 ASN E 143 THR E 144 0
SHEET 2 AB5 2 ALA E 147 THR E 148 -1 O ALA E 147 N THR E 144
SHEET 1 AB6 2 VAL E 157 LEU E 160 0
SHEET 2 AB6 2 MET E 163 GLY E 166 -1 O VAL E 165 N VAL E 158
SHEET 1 AB7 8 SER F 2 ARG F 8 0
SHEET 2 AB7 8 LEU F 11 GLU F 18 -1 O LEU F 13 N ILE F 6
SHEET 3 AB7 8 VAL F 55 PHE F 60 -1 O SER F 57 N GLU F 18
SHEET 4 AB7 8 TYR F 25 MET F 31 1 N ASP F 26 O ALA F 56
SHEET 5 AB7 8 VAL F 97 HIS F 105 1 O PHE F 101 N ILE F 29
SHEET 6 AB7 8 VAL F 123 LEU F 129 1 O LEU F 129 N GLY F 104
SHEET 7 AB7 8 VAL F 189 GLY F 194 1 O SER F 190 N VAL F 126
SHEET 8 AB7 8 SER F 215 ILE F 220 1 O GLU F 216 N VAL F 191
SHEET 1 AB8 2 ASN F 143 THR F 144 0
SHEET 2 AB8 2 ALA F 147 THR F 148 -1 O ALA F 147 N THR F 144
SHEET 1 AB9 2 VAL F 157 PRO F 159 0
SHEET 2 AB9 2 LYS F 164 GLY F 166 -1 O VAL F 165 N VAL F 158
CRYST1 109.970 99.505 162.947 90.00 98.43 90.00 I 1 2 1 24
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 0.009093 0.000000 0.001347 0.00000
SCALE2 0.000000 0.010050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006204 0.00000
TER 1925 PHE A 247
TER 3850 PHE B 247
TER 5731 PRO C 245
TER 7632 PRO D 245
TER 9537 PRO E 245
TER 11385 PRO F 245
MASTER 356 0 0 54 72 0 0 611379 6 0 120
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