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HEADER HYDROLASE 20-JUN-09 3HXK
TITLE CRYSTAL STRUCTURE OF A SUGAR HYDROLASE (YEEB) FROM
TITLE 2 LACTOCOCCUS LACTIS, NORTHEAST STRUCTURAL GENOMICS
TITLE 3 CONSORTIUM TARGET KR108
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUGAR HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. LACTIS;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS LACTIS;
SOURCE 4 ORGANISM_TAXID: 1360;
SOURCE 5 STRAIN: IL1403;
SOURCE 6 GENE: L427, L42784, LL0430, YEEB;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+ MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET 21-23C
KEYWDS ALPHA-BETA PROTEIN., STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, NESG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,M.SU,J.SEETHARAMAN,M.MAO,R.XIAO,C.CICCOSANTI,
AUTHOR 2 E.L.FOOTE,M.MAGLAQUI,L.ZHAO,J.K.EVERETT,R.NAIR,T.B.ACTON,
AUTHOR 3 B.ROST,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (NESG)
REVDAT 1 07-JUL-09 3HXK 0
JRNL AUTH F.FOROUHAR,M.SU,J.SEETHARAMAN,M.MAO,R.XIAO,
JRNL AUTH 2 C.CICCOSANTI,E.L.FOOTE,M.MAGLAQUI,L.ZHAO,
JRNL AUTH 3 J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,
JRNL AUTH 4 L.TONG,J.F.HUNT
JRNL TITL CRYSTAL STRUCTURE OF A SUGAR HYDROLASE (YEEB) FROM
JRNL TITL 2 LACTOCOCCUS LACTIS, NORTHEAST STRUCTURAL GENOMICS
JRNL TITL 3 CONSORTIUM TARGET KR108
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2 & XTALVIEW
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 350784.812
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 32873
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.256
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 3177
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2374
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 225
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8080
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.28000
REMARK 3 B22 (A**2) : -11.63000
REMARK 3 B33 (A**2) : 25.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM SIGMAA (A) : 0.61
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.87
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 22.32
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HXK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36064
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08200
REMARK 200 FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17200
REMARK 200 R SYM FOR SHELL (I) : 0.21100
REMARK 200 FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: BNP THEN SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM
REMARK 280 DTT, 0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION:
REMARK 280 0.1 M TRIS (PH 9.1), 29% PEG400, AND 0.1M (MG)2SO4. ,
REMARK 280 MICROBATCH, UNDER OIL, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.42950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.42950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.19550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.21250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.19550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.21250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 109.42950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.19550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.21250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 109.42950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.19550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.21250
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MSE A 1
REMARK 465 ILE A 2
REMARK 465 PHE A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 THR A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 TRP A 9
REMARK 465 TYR A 10
REMARK 465 ASN A 11
REMARK 465 LYS A 12
REMARK 465 LEU A 13
REMARK 465 MSE A 14
REMARK 465 PRO A 35
REMARK 465 ARG A 36
REMARK 465 GLN A 37
REMARK 465 ASN A 38
REMARK 465 GLU A 39
REMARK 465 ASN A 40
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 MSE B 1
REMARK 465 ILE B 2
REMARK 465 PHE B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 THR B 6
REMARK 465 LEU B 7
REMARK 465 PHE B 8
REMARK 465 TRP B 9
REMARK 465 TYR B 10
REMARK 465 ASN B 11
REMARK 465 LYS B 12
REMARK 465 LEU B 13
REMARK 465 MSE B 14
REMARK 465 PRO B 35
REMARK 465 ARG B 36
REMARK 465 GLN B 37
REMARK 465 ASN B 38
REMARK 465 GLU B 39
REMARK 465 ASN B 40
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 HIS B 273
REMARK 465 HIS B 274
REMARK 465 HIS B 275
REMARK 465 HIS B 276
REMARK 465 MSE C 1
REMARK 465 ILE C 2
REMARK 465 PHE C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 THR C 6
REMARK 465 LEU C 7
REMARK 465 PHE C 8
REMARK 465 TRP C 9
REMARK 465 TYR C 10
REMARK 465 ASN C 11
REMARK 465 LYS C 12
REMARK 465 LEU C 13
REMARK 465 MSE C 14
REMARK 465 PRO C 35
REMARK 465 ARG C 36
REMARK 465 GLN C 37
REMARK 465 ASN C 38
REMARK 465 GLU C 39
REMARK 465 ASN C 40
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 HIS C 273
REMARK 465 HIS C 274
REMARK 465 HIS C 275
REMARK 465 HIS C 276
REMARK 465 MSE D 1
REMARK 465 ILE D 2
REMARK 465 PHE D 3
REMARK 465 LEU D 4
REMARK 465 SER D 5
REMARK 465 THR D 6
REMARK 465 LEU D 7
REMARK 465 PHE D 8
REMARK 465 TRP D 9
REMARK 465 TYR D 10
REMARK 465 ASN D 11
REMARK 465 LYS D 12
REMARK 465 LEU D 13
REMARK 465 MSE D 14
REMARK 465 PRO D 35
REMARK 465 ARG D 36
REMARK 465 GLN D 37
REMARK 465 ASN D 38
REMARK 465 GLU D 39
REMARK 465 ASN D 40
REMARK 465 HIS D 271
REMARK 465 HIS D 272
REMARK 465 HIS D 273
REMARK 465 HIS D 274
REMARK 465 HIS D 275
REMARK 465 HIS D 276
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 LEU A 21 -76.07 -109.90
REMARK 500 ASN A 22 -165.67 -119.89
REMARK 500 ALA A 25 93.47 -176.99
REMARK 500 THR A 42 79.78 -153.41
REMARK 500 TYR A 54 -5.52 62.36
REMARK 500 HIS A 56 -155.15 -135.23
REMARK 500 SER A 58 103.91 -50.69
REMARK 500 ARG A 60 14.69 -69.19
REMARK 500 SER A 62 -112.71 -114.83
REMARK 500 LYS A 86 46.44 -144.31
REMARK 500 ASN A 89 -80.24 -121.14
REMARK 500 ASN A 91 82.64 -67.27
REMARK 500 PHE A 92 3.86 -64.12
REMARK 500 SER A 127 -141.10 52.16
REMARK 500 ASN A 138 145.53 172.49
REMARK 500 SER A 139 71.62 73.83
REMARK 500 GLN A 141 -115.69 -137.16
REMARK 500 ILE A 142 42.92 -78.74
REMARK 500 HIS A 143 16.17 -143.06
REMARK 500 TYR A 152 63.96 30.98
REMARK 500 PHE A 159 76.45 -109.91
REMARK 500 HIS A 167 -93.08 -142.75
REMARK 500 PHE A 168 9.56 -69.05
REMARK 500 GLU A 171 -137.68 82.63
REMARK 500 ILE A 172 94.83 59.92
REMARK 500 ASN A 174 95.98 -50.89
REMARK 500 LYS A 183 27.34 -66.82
REMARK 500 ASP A 198 3.83 -176.96
REMARK 500 LEU A 208 -70.16 -51.71
REMARK 500 ARG A 213 30.27 -72.25
REMARK 500 SER A 234 -119.16 58.55
REMARK 500 ALA A 236 15.42 59.39
REMARK 500 ARG A 238 4.82 -64.49
REMARK 500 ALA A 241 119.16 178.63
REMARK 500 SER A 243 -167.81 -108.49
REMARK 500 ASN A 268 45.69 -84.24
REMARK 500 LEU B 21 -74.61 -110.23
REMARK 500 ASN B 22 -165.01 -120.82
REMARK 500 ALA B 25 92.79 -177.37
REMARK 500 THR B 42 77.41 -154.41
REMARK 500 TYR B 54 -5.35 59.92
REMARK 500 HIS B 56 -154.94 -133.88
REMARK 500 SER B 58 103.57 -49.61
REMARK 500 ARG B 60 15.83 -69.09
REMARK 500 SER B 62 -112.73 -114.00
REMARK 500 LYS B 86 45.17 -142.90
REMARK 500 ASN B 89 -80.90 -120.76
REMARK 500 ASN B 91 83.04 -66.95
REMARK 500 PHE B 92 3.55 -63.90
REMARK 500 SER B 127 -140.62 52.49
REMARK 500 ASN B 138 145.98 171.87
REMARK 500 SER B 139 71.20 73.55
REMARK 500 GLN B 141 -114.53 -136.19
REMARK 500 ILE B 142 42.50 -79.45
REMARK 500 HIS B 143 17.02 -142.89
REMARK 500 LYS B 146 -8.95 -59.73
REMARK 500 TYR B 152 62.93 29.14
REMARK 500 PHE B 159 75.78 -109.20
REMARK 500 HIS B 167 -93.05 -143.58
REMARK 500 PHE B 168 9.28 -68.93
REMARK 500 GLU B 171 -138.18 80.93
REMARK 500 ILE B 172 95.60 60.98
REMARK 500 ASN B 174 94.48 -51.30
REMARK 500 ILE B 180 7.38 -69.84
REMARK 500 LYS B 183 27.34 -66.62
REMARK 500 ASP B 198 3.25 -176.58
REMARK 500 ARG B 213 29.15 -71.47
REMARK 500 SER B 234 -119.06 55.10
REMARK 500 ARG B 238 2.74 -63.91
REMARK 500 ALA B 241 117.49 -178.35
REMARK 500 SER B 243 -168.67 -108.04
REMARK 500 ASN B 268 49.90 -72.41
REMARK 500 LEU B 269 -147.86 -138.78
REMARK 500 LEU C 21 -76.17 -108.76
REMARK 500 ASN C 22 -164.56 -119.73
REMARK 500 ALA C 25 93.39 -178.29
REMARK 500 THR C 42 79.45 -153.83
REMARK 500 TYR C 54 -4.37 62.08
REMARK 500 HIS C 56 -155.10 -134.33
REMARK 500 SER C 58 102.33 -50.05
REMARK 500 ARG C 60 15.70 -69.82
REMARK 500 SER C 62 -113.46 -113.68
REMARK 500 LYS C 86 45.71 -143.38
REMARK 500 ASN C 89 -82.03 -119.93
REMARK 500 ASN C 91 81.96 -65.93
REMARK 500 PHE C 92 3.51 -63.48
REMARK 500 SER C 127 -140.22 52.26
REMARK 500 ASN C 138 145.86 171.39
REMARK 500 SER C 139 70.30 72.73
REMARK 500 GLN C 141 -114.36 -136.99
REMARK 500 ILE C 142 42.37 -79.86
REMARK 500 HIS C 143 16.57 -143.04
REMARK 500 TYR C 152 63.34 29.18
REMARK 500 PHE C 159 77.46 -110.40
REMARK 500 HIS C 167 -92.92 -144.16
REMARK 500 PHE C 168 9.56 -69.28
REMARK 500 GLU C 171 -137.67 82.12
REMARK 500 ILE C 172 94.78 60.60
REMARK 500 ASN C 174 93.92 -50.65
REMARK 500 LYS C 183 27.38 -65.82
REMARK 500 ASP C 198 4.70 -175.97
REMARK 500 LEU C 208 -72.04 -52.48
REMARK 500 ARG C 213 29.97 -73.52
REMARK 500 SER C 234 -117.93 56.51
REMARK 500 ARG C 238 4.03 -62.00
REMARK 500 ALA C 241 118.90 179.46
REMARK 500 SER C 243 -167.54 -107.65
REMARK 500 ASN C 268 31.72 -81.11
REMARK 500 LEU D 21 -76.21 -110.90
REMARK 500 ASN D 22 -163.25 -119.71
REMARK 500 ALA D 25 94.05 -175.37
REMARK 500 THR D 42 79.23 -153.34
REMARK 500 TYR D 54 -5.92 61.13
REMARK 500 HIS D 56 -154.65 -134.66
REMARK 500 SER D 58 103.55 -51.35
REMARK 500 ARG D 60 14.14 -68.65
REMARK 500 SER D 62 -113.21 -113.27
REMARK 500 LYS D 86 44.53 -144.21
REMARK 500 ASN D 89 -81.76 -120.54
REMARK 500 ASN D 91 83.78 -66.76
REMARK 500 PHE D 92 3.29 -65.13
REMARK 500 SER D 127 -142.03 52.62
REMARK 500 ASN D 138 144.93 172.95
REMARK 500 SER D 139 70.79 74.37
REMARK 500 GLN D 141 -115.19 -136.56
REMARK 500 ILE D 142 42.83 -79.42
REMARK 500 HIS D 143 15.75 -142.59
REMARK 500 LYS D 146 -9.40 -58.54
REMARK 500 TYR D 152 65.22 29.17
REMARK 500 PHE D 159 78.21 -110.74
REMARK 500 HIS D 167 -92.35 -143.90
REMARK 500 PHE D 168 9.33 -69.37
REMARK 500 GLU D 171 -138.20 82.02
REMARK 500 ILE D 172 95.49 60.71
REMARK 500 ASN D 174 94.78 -49.53
REMARK 500 ILE D 180 5.76 -68.88
REMARK 500 LYS D 183 27.36 -66.96
REMARK 500 ASP D 198 4.82 -176.34
REMARK 500 ARG D 213 28.50 -72.79
REMARK 500 SER D 234 -120.21 54.40
REMARK 500 ARG D 238 4.56 -62.57
REMARK 500 ALA D 241 120.94 179.96
REMARK 500 SER D 243 -167.83 -108.82
REMARK 500 LEU D 269 -73.88 -113.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: KR108 RELATED DB: TARGETDB
DBREF 3HXK A 1 268 UNP Q9CID4 Q9CID4_LACLA 1 268
DBREF 3HXK B 1 268 UNP Q9CID4 Q9CID4_LACLA 1 268
DBREF 3HXK C 1 268 UNP Q9CID4 Q9CID4_LACLA 1 268
DBREF 3HXK D 1 268 UNP Q9CID4 Q9CID4_LACLA 1 268
SEQADV 3HXK LEU A 269 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK GLU A 270 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 271 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 272 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 273 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 274 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 275 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS A 276 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK LEU B 269 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK GLU B 270 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 271 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 272 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 273 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 274 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 275 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS B 276 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK LEU C 269 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK GLU C 270 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 271 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 272 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 273 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 274 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 275 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS C 276 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK LEU D 269 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK GLU D 270 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 271 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 272 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 273 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 274 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 275 UNP Q9CID4 EXPRESSION TAG
SEQADV 3HXK HIS D 276 UNP Q9CID4 EXPRESSION TAG
SEQRES 1 A 276 MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU
SEQRES 2 A 276 MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP
SEQRES 3 A 276 VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU
SEQRES 4 A 276 ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY
SEQRES 5 A 276 GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU
SEQRES 6 A 276 ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU
SEQRES 7 A 276 LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN
SEQRES 8 A 276 PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE
SEQRES 9 A 276 SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN
SEQRES 10 A 276 PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY
SEQRES 11 A 276 HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS
SEQRES 12 A 276 ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER
SEQRES 13 A 276 PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN
SEQRES 14 A 276 PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU
SEQRES 15 A 276 LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS
SEQRES 16 A 276 THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU
SEQRES 17 A 276 LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE
SEQRES 18 A 276 GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER
SEQRES 19 A 276 LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS
SEQRES 20 A 276 LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP
SEQRES 21 A 276 TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS
SEQRES 22 A 276 HIS HIS HIS
SEQRES 1 B 276 MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU
SEQRES 2 B 276 MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP
SEQRES 3 B 276 VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU
SEQRES 4 B 276 ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY
SEQRES 5 B 276 GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU
SEQRES 6 B 276 ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU
SEQRES 7 B 276 LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN
SEQRES 8 B 276 PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE
SEQRES 9 B 276 SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN
SEQRES 10 B 276 PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY
SEQRES 11 B 276 HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS
SEQRES 12 B 276 ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER
SEQRES 13 B 276 PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN
SEQRES 14 B 276 PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU
SEQRES 15 B 276 LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS
SEQRES 16 B 276 THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU
SEQRES 17 B 276 LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE
SEQRES 18 B 276 GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER
SEQRES 19 B 276 LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS
SEQRES 20 B 276 LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP
SEQRES 21 B 276 TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS
SEQRES 22 B 276 HIS HIS HIS
SEQRES 1 C 276 MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU
SEQRES 2 C 276 MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP
SEQRES 3 C 276 VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU
SEQRES 4 C 276 ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY
SEQRES 5 C 276 GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU
SEQRES 6 C 276 ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU
SEQRES 7 C 276 LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN
SEQRES 8 C 276 PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE
SEQRES 9 C 276 SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN
SEQRES 10 C 276 PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY
SEQRES 11 C 276 HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS
SEQRES 12 C 276 ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER
SEQRES 13 C 276 PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN
SEQRES 14 C 276 PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU
SEQRES 15 C 276 LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS
SEQRES 16 C 276 THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU
SEQRES 17 C 276 LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE
SEQRES 18 C 276 GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER
SEQRES 19 C 276 LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS
SEQRES 20 C 276 LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP
SEQRES 21 C 276 TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS
SEQRES 22 C 276 HIS HIS HIS
SEQRES 1 D 276 MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU
SEQRES 2 D 276 MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP
SEQRES 3 D 276 VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU
SEQRES 4 D 276 ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY
SEQRES 5 D 276 GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU
SEQRES 6 D 276 ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU
SEQRES 7 D 276 LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN
SEQRES 8 D 276 PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE
SEQRES 9 D 276 SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN
SEQRES 10 D 276 PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY
SEQRES 11 D 276 HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS
SEQRES 12 D 276 ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER
SEQRES 13 D 276 PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN
SEQRES 14 D 276 PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU
SEQRES 15 D 276 LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS
SEQRES 16 D 276 THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU
SEQRES 17 D 276 LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE
SEQRES 18 D 276 GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER
SEQRES 19 D 276 LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS
SEQRES 20 D 276 LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP
SEQRES 21 D 276 TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS
SEQRES 22 D 276 HIS HIS HIS
MODRES 3HXK MSE A 84 MET SELENOMETHIONINE
MODRES 3HXK MSE B 84 MET SELENOMETHIONINE
MODRES 3HXK MSE C 84 MET SELENOMETHIONINE
MODRES 3HXK MSE D 84 MET SELENOMETHIONINE
HET MSE A 84 8
HET MSE B 84 8
HET MSE C 84 8
HET MSE D 84 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 5 HOH *61(H2 O)
HELIX 1 1 SER A 58 GLU A 61 5 4
HELIX 2 2 SER A 62 GLN A 72 1 11
HELIX 3 3 PHE A 92 HIS A 111 1 20
HELIX 4 4 ALA A 128 GLY A 137 1 10
HELIX 5 5 ILE A 175 ASN A 179 5 5
HELIX 6 6 ILE A 204 LYS A 216 1 13
HELIX 7 7 LEU A 248 ARG A 253 1 6
HELIX 8 8 ARG A 253 ASN A 268 1 16
HELIX 9 9 SER B 58 GLU B 61 5 4
HELIX 10 10 SER B 62 GLN B 72 1 11
HELIX 11 11 PHE B 92 HIS B 111 1 20
HELIX 12 12 ALA B 128 GLY B 137 1 10
HELIX 13 13 ILE B 175 ASN B 179 5 5
HELIX 14 14 ILE B 204 LYS B 216 1 13
HELIX 15 15 LEU B 248 ASN B 268 1 21
HELIX 16 16 SER C 58 GLU C 61 5 4
HELIX 17 17 SER C 62 GLN C 72 1 11
HELIX 18 18 PHE C 92 HIS C 111 1 20
HELIX 19 19 ALA C 128 GLY C 137 1 10
HELIX 20 20 ILE C 175 ASN C 179 5 5
HELIX 21 21 ILE C 204 LYS C 216 1 13
HELIX 22 22 LEU C 248 ASN C 268 1 21
HELIX 23 23 SER D 58 GLU D 61 5 4
HELIX 24 24 SER D 62 GLN D 72 1 11
HELIX 25 25 PHE D 92 HIS D 111 1 20
HELIX 26 26 SER D 127 GLY D 137 1 11
HELIX 27 27 ILE D 175 ASN D 179 5 5
HELIX 28 28 ILE D 204 LYS D 216 1 13
HELIX 29 29 LEU D 248 ASN D 268 1 21
SHEET 1 A16 LYS A 16 THR A 18 0
SHEET 2 A16 TRP A 26 TYR A 30 -1 O PHE A 29 N SER A 17
SHEET 3 A16 GLN A 75 ASN A 80 -1 O VAL A 76 N TYR A 30
SHEET 4 A16 ALA A 45 CYS A 49 1 N ILE A 46 O GLN A 75
SHEET 5 A16 PHE A 122 SER A 127 1 O PHE A 122 N ILE A 47
SHEET 6 A16 GLY A 147 PRO A 153 1 O CYS A 151 N SER A 127
SHEET 7 A16 THR A 191 THR A 196 1 O PHE A 192 N LEU A 150
SHEET 8 A16 PHE A 221 PHE A 226 1 O GLU A 222 N ILE A 193
SHEET 9 A16 PHE B 221 PHE B 226 -1 O ALA B 223 N PHE A 225
SHEET 10 A16 THR B 191 THR B 196 1 N ILE B 193 O GLU B 222
SHEET 11 A16 VAL B 148 PRO B 153 1 N LEU B 150 O PHE B 192
SHEET 12 A16 PHE B 122 SER B 127 1 N SER B 127 O CYS B 151
SHEET 13 A16 ALA B 45 CYS B 49 1 N ILE B 47 O PHE B 122
SHEET 14 A16 GLN B 75 ASN B 80 1 O GLN B 75 N ILE B 46
SHEET 15 A16 TRP B 26 TYR B 30 -1 N TYR B 30 O VAL B 76
SHEET 16 A16 LYS B 16 THR B 18 -1 N SER B 17 O PHE B 29
SHEET 1 B16 LYS C 16 THR C 18 0
SHEET 2 B16 TRP C 26 TYR C 30 -1 O PHE C 29 N SER C 17
SHEET 3 B16 GLN C 75 ASN C 80 -1 O VAL C 76 N TYR C 30
SHEET 4 B16 ALA C 45 CYS C 49 1 N ILE C 46 O GLN C 75
SHEET 5 B16 PHE C 122 SER C 127 1 O PHE C 122 N ILE C 47
SHEET 6 B16 GLY C 147 PRO C 153 1 O CYS C 151 N SER C 127
SHEET 7 B16 THR C 191 THR C 196 1 O PHE C 192 N LEU C 150
SHEET 8 B16 PHE C 221 PHE C 226 1 O GLU C 222 N ILE C 193
SHEET 9 B16 PHE D 221 PHE D 226 -1 O ALA D 223 N PHE C 225
SHEET 10 B16 THR D 191 THR D 196 1 N ILE D 193 O GLU D 222
SHEET 11 B16 VAL D 148 CYS D 151 1 N LEU D 150 O PHE D 192
SHEET 12 B16 PHE D 122 CYS D 126 1 N GLY D 125 O CYS D 151
SHEET 13 B16 ALA D 45 CYS D 49 1 N ILE D 47 O PHE D 122
SHEET 14 B16 GLN D 75 ASN D 80 1 O LEU D 77 N ILE D 48
SHEET 15 B16 TRP D 26 TYR D 30 -1 N TYR D 30 O VAL D 76
SHEET 16 B16 LYS D 16 THR D 18 -1 N SER D 17 O PHE D 29
LINK C VAL A 83 N MSE A 84 1555 1555 1.33
LINK C MSE A 84 N ASN A 85 1555 1555 1.33
LINK C VAL B 83 N MSE B 84 1555 1555 1.34
LINK C MSE B 84 N ASN B 85 1555 1555 1.33
LINK C VAL C 83 N MSE C 84 1555 1555 1.34
LINK C MSE C 84 N ASN C 85 1555 1555 1.33
LINK C VAL D 83 N MSE D 84 1555 1555 1.34
LINK C MSE D 84 N ASN D 85 1555 1555 1.33
CISPEP 1 TRP A 161 PRO A 162 0 0.21
CISPEP 2 TRP B 161 PRO B 162 0 -0.63
CISPEP 3 TRP C 161 PRO C 162 0 1.24
CISPEP 4 TRP D 161 PRO D 162 0 0.16
CRYST1 68.391 150.425 218.859 90.00 90.00 90.00 C 2 2 21 32
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 0.014622 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004569 0.00000
TER 2021 GLU A 270
TER 4042 GLU B 270
TER 6063 GLU C 270
TER 8084 GLU D 270
MASTER 507 0 4 29 32 0 0 6 8141 4 40 88
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