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HEADER HYDROLASE 14-NOV-24 9KL9
TITLE CRYSTAL STRUCTURE OF A MUTANT POLY(ETHYLENE TEREPHTHALATE) HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.101;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIUM HR29;
SOURCE 3 ORGANISM_TAXID: 2035424;
SOURCE 4 GENE: HRBIN29_00073;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, MUTANT, DIMER
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WANG,Y.FENG,X.Y.DU
REVDAT 1 01-OCT-25 9KL9 0
JRNL AUTH H.WANG,Y.CUN,M.WANG,X.DU,Z.YANG,H.WANG,J.ZHANG,P.WANG,
JRNL AUTH 2 Y.FENG,Y.ZHU
JRNL TITL COMPUTATIONAL LOOP RECONSTRUCTION BASED DESIGN OF EFFICIENT
JRNL TITL 2 PET HYDROLASES.
JRNL REF COMMUN BIOL V. 8 934 2025
JRNL REFN ESSN 2399-3642
JRNL PMID 40527955
JRNL DOI 10.1038/S42003-025-08364-6
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.1_5286
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 9942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 498
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 32.1700 - 4.6000 1.00 2409 136 0.1739 0.1835
REMARK 3 2 4.6000 - 3.6500 0.99 2387 138 0.1666 0.2200
REMARK 3 3 3.6500 - 3.1900 0.97 2361 130 0.2177 0.2824
REMARK 3 4 3.1900 - 2.9000 0.93 2287 94 0.2476 0.3100
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) : 0.351
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.552
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.63
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 : 0.003 4016
REMARK 3 ANGLE : 0.620 5503
REMARK 3 CHIRALITY : 0.045 630
REMARK 3 PLANARITY : 0.007 721
REMARK 3 DIHEDRAL : 12.799 1431
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 9KL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 20-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1300053755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-24
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 : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10117
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.899
REMARK 200 RESOLUTION RANGE LOW (A) : 32.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.19
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M NACL, 100 MM IMIDAZOLE PH8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 MET A 1
REMARK 465 GLN A 2
REMARK 465 GLU A 262
REMARK 465 LEU A 263
REMARK 465 GLU A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 LEU B 261
REMARK 465 GLU B 262
REMARK 465 LEU B 263
REMARK 465 GLU B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
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 63 -14.93 65.80
REMARK 500 SER A 132 -112.29 66.38
REMARK 500 THR A 155 57.46 39.93
REMARK 500 HIS A 158 141.79 -170.47
REMARK 500 ASN A 185 -81.24 -124.44
REMARK 500 THR B 63 -1.43 68.68
REMARK 500 SER B 132 -122.68 61.00
REMARK 500 THR B 155 59.71 34.83
REMARK 500 HIS B 158 141.84 -170.57
REMARK 500 ASN B 185 -80.15 -125.03
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9KL9 A 2 260 UNP A0A2H5Z9R5_UNCXX
DBREF2 9KL9 A A0A2H5Z9R5 35 293
DBREF1 9KL9 B 2 260 UNP A0A2H5Z9R5_UNCXX
DBREF2 9KL9 B A0A2H5Z9R5 35 293
SEQADV 9KL9 MET A 1 UNP A0A2H5Z9R INITIATING METHIONINE
SEQADV 9KL9 ASN A 185 UNP A0A2H5Z9R HIS 218 CONFLICT
SEQADV 9KL9 MET A 189 UNP A0A2H5Z9R PHE 222 CONFLICT
SEQADV 9KL9 THR A 210 UNP A0A2H5Z9R PHE 243 CONFLICT
SEQADV 9KL9 LEU A 261 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 GLU A 262 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 LEU A 263 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 GLU A 264 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 265 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 266 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 267 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 268 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 269 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS A 270 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 MET B 1 UNP A0A2H5Z9R INITIATING METHIONINE
SEQADV 9KL9 ASN B 185 UNP A0A2H5Z9R HIS 218 CONFLICT
SEQADV 9KL9 MET B 189 UNP A0A2H5Z9R PHE 222 CONFLICT
SEQADV 9KL9 THR B 210 UNP A0A2H5Z9R PHE 243 CONFLICT
SEQADV 9KL9 LEU B 261 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 GLU B 262 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 LEU B 263 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 GLU B 264 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 265 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 266 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 267 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 268 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 269 UNP A0A2H5Z9R EXPRESSION TAG
SEQADV 9KL9 HIS B 270 UNP A0A2H5Z9R EXPRESSION TAG
SEQRES 1 A 270 MET GLN SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR
SEQRES 2 A 270 ARG SER ALA LEU THR THR ASP GLY PRO PHE SER VAL ALA
SEQRES 3 A 270 THR TYR SER VAL SER ARG LEU SER VAL SER GLY PHE GLY
SEQRES 4 A 270 GLY GLY VAL ILE TYR TYR PRO THR GLY THR THR LEU THR
SEQRES 5 A 270 PHE GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP
SEQRES 6 A 270 ALA SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER
SEQRES 7 A 270 HIS GLY PHE VAL VAL ILE VAL ILE ASN THR ASN SER ARG
SEQRES 8 A 270 LEU ASP PHE PRO ASP SER ARG ALA SER GLN LEU SER ALA
SEQRES 9 A 270 ALA LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL
SEQRES 10 A 270 ARG ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY
SEQRES 11 A 270 HIS SER MET GLY GLY GLY ALA THR LEU ARG ILE SER GLU
SEQRES 12 A 270 GLN ILE PRO THR LEU LYS ALA GLY VAL PRO LEU THR PRO
SEQRES 13 A 270 TRP HIS THR ASP LYS THR PHE ASN THR PRO VAL PRO GLN
SEQRES 14 A 270 LEU ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL
SEQRES 15 A 270 SER GLN ASN ALA ILE PRO MET TYR GLN ASN LEU PRO SER
SEQRES 16 A 270 THR THR PRO LYS VAL TYR VAL GLU LEU ASP ASN ALA THR
SEQRES 17 A 270 HIS THR ALA PRO ASN SER PRO ASN ALA ALA ILE SER VAL
SEQRES 18 A 270 TYR THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP
SEQRES 19 A 270 THR ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO
SEQRES 20 A 270 ALA LEU SER ASP PHE ARG SER ASN ASN ARG HIS CYS GLN
SEQRES 21 A 270 LEU GLU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 MET GLN SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR
SEQRES 2 B 270 ARG SER ALA LEU THR THR ASP GLY PRO PHE SER VAL ALA
SEQRES 3 B 270 THR TYR SER VAL SER ARG LEU SER VAL SER GLY PHE GLY
SEQRES 4 B 270 GLY GLY VAL ILE TYR TYR PRO THR GLY THR THR LEU THR
SEQRES 5 B 270 PHE GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP
SEQRES 6 B 270 ALA SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER
SEQRES 7 B 270 HIS GLY PHE VAL VAL ILE VAL ILE ASN THR ASN SER ARG
SEQRES 8 B 270 LEU ASP PHE PRO ASP SER ARG ALA SER GLN LEU SER ALA
SEQRES 9 B 270 ALA LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL
SEQRES 10 B 270 ARG ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY
SEQRES 11 B 270 HIS SER MET GLY GLY GLY ALA THR LEU ARG ILE SER GLU
SEQRES 12 B 270 GLN ILE PRO THR LEU LYS ALA GLY VAL PRO LEU THR PRO
SEQRES 13 B 270 TRP HIS THR ASP LYS THR PHE ASN THR PRO VAL PRO GLN
SEQRES 14 B 270 LEU ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL
SEQRES 15 B 270 SER GLN ASN ALA ILE PRO MET TYR GLN ASN LEU PRO SER
SEQRES 16 B 270 THR THR PRO LYS VAL TYR VAL GLU LEU ASP ASN ALA THR
SEQRES 17 B 270 HIS THR ALA PRO ASN SER PRO ASN ALA ALA ILE SER VAL
SEQRES 18 B 270 TYR THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP
SEQRES 19 B 270 THR ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO
SEQRES 20 B 270 ALA LEU SER ASP PHE ARG SER ASN ASN ARG HIS CYS GLN
SEQRES 21 B 270 LEU GLU LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 AA1 ARG A 14 THR A 19 5 6
HELIX 2 AA2 ASP A 65 SER A 68 5 4
HELIX 3 AA3 LEU A 69 HIS A 79 1 11
HELIX 4 AA4 PHE A 94 SER A 112 1 19
HELIX 5 AA5 PRO A 114 ARG A 120 1 7
HELIX 6 AA6 SER A 132 ILE A 145 1 14
HELIX 7 AA7 ASN A 185 LEU A 193 1 9
HELIX 8 AA8 THR A 210 SER A 214 5 5
HELIX 9 AA9 ASN A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 LEU A 241 5 8
HELIX 11 AB2 SER B 15 THR B 19 5 5
HELIX 12 AB3 SER B 31 VAL B 35 5 5
HELIX 13 AB4 ASP B 65 SER B 68 5 4
HELIX 14 AB5 LEU B 69 HIS B 79 1 11
HELIX 15 AB6 PHE B 94 SER B 112 1 19
HELIX 16 AB7 PRO B 114 ALA B 119 1 6
HELIX 17 AB8 SER B 132 ILE B 145 1 14
HELIX 18 AB9 ASN B 185 LEU B 193 1 9
HELIX 19 AC1 THR B 210 SER B 214 5 5
HELIX 20 AC2 ASN B 216 ASP B 232 1 17
HELIX 21 AC3 ASP B 234 LEU B 241 5 8
SHEET 1 AA1 6 SER A 24 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 THR A 47 -1 O TYR A 45 N ALA A 26
SHEET 3 AA1 6 VAL A 82 ILE A 86 -1 O VAL A 83 N TYR A 44
SHEET 4 AA1 6 PHE A 53 SER A 59 1 N MET A 58 O ILE A 86
SHEET 5 AA1 6 LEU A 121 HIS A 131 1 O ARG A 125 N GLY A 55
SHEET 6 AA1 6 ALA A 150 LEU A 154 1 O LEU A 154 N GLY A 130
SHEET 1 AA2 3 GLN A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O VAL A 200 N ILE A 171
SHEET 3 AA2 3 LEU A 249 SER A 254 -1 O SER A 250 N GLU A 203
SHEET 1 AA3 6 SER B 24 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 THR B 47 -1 O ILE B 43 N TYR B 28
SHEET 3 AA3 6 VAL B 82 ILE B 86 -1 O VAL B 83 N TYR B 44
SHEET 4 AA3 6 PHE B 53 SER B 59 1 N ILE B 56 O ILE B 84
SHEET 5 AA3 6 LEU B 121 HIS B 131 1 O ARG B 125 N GLY B 55
SHEET 6 AA3 6 GLY B 151 LEU B 154 1 O LEU B 154 N GLY B 130
SHEET 1 AA4 3 GLN B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O VAL B 202 N ILE B 171
SHEET 3 AA4 3 LEU B 249 SER B 254 -1 O ASP B 251 N GLU B 203
SSBOND 1 CYS A 242 CYS A 259 1555 1555 2.03
SSBOND 2 CYS B 242 CYS B 259 1555 1555 2.03
CRYST1 43.713 51.615 56.679 103.23 103.61 96.66 P 1 2
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 0.022876 0.002672 0.006481 0.00000
SCALE2 0.000000 0.019506 0.005370 0.00000
SCALE3 0.000000 0.000000 0.018828 0.00000
TER 1963 LEU A 261
TER 3918 GLN B 260
MASTER 242 0 0 21 18 0 0 6 3916 2 4 42
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