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HEADER HYDROLASE 05-MAY-25 9UTX
TITLE THE STRUCTURE OF THE Q174E MUTANT OF PES-H1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PES-H1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, ENZYME ENGINEERING, SALT TOLERANCE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,A.LIU
REVDAT 1 13-MAY-26 9UTX 0
JRNL AUTH W.XIE,A.LIU
JRNL TITL RATIONAL DESIGN OF THE POLYETHYLENE TEREPHTHALATE-DEGRADING
JRNL TITL 2 ENZYME PES-H1 WITH LOW SALT TOLERANCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 65694
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 34.2300 - 4.0000 1.00 4685 144 0.2087 0.2102
REMARK 3 2 4.0000 - 3.1700 1.00 4619 151 0.2183 0.2302
REMARK 3 3 3.1700 - 2.7700 1.00 4580 136 0.2310 0.2343
REMARK 3 4 2.7700 - 2.5200 1.00 4577 148 0.2272 0.2556
REMARK 3 5 2.5200 - 2.3400 1.00 4563 136 0.2279 0.2618
REMARK 3 6 2.3400 - 2.2000 1.00 4565 145 0.2161 0.2372
REMARK 3 7 2.2000 - 2.0900 1.00 4576 145 0.2163 0.2715
REMARK 3 8 2.0900 - 2.0000 1.00 4548 146 0.2212 0.2396
REMARK 3 9 2.0000 - 1.9200 1.00 4554 141 0.2242 0.2851
REMARK 3 10 1.9200 - 1.8600 1.00 4551 151 0.2301 0.2888
REMARK 3 11 1.8600 - 1.8000 1.00 4534 138 0.2369 0.2747
REMARK 3 12 1.8000 - 1.7500 1.00 4537 141 0.2380 0.3023
REMARK 3 13 1.7500 - 1.7000 0.99 4541 139 0.2503 0.2997
REMARK 3 14 1.7000 - 1.6600 0.94 4265 138 0.2685 0.3428
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 4025
REMARK 3 ANGLE : 0.811 5495
REMARK 3 CHIRALITY : 0.051 611
REMARK 3 PLANARITY : 0.009 732
REMARK 3 DIHEDRAL : 12.772 1445
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 9UTX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1300059144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97954
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65711
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 34.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V POLYETHYLENE GLYCOL 6000, 0.1
REMARK 280 M CITRIC ACID (PH 5.0), 30% V/V 2-METHYLPENTANE-2,4-DIOL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 27.64000
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
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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 67 O HOH A 301 2.07
REMARK 500 OG SER B 254 O HOH B 301 2.07
REMARK 500 O HOH A 309 O HOH A 311 2.08
REMARK 500 O PRO A 10 O HOH A 302 2.09
REMARK 500 OD1 ASN B 142 O HOH B 302 2.09
REMARK 500 O HOH A 301 O HOH B 305 2.10
REMARK 500 O HOH A 465 O HOH B 395 2.10
REMARK 500 OD1 ASP A 195 O HOH A 303 2.11
REMARK 500 NH1 ARG A 253 O HOH A 304 2.11
REMARK 500 O HOH B 317 O HOH B 424 2.12
REMARK 500 ND2 ASN A 2 O HOH A 305 2.13
REMARK 500 O HOH A 472 O HOH B 432 2.14
REMARK 500 O PHE B 229 O HOH B 303 2.15
REMARK 500 O HOH A 462 O HOH A 472 2.16
REMARK 500 OG1 THR B 111 O HOH B 304 2.18
REMARK 500 O HOH A 423 O HOH A 479 2.18
REMARK 500 NH2 ARG A 91 O HOH A 301 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 367 O HOH B 417 2655 2.17
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 SER A 130 -127.44 63.11
REMARK 500 HIS A 184 -91.99 -119.83
REMARK 500 PRO A 242 -177.80 -69.49
REMARK 500 THR A 255 44.42 -94.58
REMARK 500 SER B 130 -124.78 62.36
REMARK 500 ASN B 143 95.17 -161.84
REMARK 500 LEU B 175 33.31 -98.94
REMARK 500 HIS B 184 -95.80 -123.33
REMARK 500 THR B 255 51.59 -109.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9UTX A -3 258 PDB 9UTX 9UTX -3 258
DBREF 9UTX B -3 258 PDB 9UTX 9UTX -3 258
SEQRES 1 A 262 GLY PRO HIS MET ALA ASN PRO TYR GLU ARG GLY PRO ASP
SEQRES 2 A 262 PRO THR GLU SER SER ILE GLU ALA VAL ARG GLY PRO PHE
SEQRES 3 A 262 ALA VAL ALA GLN THR THR VAL SER ARG LEU GLN ALA ASP
SEQRES 4 A 262 GLY PHE GLY GLY GLY THR ILE TYR TYR PRO THR ASP THR
SEQRES 5 A 262 SER GLN GLY THR PHE GLY ALA VAL ALA ILE SER PRO GLY
SEQRES 6 A 262 PHE THR ALA GLY GLN GLU SER ILE ALA TRP LEU GLY PRO
SEQRES 7 A 262 ARG ILE ALA SER GLN GLY PHE VAL VAL ILE THR ILE ASP
SEQRES 8 A 262 THR ILE THR ARG LEU ASP GLN PRO ASP SER ARG GLY ARG
SEQRES 9 A 262 GLN LEU GLN ALA ALA LEU ASP HIS LEU ARG THR ASN SER
SEQRES 10 A 262 VAL VAL ARG ASN ARG ILE ASP PRO ASN ARG MET ALA VAL
SEQRES 11 A 262 MET GLY HIS SER MET GLY GLY GLY GLY ALA LEU SER ALA
SEQRES 12 A 262 ALA ALA ASN ASN THR SER LEU GLU ALA ALA ILE PRO LEU
SEQRES 13 A 262 GLN GLY TRP HIS THR ARG LYS ASN TRP SER SER VAL ARG
SEQRES 14 A 262 THR PRO THR LEU VAL VAL GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 262 ALA PRO VAL SER SER HIS SER GLU ALA PHE TYR ASN SER
SEQRES 16 A 262 LEU PRO SER ASP LEU ASP LYS ALA TYR MET GLU LEU ARG
SEQRES 17 A 262 GLY ALA SER HIS LEU VAL SER ASN THR PRO ASP THR THR
SEQRES 18 A 262 THR ALA LYS TYR SER ILE ALA TRP LEU LYS ARG PHE VAL
SEQRES 19 A 262 ASP ASP ASP LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA
SEQRES 20 A 262 PRO ASP ASP PHE ALA ILE SER GLU TYR ARG SER THR CYS
SEQRES 21 A 262 PRO PHE
SEQRES 1 B 262 GLY PRO HIS MET ALA ASN PRO TYR GLU ARG GLY PRO ASP
SEQRES 2 B 262 PRO THR GLU SER SER ILE GLU ALA VAL ARG GLY PRO PHE
SEQRES 3 B 262 ALA VAL ALA GLN THR THR VAL SER ARG LEU GLN ALA ASP
SEQRES 4 B 262 GLY PHE GLY GLY GLY THR ILE TYR TYR PRO THR ASP THR
SEQRES 5 B 262 SER GLN GLY THR PHE GLY ALA VAL ALA ILE SER PRO GLY
SEQRES 6 B 262 PHE THR ALA GLY GLN GLU SER ILE ALA TRP LEU GLY PRO
SEQRES 7 B 262 ARG ILE ALA SER GLN GLY PHE VAL VAL ILE THR ILE ASP
SEQRES 8 B 262 THR ILE THR ARG LEU ASP GLN PRO ASP SER ARG GLY ARG
SEQRES 9 B 262 GLN LEU GLN ALA ALA LEU ASP HIS LEU ARG THR ASN SER
SEQRES 10 B 262 VAL VAL ARG ASN ARG ILE ASP PRO ASN ARG MET ALA VAL
SEQRES 11 B 262 MET GLY HIS SER MET GLY GLY GLY GLY ALA LEU SER ALA
SEQRES 12 B 262 ALA ALA ASN ASN THR SER LEU GLU ALA ALA ILE PRO LEU
SEQRES 13 B 262 GLN GLY TRP HIS THR ARG LYS ASN TRP SER SER VAL ARG
SEQRES 14 B 262 THR PRO THR LEU VAL VAL GLY ALA GLU LEU ASP THR ILE
SEQRES 15 B 262 ALA PRO VAL SER SER HIS SER GLU ALA PHE TYR ASN SER
SEQRES 16 B 262 LEU PRO SER ASP LEU ASP LYS ALA TYR MET GLU LEU ARG
SEQRES 17 B 262 GLY ALA SER HIS LEU VAL SER ASN THR PRO ASP THR THR
SEQRES 18 B 262 THR ALA LYS TYR SER ILE ALA TRP LEU LYS ARG PHE VAL
SEQRES 19 B 262 ASP ASP ASP LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA
SEQRES 20 B 262 PRO ASP ASP PHE ALA ILE SER GLU TYR ARG SER THR CYS
SEQRES 21 B 262 PRO PHE
FORMUL 3 HOH *320(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 GLY A 65 ALA A 70 5 6
HELIX 3 AA3 TRP A 71 SER A 78 1 8
HELIX 4 AA4 GLN A 94 ASN A 112 1 19
HELIX 5 AA5 SER A 130 ASN A 142 1 13
HELIX 6 AA6 HIS A 184 LEU A 192 1 9
HELIX 7 AA7 SER A 207 THR A 213 5 7
HELIX 8 AA8 ASP A 215 ASP A 231 1 17
HELIX 9 AA9 ASP A 233 ARG A 235 5 3
HELIX 10 AB1 TYR A 236 CYS A 241 1 6
HELIX 11 AB2 THR B 11 ALA B 17 1 7
HELIX 12 AB3 GLY B 65 ALA B 70 5 6
HELIX 13 AB4 TRP B 71 SER B 78 1 8
HELIX 14 AB5 GLN B 94 ARG B 110 1 17
HELIX 15 AB6 SER B 130 ASN B 142 1 13
HELIX 16 AB7 HIS B 184 LEU B 192 1 9
HELIX 17 AB8 LEU B 209 THR B 213 5 5
HELIX 18 AB9 ASP B 215 ASP B 231 1 17
HELIX 19 AC1 ASP B 233 ARG B 235 5 3
HELIX 20 AC2 TYR B 236 CYS B 241 1 6
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 THR 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 VAL A 56 O ILE A 84
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O HIS A 129 N SER A 59
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O ALA A 199 N VAL A 170
SHEET 3 AA2 3 ILE A 249 SER A 254 -1 O ARG A 253 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 ILE B 42 N THR B 27
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 VAL B 56 O ILE B 84
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O MET B 127 N ALA B 57
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O ALA B 199 N VAL B 170
SHEET 3 AA4 3 ILE B 249 SER B 254 -1 O ARG B 253 N TYR B 200
SSBOND 1 CYS A 241 CYS A 256 1555 1555 2.02
SSBOND 2 CYS B 241 CYS B 256 1555 1555 2.03
CISPEP 1 CYS A 241 PRO A 242 0 -0.39
CISPEP 2 CYS A 256 PRO A 257 0 -7.33
CISPEP 3 CYS B 241 PRO B 242 0 -4.59
CISPEP 4 CYS B 256 PRO B 257 0 -7.29
CRYST1 51.310 55.280 99.820 90.00 94.85 90.00 P 1 21 1 4
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 0.019489 0.000000 0.001654 0.00000
SCALE2 0.000000 0.018090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010054 0.00000
TER 1963 PHE A 258
TER 3932 PHE B 258
MASTER 286 0 0 20 18 0 0 6 4244 2 4 42
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