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HEADER HYDROLASE 12-MAR-21 7ECB
TITLE POLYETHYLENE TEREPHTHALATE HYDROLYZING LIPASE PET2 MUTANT - R47C-G89C-
TITLE 2 F105R-E110K-S156P-G180A-T297P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPIAF5-2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: LIPIAF5-2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYETHYLENE TEREPHTHALATE HYDROLASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAKAMURA
REVDAT 1 07-JUL-21 7ECB 0
JRNL AUTH A.NAKAMURA
JRNL TITL POSITIVE CHARGE INTRODUCTION ON THE SURFACE OF
JRNL TITL 2 THERMOSTABILIZED PET HYDROLASE FACILITATES PET BINDING AND
JRNL TITL 3 DEGRADATION.
JRNL REF ACS CATALYSIS 2021
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.1C01204
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24346
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1217
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 38.0800 - 3.8100 1.00 2739 145 0.1276 0.1519
REMARK 3 2 3.8100 - 3.0300 1.00 2602 137 0.1353 0.1744
REMARK 3 3 3.0300 - 2.6400 1.00 2576 135 0.1484 0.1737
REMARK 3 4 2.6400 - 2.4000 1.00 2558 135 0.1570 0.2032
REMARK 3 5 2.4000 - 2.2300 1.00 2558 134 0.1512 0.2285
REMARK 3 6 2.2300 - 2.1000 1.00 2522 132 0.1628 0.2425
REMARK 3 7 2.1000 - 1.9900 1.00 2550 134 0.1632 0.2156
REMARK 3 8 1.9900 - 1.9100 1.00 2531 134 0.1845 0.2156
REMARK 3 9 1.9100 - 1.8300 0.98 2493 131 0.2147 0.2539
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.181
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.940
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.84
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 : 0.016 2056
REMARK 3 ANGLE : 1.244 2811
REMARK 3 CHIRALITY : 0.083 302
REMARK 3 PLANARITY : 0.008 369
REMARK 3 DIHEDRAL : 6.162 1201
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 7ECB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1300021143.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AICHISR
REMARK 200 BEAMLINE : BL2S1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24351
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 38.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.67600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 7EC8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350 IN 100 MM TRIS-HCL PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 33.62000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.62000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.36000
REMARK 290 SMTRY3 4 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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 672 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 675 LIES ON A SPECIAL POSITION.
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 ALA A 28
REMARK 465 ASN A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 GLY A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 PRO A 35
REMARK 465 ASP A 36
REMARK 465 PRO A 37
REMARK 465 GLY A 38
REMARK 465 CYS A 39
REMARK 465 GLN A 40
REMARK 465 THR A 41
REMARK 465 ASP A 42
REMARK 465 CYS A 43
REMARK 465 ASN A 44
REMARK 465 TYR A 45
REMARK 465 LEU A 311
REMARK 465 TYR A 312
REMARK 465 PHE A 313
REMARK 465 GLN A 314
REMARK 465 GLY A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
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 SG CYS A 47 SG CYS A 89 1.64
REMARK 500 NH2 ARG A 208 O HOH A 401 2.05
REMARK 500 O HOH A 612 O HOH A 613 2.06
REMARK 500 O HOH A 445 O HOH A 597 2.08
REMARK 500 OD1 ASP A 187 O HOH A 401 2.12
REMARK 500 O HOH A 551 O HOH A 610 2.12
REMARK 500 O HOH A 495 O HOH A 637 2.14
REMARK 500 O HOH A 525 O HOH A 648 2.18
REMARK 500 O HOH A 583 O HOH A 602 2.19
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 A 418 O HOH A 583 4554 1.97
REMARK 500 O HOH A 483 O HOH A 626 4554 2.04
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 175 -129.73 66.69
REMARK 500 ASN A 207 3.36 -68.39
REMARK 500 HIS A 229 -86.31 -125.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 686 DISTANCE = 6.59 ANGSTROMS
DBREF 7ECB A 28 308 UNP C3RYL0 C3RYL0_9BACT 28 308
SEQADV 7ECB CYS A 47 UNP C3RYL0 ARG 47 ENGINEERED MUTATION
SEQADV 7ECB CYS A 89 UNP C3RYL0 GLY 89 ENGINEERED MUTATION
SEQADV 7ECB ARG A 105 UNP C3RYL0 PHE 105 ENGINEERED MUTATION
SEQADV 7ECB LYS A 110 UNP C3RYL0 GLU 110 ENGINEERED MUTATION
SEQADV 7ECB PRO A 156 UNP C3RYL0 SER 156 ENGINEERED MUTATION
SEQADV 7ECB ALA A 180 UNP C3RYL0 GLY 180 ENGINEERED MUTATION
SEQADV 7ECB PRO A 297 UNP C3RYL0 THR 297 ENGINEERED MUTATION
SEQADV 7ECB GLU A 309 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB ASN A 310 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB LEU A 311 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB TYR A 312 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB PHE A 313 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB GLN A 314 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB GLY A 315 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 316 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 317 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 318 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 319 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 320 UNP C3RYL0 EXPRESSION TAG
SEQADV 7ECB HIS A 321 UNP C3RYL0 EXPRESSION TAG
SEQRES 1 A 294 ALA ASN PRO PRO GLY GLY ASP PRO ASP PRO GLY CYS GLN
SEQRES 2 A 294 THR ASP CYS ASN TYR GLN CYS GLY PRO ASP PRO THR ASP
SEQRES 3 A 294 ALA TYR LEU GLU ALA ALA SER GLY PRO TYR THR VAL SER
SEQRES 4 A 294 THR ILE ARG VAL SER SER LEU VAL PRO GLY PHE GLY GLY
SEQRES 5 A 294 GLY THR ILE HIS TYR PRO THR ASN ALA CYS GLY GLY LYS
SEQRES 6 A 294 MET ALA GLY ILE VAL VAL ILE PRO GLY TYR LEU SER ARG
SEQRES 7 A 294 GLU SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 A 294 HIS GLY PHE VAL VAL MET THR ILE ASP THR ASN THR ILE
SEQRES 9 A 294 TYR ASP GLN PRO SER GLN ARG ARG ASP GLN ILE GLU ALA
SEQRES 10 A 294 ALA LEU GLN TYR LEU VAL ASN GLN SER ASN SER PRO SER
SEQRES 11 A 294 SER PRO ILE SER GLY MET VAL ASP SER SER ARG LEU ALA
SEQRES 12 A 294 ALA VAL GLY TRP SER MET GLY GLY GLY ALA THR LEU GLN
SEQRES 13 A 294 LEU ALA ALA ASP GLY GLY ILE LYS ALA ALA ILE ALA LEU
SEQRES 14 A 294 ALA PRO TRP ASN SER SER ILE ASN ASP PHE ASN ARG ILE
SEQRES 15 A 294 GLN VAL PRO THR LEU ILE PHE ALA CYS GLN LEU ASP ALA
SEQRES 16 A 294 ILE ALA PRO VAL ALA LEU HIS ALA SER PRO PHE TYR ASN
SEQRES 17 A 294 ARG ILE PRO ASN THR THR PRO LYS ALA PHE PHE GLU MET
SEQRES 18 A 294 THR GLY GLY ASP HIS TRP CYS ALA ASN GLY GLY ASN ILE
SEQRES 19 A 294 TYR SER ALA LEU LEU GLY LYS TYR GLY VAL SER TRP MET
SEQRES 20 A 294 LYS LEU HIS LEU ASP GLN ASP THR ARG TYR ALA PRO PHE
SEQRES 21 A 294 LEU CYS GLY PRO ASN HIS ALA ALA GLN PRO LEU ILE SER
SEQRES 22 A 294 GLU TYR ARG GLY ASN CYS PRO TYR GLU ASN LEU TYR PHE
SEQRES 23 A 294 GLN GLY HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *286(H2 O)
HELIX 1 AA1 THR A 52 ALA A 58 1 7
HELIX 2 AA2 ARG A 105 LYS A 110 5 6
HELIX 3 AA3 TRP A 111 SER A 118 1 8
HELIX 4 AA4 GLN A 134 ASN A 154 1 21
HELIX 5 AA5 SER A 175 GLY A 188 1 14
HELIX 6 AA6 ASP A 205 ILE A 209 5 5
HELIX 7 AA7 HIS A 229 ILE A 237 1 9
HELIX 8 AA8 TRP A 254 GLY A 258 5 5
HELIX 9 AA9 TYR A 262 ASP A 279 1 18
HELIX 10 AB1 ASP A 281 LEU A 288 5 8
HELIX 11 AB2 ASN A 292 GLN A 296 5 5
SHEET 1 AA1 9 VAL A 65 VAL A 70 0
SHEET 2 AA1 9 GLY A 80 PRO A 85 -1 O GLY A 80 N VAL A 70
SHEET 3 AA1 9 VAL A 122 ILE A 126 -1 O VAL A 123 N HIS A 83
SHEET 4 AA1 9 MET A 93 ILE A 99 1 N ILE A 96 O MET A 124
SHEET 5 AA1 9 VAL A 164 TRP A 174 1 O ASP A 165 N MET A 93
SHEET 6 AA1 9 ALA A 192 LEU A 196 1 O LEU A 196 N GLY A 173
SHEET 7 AA1 9 THR A 213 CYS A 218 1 O PHE A 216 N ALA A 195
SHEET 8 AA1 9 LYS A 243 MET A 248 1 O MET A 248 N ALA A 217
SHEET 9 AA1 9 ILE A 299 GLY A 304 -1 O GLU A 301 N GLU A 247
SSBOND 1 CYS A 218 CYS A 255 1555 1555 2.02
SSBOND 2 CYS A 289 CYS A 306 1555 1555 2.01
CISPEP 1 CYS A 306 PRO A 307 0 -3.63
CRYST1 67.240 86.720 46.210 90.00 90.00 90.00 P 21 21 2 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 0.014872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021640 0.00000
TER 1997 ASN A 310
MASTER 311 0 0 11 9 0 0 6 2282 1 4 23
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