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HEADER HYDROLASE 08-OCT-21 7SH6
TITLE CRYSTAL STRUCTURE OF A PET HYDROLASE MUTANT FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: PSEUDOMONAS PUTIDA KT2440;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 160488
KEYWDS PET HYDROLASE, PET DEGRADATION, PROTEIN ENGINEERING, MACHINE
KEYWDS 2 LEARNING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.KIM,Y.ZHANG
REVDAT 1 06-APR-22 7SH6 0
JRNL AUTH H.LU,D.J.DIAZ,N.J.CZARNECKI,C.ZHU,W.KIM,R.SHROFF,D.J.ACOSTA,
JRNL AUTH 2 B.ALEXANDER,H.COLE,Y.ZHANG,N.LYND,A.D.ELLINGTON,H.S.ALPER
JRNL TITL MACHINE LEARNING-AIDED ENGINEERING OF HYDROLASES FOR PET
JRNL TITL 2 DEPOLYMERIZATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18RC3_3805
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) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 40272
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1988
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 43.7100 - 3.4700 0.99 2922 147 0.2120 0.1974
REMARK 3 2 3.4700 - 2.7500 1.00 2832 145 0.1611 0.1447
REMARK 3 3 2.7500 - 2.4000 1.00 2736 144 0.1518 0.1618
REMARK 3 4 2.4000 - 2.1800 1.00 2783 143 0.1442 0.1577
REMARK 3 5 2.1800 - 2.0300 1.00 2754 144 0.1380 0.1587
REMARK 3 6 2.0300 - 1.9100 1.00 2733 143 0.1407 0.1383
REMARK 3 7 1.9100 - 1.8100 1.00 2736 142 0.1467 0.1867
REMARK 3 8 1.8100 - 1.7300 1.00 2735 143 0.1453 0.1657
REMARK 3 9 1.7300 - 1.6700 1.00 2725 141 0.1417 0.1747
REMARK 3 10 1.6700 - 1.6100 1.00 2700 142 0.1343 0.1680
REMARK 3 11 1.6100 - 1.5600 1.00 2721 138 0.1412 0.1826
REMARK 3 12 1.5600 - 1.5100 1.00 2735 142 0.1382 0.1504
REMARK 3 13 1.5100 - 1.4800 0.98 2648 142 0.1469 0.1788
REMARK 3 14 1.4800 - 1.4400 0.92 2524 132 0.1716 0.2180
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.68
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 2044
REMARK 3 ANGLE : 0.865 2804
REMARK 3 CHIRALITY : 0.083 306
REMARK 3 PLANARITY : 0.006 373
REMARK 3 DIHEDRAL : 6.029 301
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 7SH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1000260280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03317
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 : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40349
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.19500
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: 6IJ6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 5.5, 2.0M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.47100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.02350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.59100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.02350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.47100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.59100
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 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 7
REMARK 465 SER A 8
REMARK 465 HIS A 9
REMARK 465 ILE A 10
REMARK 465 LEU A 11
REMARK 465 ARG A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 VAL A 15
REMARK 465 LEU A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 MET A 19
REMARK 465 LEU A 20
REMARK 465 LEU A 21
REMARK 465 PRO A 22
REMARK 465 LEU A 23
REMARK 465 PRO A 24
REMARK 465 SER A 25
REMARK 465 MET A 26
REMARK 465 ALA A 27
REMARK 465 GLN A 28
REMARK 465 SER A 290
REMARK 465 LEU A 291
REMARK 465 GLU A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
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 THR A 29 OG1 CG2
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 O HOH A 409 O HOH A 689 1.85
REMARK 500 O HOH A 520 O HOH A 656 1.88
REMARK 500 O HOH A 587 O HOH A 620 1.96
REMARK 500 O HOH A 686 O HOH A 724 1.97
REMARK 500 O HOH A 520 O HOH A 680 1.98
REMARK 500 O HOH A 620 O HOH A 714 1.98
REMARK 500 O HOH A 690 O HOH A 715 2.03
REMARK 500 O HOH A 410 O HOH A 694 2.03
REMARK 500 O HOH A 590 O HOH A 693 2.06
REMARK 500 O HOH A 694 O HOH A 736 2.07
REMARK 500 OD1 ASN A 212 O HOH A 401 2.07
REMARK 500 O HOH A 665 O HOH A 673 2.08
REMARK 500 O HOH A 439 O HOH A 524 2.09
REMARK 500 O HOH A 700 O HOH A 753 2.12
REMARK 500 O HOH A 540 O HOH A 623 2.13
REMARK 500 OG SER A 58 O HOH A 402 2.17
REMARK 500 O HOH A 606 O HOH A 626 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 A 409 O HOH A 710 3445 1.91
REMARK 500 O HOH A 618 O HOH A 660 4545 1.92
REMARK 500 O HOH A 559 O HOH A 732 4545 2.18
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 ASN A 73 30.50 -142.46
REMARK 500 THR A 88 -10.28 73.03
REMARK 500 SER A 160 -118.12 64.36
REMARK 500 HIS A 186 145.84 -173.79
REMARK 500 SER A 214 -81.09 -129.04
REMARK 500 SER A 214 -82.58 -128.04
REMARK 500 SER A 214 -84.76 -126.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7SH6 A 27 290 UNP PETH_IDESA
DBREF2 7SH6 A A0A0K8P6T7 27 290
SEQADV 7SH6 MET A 7 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 7SH6 SER A 8 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 9 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ILE A 10 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 LEU A 11 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ARG A 12 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ALA A 13 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ALA A 14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 VAL A 15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 LEU A 16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ALA A 17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 ALA A 18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 MET A 19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 LEU A 20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 LEU A 21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 PRO A 22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 LEU A 23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 PRO A 24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 SER A 25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 MET A 26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 7SH6 HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 7SH6 GLN A 224 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 7SH6 LYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 7SH6 ALA A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 7SH6 LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7SH6 HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 292 MET SER HIS ILE LEU ARG ALA ALA VAL LEU ALA ALA MET
SEQRES 2 A 292 LEU LEU PRO LEU PRO SER MET ALA GLN THR ASN PRO TYR
SEQRES 3 A 292 ALA ARG GLY PRO ASN PRO THR ALA ALA SER LEU GLU ALA
SEQRES 4 A 292 SER ALA GLY PRO PHE THR VAL ARG SER PHE THR VAL SER
SEQRES 5 A 292 ARG PRO SER GLY TYR GLY ALA GLY THR VAL TYR TYR PRO
SEQRES 6 A 292 THR ASN ALA GLY GLY THR VAL GLY ALA ILE ALA ILE VAL
SEQRES 7 A 292 PRO GLY TYR THR ALA ARG GLN SER SER ILE LYS TRP TRP
SEQRES 8 A 292 GLY PRO ARG LEU ALA SER HIS GLY PHE VAL VAL ILE THR
SEQRES 9 A 292 ILE ASP THR ASN SER THR LEU ASP GLN PRO GLU SER ARG
SEQRES 10 A 292 SER SER GLN GLN MET ALA ALA LEU ARG GLN VAL ALA SER
SEQRES 11 A 292 LEU ASN GLY THR SER SER SER PRO ILE TYR GLY LYS VAL
SEQRES 12 A 292 ASP THR ALA ARG MET GLY VAL MET GLY TRP SER MET GLY
SEQRES 13 A 292 GLY GLY GLY SER LEU ILE SER ALA ALA ASN ASN PRO SER
SEQRES 14 A 292 LEU LYS ALA ALA ALA PRO GLN ALA PRO TRP HIS SER SER
SEQRES 15 A 292 THR ASN PHE SER SER VAL THR VAL PRO THR LEU ILE PHE
SEQRES 16 A 292 ALA CYS GLU ASN ASP SER ILE ALA PRO VAL ASN SER SER
SEQRES 17 A 292 ALA LEU PRO ILE TYR ASP SER MET SER GLN ASN ALA LYS
SEQRES 18 A 292 GLN PHE LEU GLU ILE LYS GLY GLY SER HIS SER CYS ALA
SEQRES 19 A 292 ASN SER GLY ASN SER ASN GLN ALA LEU ILE GLY LYS LYS
SEQRES 20 A 292 GLY VAL ALA TRP MET LYS ARG PHE MET ASP ASN ASP THR
SEQRES 21 A 292 ARG TYR SER THR PHE ALA CYS GLU ASN PRO ASN SER THR
SEQRES 22 A 292 ALA VAL SER ASP PHE ARG THR ALA ASN CYS SER LEU GLU
SEQRES 23 A 292 HIS HIS HIS HIS HIS HIS
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *362(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.03
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.04
CRYST1 50.942 51.182 84.047 90.00 90.00 90.00 P 21 21 21 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 0.019630 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011898 0.00000
TER 1982 CYS A 289
MASTER 316 0 1 9 9 0 0 6 2282 1 9 23
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