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HEADER HYDROLASE 15-AUG-17 5Y6Y
TITLE THE CRYSTAL STRUCTURE OF VREH2 MUTANT M263N
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIGNA RADIATA;
SOURCE 3 ORGANISM_COMMON: MUNG BEAN;
SOURCE 4 ORGANISM_TAXID: 157791;
SOURCE 5 GENE: EH2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE, EPOXIDE HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.L.LI,H.L.YU,Q.CHEN,X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT 1 05-SEP-18 5Y6Y 0
JRNL AUTH F.L.LI,X.D.KONG,Q.CHEN,Y.C.ZHENG,Q.XU,F.F.CHEN,L.Q.FAN,
JRNL AUTH 2 G.Q.LIN,J.H.ZHOU,H.L.YU,J.H.XU
JRNL TITL REGIOSELECTIVITY ENGINEERING OF EPOXIDE HYDROLASE:
JRNL TITL 2 NEAR-PERFECT ENANTIOCONVERGENCE THROUGH A SINGLE SITE
JRNL TITL 3 MUTATION
JRNL REF ACS CATALYSIS V. 8 8314 2018
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B02622
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 51453
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2619
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 49.3609 - 3.9944 0.99 2847 143 0.1839 0.2084
REMARK 3 2 3.9944 - 3.1706 1.00 2721 139 0.1664 0.1787
REMARK 3 3 3.1706 - 2.7699 1.00 2685 149 0.1839 0.2043
REMARK 3 4 2.7699 - 2.5167 1.00 2645 142 0.1749 0.1917
REMARK 3 5 2.5167 - 2.3363 1.00 2641 147 0.1705 0.1727
REMARK 3 6 2.3363 - 2.1985 1.00 2624 141 0.1682 0.1950
REMARK 3 7 2.1985 - 2.0884 1.00 2658 124 0.1604 0.1900
REMARK 3 8 2.0884 - 1.9975 1.00 2586 138 0.1606 0.2050
REMARK 3 9 1.9975 - 1.9206 1.00 2654 122 0.1688 0.1682
REMARK 3 10 1.9206 - 1.8543 1.00 2581 144 0.1691 0.1992
REMARK 3 11 1.8543 - 1.7964 1.00 2615 137 0.1667 0.1960
REMARK 3 12 1.7964 - 1.7450 1.00 2587 136 0.1808 0.2025
REMARK 3 13 1.7450 - 1.6991 1.00 2566 145 0.1757 0.2217
REMARK 3 14 1.6991 - 1.6576 1.00 2579 154 0.1826 0.2203
REMARK 3 15 1.6576 - 1.6199 0.99 2558 139 0.1784 0.2005
REMARK 3 16 1.6199 - 1.5854 0.99 2562 141 0.1881 0.2210
REMARK 3 17 1.5854 - 1.5537 0.94 2414 138 0.1961 0.2022
REMARK 3 18 1.5537 - 1.5244 0.88 2305 118 0.2015 0.2348
REMARK 3 19 1.5244 - 1.4972 0.78 2006 122 0.2211 0.2689
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.060
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 : 0.007 2634
REMARK 3 ANGLE : 1.103 3584
REMARK 3 CHIRALITY : 0.076 377
REMARK 3 PLANARITY : 0.006 464
REMARK 3 DIHEDRAL : 12.858 954
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 5Y6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3-8.6
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) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : 0.09400
REMARK 200 FOR THE DATA SET : 27.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.30
REMARK 200 R MERGE FOR SHELL (I) : 0.70200
REMARK 200 R SYM FOR SHELL (I) : 1.06900
REMARK 200 FOR SHELL : 2.500
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: 5XMD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRI-HCL, ETHYLENE GLYCOL, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 65.25750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.88450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.88450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 97.88625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.88450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.88450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.62875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.88450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.88450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 97.88625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.88450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.88450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.62875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.25750
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: 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 LEU B 319
REMARK 465 GLU B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
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 B 660 O HOH B 678 1.93
REMARK 500 O HOH B 673 O HOH B 680 2.03
REMARK 500 O HOH B 665 O HOH B 689 2.07
REMARK 500 O HOH B 615 O HOH B 685 2.08
REMARK 500 O HOH B 697 O HOH B 732 2.10
REMARK 500 O HOH B 629 O HOH B 668 2.15
REMARK 500 O HOH B 434 O HOH B 638 2.18
REMARK 500 O HOH B 669 O HOH B 674 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 483 O HOH B 661 4455 2.07
REMARK 500 O HOH B 684 O HOH B 743 6555 2.09
REMARK 500 O HOH B 657 O HOH B 679 8555 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 35 CD GLU B 35 OE2 -0.116
REMARK 500 SER B 72 CB SER B 72 OG -0.088
REMARK 500 GLU B 260 CD GLU B 260 OE2 -0.088
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 GLU B 35 -154.82 -112.65
REMARK 500 ASP B 101 -128.31 59.66
REMARK 500 SER B 125 -58.16 77.57
REMARK 500 PHE B 298 58.32 -91.08
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 5Y6Y B 1 318 UNP A0A0R5NGA4_VIGRA
DBREF2 5Y6Y B A0A0R5NGA4 1 318
SEQADV 5Y6Y GLU B 3 UNP A0A0R5NGA GLY 3 ENGINEERED MUTATION
SEQADV 5Y6Y ILE B 4 UNP A0A0R5NGA VAL 4 ENGINEERED MUTATION
SEQADV 5Y6Y ASN B 263 UNP A0A0R5NGA MET 263 ENGINEERED MUTATION
SEQADV 5Y6Y LEU B 319 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y GLU B 320 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 321 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 322 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 323 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 324 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 325 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5Y6Y HIS B 326 UNP A0A0R5NGA EXPRESSION TAG
SEQRES 1 B 326 MET GLU GLU ILE GLU HIS ARG THR VAL GLU VAL ASN GLY
SEQRES 2 B 326 ILE LYS MET HIS VAL ALA GLU LYS GLY GLU GLY PRO VAL
SEQRES 3 B 326 VAL LEU PHE LEU HIS GLY PHE PRO GLU LEU TRP TYR SER
SEQRES 4 B 326 TRP ARG HIS GLN ILE LEU ALA LEU SER SER ARG GLY TYR
SEQRES 5 B 326 ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY ASP THR
SEQRES 6 B 326 GLU ALA PRO VAL SER ILE SER SER TYR THR GLY PHE HIS
SEQRES 7 B 326 ILE VAL GLY ASP LEU ILE ALA LEU ILE ASP LEU LEU GLY
SEQRES 8 B 326 VAL ASP GLN VAL PHE LEU VAL ALA HIS ASP TRP GLY ALA
SEQRES 9 B 326 ILE ILE GLY TRP TYR LEU CYS THR PHE HIS PRO ASP ARG
SEQRES 10 B 326 VAL LYS ALA TYR VAL CYS LEU SER VAL PRO LEU LEU HIS
SEQRES 11 B 326 ARG ASP PRO ASN ILE ARG THR VAL ASP ALA MET ARG ALA
SEQRES 12 B 326 MET TYR GLY ASP ASP TYR TYR ILE CYS ARG PHE GLN LYS
SEQRES 13 B 326 PRO GLY GLU MET GLU ALA GLN MET ALA GLU VAL GLY THR
SEQRES 14 B 326 GLU TYR VAL LEU LYS ASN ILE LEU THR THR ARG LYS PRO
SEQRES 15 B 326 GLY PRO PRO ILE PHE PRO LYS GLY GLU TYR GLY THR GLY
SEQRES 16 B 326 PHE ASN PRO ASP MET PRO ASN SER LEU PRO SER TRP LEU
SEQRES 17 B 326 THR GLN ASP ASP LEU ALA TYR TYR VAL SER LYS TYR GLU
SEQRES 18 B 326 LYS THR GLY PHE THR GLY PRO LEU ASN TYR TYR ARG ASN
SEQRES 19 B 326 MET ASN LEU ASN TRP GLU LEU THR ALA PRO TRP SER GLY
SEQRES 20 B 326 GLY LYS ILE GLN VAL PRO VAL LYS PHE ILE THR GLY GLU
SEQRES 21 B 326 LEU ASP ASN VAL TYR THR SER LEU ASN MET LYS GLU TYR
SEQRES 22 B 326 ILE HIS GLY GLY GLY PHE LYS GLN ASP VAL PRO ASN LEU
SEQRES 23 B 326 GLU GLU VAL ILE VAL GLN LYS ASN VAL ALA HIS PHE ASN
SEQRES 24 B 326 ASN GLN GLU ALA ALA GLU GLU ILE ASN ASN HIS ILE TYR
SEQRES 25 B 326 ASP PHE ILE LYS LYS PHE LEU GLU HIS HIS HIS HIS HIS
SEQRES 26 B 326 HIS
FORMUL 2 HOH *350(H2 O)
HELIX 1 AA1 LEU B 36 SER B 39 5 4
HELIX 2 AA2 TRP B 40 ARG B 50 1 11
HELIX 3 AA3 SER B 70 TYR B 74 5 5
HELIX 4 AA4 THR B 75 GLY B 91 1 17
HELIX 5 AA5 ASP B 101 HIS B 114 1 14
HELIX 6 AA6 ARG B 136 GLY B 146 1 11
HELIX 7 AA7 TYR B 149 PHE B 154 1 6
HELIX 8 AA8 GLY B 158 GLY B 168 1 11
HELIX 9 AA9 GLY B 168 THR B 178 1 11
HELIX 10 AB1 THR B 209 GLY B 224 1 16
HELIX 11 AB2 PHE B 225 ARG B 233 1 9
HELIX 12 AB3 ASN B 234 THR B 242 1 9
HELIX 13 AB4 ALA B 243 SER B 246 5 4
HELIX 14 AB5 ASN B 269 GLY B 277 1 9
HELIX 15 AB6 GLY B 277 VAL B 283 1 7
HELIX 16 AB7 PHE B 298 ALA B 303 1 6
HELIX 17 AB8 ALA B 303 LYS B 317 1 15
SHEET 1 AA1 8 GLU B 5 VAL B 11 0
SHEET 2 AA1 8 ILE B 14 LYS B 21 -1 O MET B 16 N VAL B 9
SHEET 3 AA1 8 ARG B 53 PRO B 57 -1 O ALA B 56 N ALA B 19
SHEET 4 AA1 8 VAL B 26 LEU B 30 1 N PHE B 29 O VAL B 55
SHEET 5 AA1 8 VAL B 95 HIS B 100 1 O PHE B 96 N LEU B 28
SHEET 6 AA1 8 VAL B 118 LEU B 124 1 O VAL B 122 N LEU B 97
SHEET 7 AA1 8 VAL B 254 GLY B 259 1 O ILE B 257 N CYS B 123
SHEET 8 AA1 8 ILE B 290 GLN B 292 1 O GLN B 292 N THR B 258
CISPEP 1 PHE B 33 PRO B 34 0 -11.48
CRYST1 69.769 69.769 130.515 90.00 90.00 90.00 P 43 21 2 8
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 0.014333 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014333 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007662 0.00000
TER 2559 PHE B 318
MASTER 316 0 0 17 8 0 0 6 2908 1 0 26
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