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HEADER HYDROLASE 03-SEP-17 5YB5
TITLE THE COMPLEX CRYSTAL STRUCTURE OF VREH2 MUTANT M263N WITH SNO
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, STYRENE OXIDE.
EXPDTA X-RAY DIFFRACTION
AUTHOR F.L.LI,F.F.CHEN,Q.CHEN,X.D.KONG,H.L.YU,J.H.XU
REVDAT 1 05-SEP-18 5YB5 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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 24122
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1234
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 45.9333 - 3.9583 0.99 2786 138 0.1647 0.2017
REMARK 3 2 3.9583 - 3.1420 0.99 2631 120 0.1780 0.2355
REMARK 3 3 3.1420 - 2.7449 0.99 2556 154 0.2004 0.2549
REMARK 3 4 2.7449 - 2.4940 0.98 2532 132 0.2129 0.3003
REMARK 3 5 2.4940 - 2.3152 0.98 2505 149 0.2229 0.3044
REMARK 3 6 2.3152 - 2.1787 0.98 2497 132 0.2354 0.3104
REMARK 3 7 2.1787 - 2.0696 0.98 2487 123 0.2435 0.3078
REMARK 3 8 2.0696 - 1.9795 0.97 2458 160 0.2728 0.3220
REMARK 3 9 1.9795 - 1.9033 0.96 2436 126 0.3029 0.3997
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.150
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 : 0.009 2648
REMARK 3 ANGLE : 1.178 3604
REMARK 3 CHIRALITY : 0.081 378
REMARK 3 PLANARITY : 0.006 467
REMARK 3 DIHEDRAL : 13.981 955
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 5YB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300004976.
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 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24144
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 16.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4940
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 16.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.160
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 (%): 38.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS-HCL, ETHYLENE GLYCOL,
REMARK 280 PH 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 60.64750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.14850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.14850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 90.97125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.14850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.14850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.32375
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.14850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.14850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 90.97125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.14850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.14850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.32375
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 60.64750
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: 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 OE1 -0.069
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 -159.81 -108.94
REMARK 500 ASP B 101 -131.67 61.10
REMARK 500 SER B 125 -58.46 69.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SNO B 401
DBREF1 5YB5 B 1 318 UNP A0A0R5NGA4_VIGRA
DBREF2 5YB5 B A0A0R5NGA4 1 318
SEQADV 5YB5 GLU B 3 UNP A0A0R5NGA GLY 3 ENGINEERED MUTATION
SEQADV 5YB5 ILE B 4 UNP A0A0R5NGA VAL 4 ENGINEERED MUTATION
SEQADV 5YB5 ASN B 263 UNP A0A0R5NGA MET 263 ENGINEERED MUTATION
SEQADV 5YB5 LEU B 319 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 GLU B 320 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 HIS B 321 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 HIS B 322 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 HIS B 323 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 HIS B 324 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 HIS B 325 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 5YB5 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
HET SNO B 401 12
HETNAM SNO (S)-PARA-NITROSTYRENE OXIDE
HETSYN SNO (2S)-2-(4-NITROPHENYL)OXIRANE
FORMUL 2 SNO C8 H7 N O3
FORMUL 3 HOH *150(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 LEU B 90 1 16
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 GLN B 155 1 7
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 GLU B 20 N GLU B 5
SHEET 3 AA1 8 ARG B 53 PRO B 57 -1 O ALA B 54 N LYS B 21
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 LYS B 255 N TYR B 121
SHEET 8 AA1 8 LEU B 286 GLN B 292 1 O GLN B 292 N THR B 258
CISPEP 1 PHE B 33 PRO B 34 0 -14.98
SITE 1 AC1 10 PHE B 33 ASP B 101 TYR B 150 ILE B 176
SITE 2 AC1 10 PHE B 196 TYR B 232 ASN B 263 HIS B 297
SITE 3 AC1 10 PHE B 298 HOH B 630
CRYST1 70.297 70.297 121.295 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 0.014225 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008244 0.00000
TER 2559 PHE B 318
MASTER 270 0 1 17 8 0 3 6 2720 1 12 26
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