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HEADER HYDROLASE 30-JUN-20 7CG6
TITLE VIGNA RADIATA EPOXIDE HYDROLASE MUTANT M263Q
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 EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.L.LI,H.L.YU,J.H.XU
REVDAT 1 07-JUL-21 7CG6 0
JRNL AUTH F.L.LI,Y.Y.QIU,Y.C.ZHENG,F.F.CHEN,X.D.KONG,J.H.XU,H.L.YU
JRNL TITL REPROGRAMMING EPOXIDE HYDROLASE TO IMPROVE
JRNL TITL 2 ENANTIOCONVERGENCE IN HYDROLYSIS OF STYRENE OXIDE SCAFFOLDS
JRNL REF ADV.SYNTH.CATAL. V. 362 4699 2021
JRNL REFN ESSN 1615-4169
JRNL DOI 10.1002/ADSC.202000898
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 21353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1093
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 34.1100 - 3.9978 1.00 2898 131 0.1654 0.2186
REMARK 3 2 3.9978 - 3.1739 0.96 2627 126 0.1840 0.2847
REMARK 3 3 3.1739 - 2.7729 1.00 2670 164 0.2242 0.2809
REMARK 3 4 2.7729 - 2.5195 0.99 2611 162 0.2580 0.3491
REMARK 3 5 2.5195 - 2.3389 1.00 2642 147 0.2613 0.3191
REMARK 3 6 2.3389 - 2.2010 0.74 1953 104 0.3294 0.4572
REMARK 3 7 2.2010 - 2.0908 1.00 2631 136 0.2901 0.3434
REMARK 3 8 2.0908 - 2.0000 0.85 2228 123 0.4212 0.4752
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.46
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 2635
REMARK 3 ANGLE : 1.066 3585
REMARK 3 CHIRALITY : 0.073 377
REMARK 3 PLANARITY : 0.006 464
REMARK 3 DIHEDRAL : 13.756 955
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 7CG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017550.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JAN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22019
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 97.1
REMARK 200 DATA REDUNDANCY : 22.00
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 46.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.30
REMARK 200 R MERGE FOR SHELL (I) : 0.85600
REMARK 200 R SYM FOR SHELL (I) : 0.85600
REMARK 200 FOR SHELL : 4.320
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: 5Y6Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M TRIS-HCL, PH 8.5, 35% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 63.68850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.40650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.40650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 95.53275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.40650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.40650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.84425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.40650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.40650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 95.53275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.40650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.40650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.84425
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 63.68850
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 MET B -1
REMARK 465 GLY B 0
REMARK 465 LEU B 319
REMARK 465 GLN 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 575 O HOH B 651 1.86
REMARK 500 O HOH B 503 O HOH B 590 1.93
REMARK 500 OE2 GLU B 159 O HOH B 401 1.93
REMARK 500 O HOH B 470 O HOH B 529 1.94
REMARK 500 O HOH B 508 O HOH B 519 1.95
REMARK 500 O HOH B 457 O HOH B 596 2.02
REMARK 500 OE1 GLU B 23 O HOH B 402 2.09
REMARK 500 O HOH B 445 O HOH B 584 2.11
REMARK 500 O HOH B 527 O HOH B 653 2.11
REMARK 500 O HOH B 601 O HOH B 613 2.12
REMARK 500 OD2 ASP B 313 O HOH B 403 2.15
REMARK 500 O PHE B 187 O HOH B 404 2.17
REMARK 500 NH2 ARG B 50 O HOH B 405 2.18
REMARK 500 O GLU B 221 O HOH B 406 2.18
REMARK 500 O HOH B 596 O HOH B 654 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 561 O HOH B 561 7555 1.43
REMARK 500 O HOH B 591 O HOH B 597 4555 1.78
REMARK 500 O HOH B 589 O HOH B 615 7555 2.03
REMARK 500 O HOH B 604 O HOH B 623 5544 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 PRO B 34 72.81 -101.99
REMARK 500 GLU B 35 -159.50 -110.98
REMARK 500 ASP B 101 -127.86 66.91
REMARK 500 SER B 125 -59.27 74.93
REMARK 500 THR B 266 31.99 -95.94
REMARK 500 GLU B 287 -108.66 -76.38
REMARK 500 ALA B 296 -142.03 -99.18
REMARK 500 ALA B 303 61.15 -117.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7CG6 B 5 318 UNP A0A0R5NGA4_VIGRA
DBREF2 7CG6 B A0A0R5NGA4 5 318
SEQADV 7CG6 MET B -1 UNP A0A0R5NGA INITIATING METHIONINE
SEQADV 7CG6 GLY B 0 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 MET B 1 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 GLU B 2 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 GLU B 3 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 ILE B 4 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 GLN B 263 UNP A0A0R5NGA MET 263 ENGINEERED MUTATION
SEQADV 7CG6 LEU B 319 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 GLN B 320 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 321 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 322 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 323 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 324 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 325 UNP A0A0R5NGA EXPRESSION TAG
SEQADV 7CG6 HIS B 326 UNP A0A0R5NGA EXPRESSION TAG
SEQRES 1 B 328 MET GLY MET GLU GLU ILE GLU HIS ARG THR VAL GLU VAL
SEQRES 2 B 328 ASN GLY ILE LYS MET HIS VAL ALA GLU LYS GLY GLU GLY
SEQRES 3 B 328 PRO VAL VAL LEU PHE LEU HIS GLY PHE PRO GLU LEU TRP
SEQRES 4 B 328 TYR SER TRP ARG HIS GLN ILE LEU ALA LEU SER SER ARG
SEQRES 5 B 328 GLY TYR ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY
SEQRES 6 B 328 ASP THR GLU ALA PRO VAL SER ILE SER SER TYR THR GLY
SEQRES 7 B 328 PHE HIS ILE VAL GLY ASP LEU ILE ALA LEU ILE ASP LEU
SEQRES 8 B 328 LEU GLY VAL ASP GLN VAL PHE LEU VAL ALA HIS ASP TRP
SEQRES 9 B 328 GLY ALA ILE ILE GLY TRP TYR LEU CYS THR PHE HIS PRO
SEQRES 10 B 328 ASP ARG VAL LYS ALA TYR VAL CYS LEU SER VAL PRO LEU
SEQRES 11 B 328 LEU HIS ARG ASP PRO ASN ILE ARG THR VAL ASP ALA MET
SEQRES 12 B 328 ARG ALA MET TYR GLY ASP ASP TYR TYR ILE CYS ARG PHE
SEQRES 13 B 328 GLN LYS PRO GLY GLU MET GLU ALA GLN MET ALA GLU VAL
SEQRES 14 B 328 GLY THR GLU TYR VAL LEU LYS ASN ILE LEU THR THR ARG
SEQRES 15 B 328 LYS PRO GLY PRO PRO ILE PHE PRO LYS GLY GLU TYR GLY
SEQRES 16 B 328 THR GLY PHE ASN PRO ASP MET PRO ASN SER LEU PRO SER
SEQRES 17 B 328 TRP LEU THR GLN ASP ASP LEU ALA TYR TYR VAL SER LYS
SEQRES 18 B 328 TYR GLU LYS THR GLY PHE THR GLY PRO LEU ASN TYR TYR
SEQRES 19 B 328 ARG ASN MET ASN LEU ASN TRP GLU LEU THR ALA PRO TRP
SEQRES 20 B 328 SER GLY GLY LYS ILE GLN VAL PRO VAL LYS PHE ILE THR
SEQRES 21 B 328 GLY GLU LEU ASP GLN VAL TYR THR SER LEU ASN MET LYS
SEQRES 22 B 328 GLU TYR ILE HIS GLY GLY GLY PHE LYS GLN ASP VAL PRO
SEQRES 23 B 328 ASN LEU GLU GLU VAL ILE VAL GLN LYS ASN VAL ALA HIS
SEQRES 24 B 328 PHE ASN ASN GLN GLU ALA ALA GLU GLU ILE ASN ASN HIS
SEQRES 25 B 328 ILE TYR ASP PHE ILE LYS LYS PHE LEU GLN HIS HIS HIS
SEQRES 26 B 328 HIS HIS HIS
FORMUL 2 HOH *257(H2 O)
HELIX 1 AA1 LEU B 36 SER B 39 5 4
HELIX 2 AA2 TRP B 40 SER B 49 1 10
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 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 VAL B 27 O ARG B 53
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 -9.71
CRYST1 70.813 70.813 127.377 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 0.014122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007851 0.00000
TER 2560 PHE B 318
MASTER 298 0 0 17 8 0 0 6 2816 1 0 26
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