| content |
HEADER HYDROLASE 09-DEC-18 6IX4
TITLE STRUCTURE OF AN EPOXIDE HYDROLASE FROM ASPERGILLUS USAMII E001 (AUEH2)
TITLE 2 AT 1.51 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROSOMAL EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS USAMII;
SOURCE 3 ORGANISM_TAXID: 186680;
SOURCE 4 GENE: EH2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA AND BETA PROTEINS, ALPHA/BETA-HYDROLASES, STYRENE OXIDE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HU,B.C.HU,X.D.HOU,L.WU,Y.J.RAO,M.C.WU
REVDAT 1 11-DEC-19 6IX4 0
JRNL AUTH D.HU,B.C.HU,X.D.HOU,Y.J.RAO,M.C.WU
JRNL TITL STRUCTURE OF AN EPOXIDE HYDROLASE FROM ASPERGILLUS USAMII
JRNL TITL 2 E001 (AUEH2) AT 1.51 ANGSTROMS RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 122834
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 6064
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 43.8850 - 4.6918 1.00 4046 232 0.1606 0.1872
REMARK 3 2 4.6918 - 3.7246 1.00 3970 200 0.1299 0.1355
REMARK 3 3 3.7246 - 3.2540 0.99 3922 214 0.1364 0.1453
REMARK 3 4 3.2540 - 2.9565 1.00 3939 217 0.1461 0.1458
REMARK 3 5 2.9565 - 2.7447 1.00 3881 234 0.1460 0.1537
REMARK 3 6 2.7447 - 2.5829 1.00 3921 215 0.1486 0.1612
REMARK 3 7 2.5829 - 2.4535 1.00 3957 190 0.1508 0.1951
REMARK 3 8 2.4535 - 2.3467 0.99 3854 212 0.1474 0.1713
REMARK 3 9 2.3467 - 2.2564 1.00 3859 229 0.1446 0.1710
REMARK 3 10 2.2564 - 2.1785 1.00 3908 225 0.1441 0.1730
REMARK 3 11 2.1785 - 2.1104 1.00 3879 236 0.1415 0.1709
REMARK 3 12 2.1104 - 2.0501 1.00 3884 194 0.1429 0.1488
REMARK 3 13 2.0501 - 1.9961 1.00 3891 188 0.1442 0.1694
REMARK 3 14 1.9961 - 1.9474 1.00 3965 214 0.1405 0.1617
REMARK 3 15 1.9474 - 1.9031 1.00 3886 192 0.1360 0.1785
REMARK 3 16 1.9031 - 1.8626 0.99 3807 219 0.1395 0.1715
REMARK 3 17 1.8626 - 1.8254 0.99 3894 196 0.1451 0.1644
REMARK 3 18 1.8254 - 1.7909 1.00 3877 166 0.1473 0.1841
REMARK 3 19 1.7909 - 1.7590 1.00 3902 213 0.1435 0.1667
REMARK 3 20 1.7590 - 1.7291 1.00 3881 182 0.1463 0.1827
REMARK 3 21 1.7291 - 1.7012 1.00 3953 176 0.1463 0.1905
REMARK 3 22 1.7012 - 1.6751 1.00 3849 199 0.1523 0.1874
REMARK 3 23 1.6751 - 1.6504 1.00 3868 210 0.1421 0.1869
REMARK 3 24 1.6504 - 1.6272 1.00 3915 167 0.1387 0.1697
REMARK 3 25 1.6272 - 1.6052 1.00 3913 185 0.1350 0.1711
REMARK 3 26 1.6052 - 1.5843 0.99 3816 206 0.1466 0.1720
REMARK 3 27 1.5843 - 1.5645 0.98 3866 168 0.1496 0.1874
REMARK 3 28 1.5645 - 1.5457 0.99 3801 201 0.1480 0.1849
REMARK 3 29 1.5457 - 1.5277 0.99 3865 204 0.1477 0.1897
REMARK 3 30 1.5277 - 1.5106 0.97 3801 180 0.1496 0.1606
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) : 15.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.45
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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: SF FILE CONTAINS FRIEDEL PAIRS UNDER
REMARK 3 I/F_MINUS AND I/F_PLUS COLUMNS.
REMARK 4
REMARK 4 6IX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1300010094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 122867
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
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 : 6.700
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.27100
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: AMPLE
REMARK 200 STARTING MODEL: 1QO7
REMARK 200
REMARK 200 REMARK: TETRAGONAL CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 6.5, 25%(W/V)
REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.96100
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ALA A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ILE A 223
REMARK 465 PRO A 224
REMARK 465 ASP A 225
REMARK 465 THR A 226
REMARK 465 ALA A 227
REMARK 465 ARG A 394
REMARK 465 LYS A 395
REMARK 465 ARG B 394
REMARK 465 LYS B 395
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 804 O HOH B 645 2.19
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 A 117 45.32 -96.65
REMARK 500 SER A 119 -179.38 -179.87
REMARK 500 THR A 152 -115.06 42.93
REMARK 500 ASP A 191 -137.58 50.19
REMARK 500 PRO B 117 42.48 -97.46
REMARK 500 SER B 119 -179.90 -179.53
REMARK 500 THR B 152 -115.28 46.51
REMARK 500 ASP B 191 -136.66 48.98
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 B1001 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B1002 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B1003 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B1004 DISTANCE = 7.55 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 112 O
REMARK 620 2 PRO B 146 O 117.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 404
DBREF 6IX4 A 1 395 UNP T2B4K5 T2B4K5_9EURO 1 395
DBREF 6IX4 B 1 395 UNP T2B4K5 T2B4K5_9EURO 1 395
SEQADV 6IX4 ALA A -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX4 PHE A 0 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX4 ALA B -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX4 PHE B 0 UNP T2B4K5 EXPRESSION TAG
SEQRES 1 A 397 ALA PHE MET ALA LEU ALA TYR SER ASN ILE PRO LEU GLY
SEQRES 2 A 397 ALA THR VAL ILE PRO SER PRO PHE GLN VAL HIS ILE SER
SEQRES 3 A 397 ASP GLU GLN ILE GLU GLU LEU GLN LEU LEU VAL LYS LEU
SEQRES 4 A 397 SER LYS LEU ALA PRO PRO THR TYR GLU GLY LEU GLN GLN
SEQRES 5 A 397 ASP ARG ARG TYR GLY ILE THR ASN GLU TRP LEU ALA ASN
SEQRES 6 A 397 ALA LYS GLU ALA TRP LYS SER PHE ASP TRP ARG PRO ALA
SEQRES 7 A 397 GLU SER ARG ILE ASN SER PHE PRO GLN PHE THR TYR ASP
SEQRES 8 A 397 ILE GLU GLY LEU THR ILE HIS PHE VAL ALA LEU PHE SER
SEQRES 9 A 397 GLU LYS LYS ASP ALA ILE PRO ILE VAL LEU LEU HIS GLY
SEQRES 10 A 397 TRP PRO GLY SER PHE LEU GLU PHE LEU PRO VAL LEU THR
SEQRES 11 A 397 SER ILE ARG ASP LYS TYR SER PRO GLU THR LEU PRO TYR
SEQRES 12 A 397 HIS ILE VAL VAL PRO SER LEU PRO GLY TYR THR PHE SER
SEQRES 13 A 397 SER GLY PRO PRO LEU ASP VAL ASN PHE ASN GLY GLU ASP
SEQRES 14 A 397 THR ALA ARG VAL ILE ASN LYS VAL MET LEU ASN LEU GLY
SEQRES 15 A 397 PHE GLU ASP GLY TYR VAL ALA GLN GLY GLY ASP ILE GLY
SEQRES 16 A 397 SER LYS ILE GLY ARG ILE LEU ALA VAL ASP HIS ASP ALA
SEQRES 17 A 397 CYS LYS ALA VAL HIS LEU ASN ALA CYS TYR MET GLY LYS
SEQRES 18 A 397 PRO SER SER ILE PRO ASP THR ALA ILE THR GLU GLU ASP
SEQRES 19 A 397 LYS ARG ALA LEU ALA ARG ALA GLN TRP PHE ALA THR PHE
SEQRES 20 A 397 GLY SER GLY TYR ALA VAL GLU HIS GLY THR ARG PRO SER
SEQRES 21 A 397 THR ILE GLY ASN ALA LEU SER THR SER PRO VAL ALA LEU
SEQRES 22 A 397 LEU SER TRP ILE GLY GLU LYS PHE LEU ASP TRP ALA GLY
SEQRES 23 A 397 GLU THR ILE PRO LEU GLU THR ILE LEU GLU SER VAL THR
SEQRES 24 A 397 LEU TYR TRP PHE THR GLU THR PHE PRO ARG SER ILE TYR
SEQRES 25 A 397 HIS TYR ARG GLU ASN PHE PRO PRO PRO LYS LEU ARG HIS
SEQRES 26 A 397 THR GLU ASP PRO ARG TRP TYR ILE ARG LYS PRO PHE GLY
SEQRES 27 A 397 PHE SER TYR TYR PRO MET GLU LEU VAL PRO THR PRO ARG
SEQRES 28 A 397 ALA TRP VAL GLU THR THR GLY ASN LEU VAL PHE TRP GLN
SEQRES 29 A 397 ALA HIS GLU LYS GLY GLY HIS PHE ALA ALA LEU GLU ARG
SEQRES 30 A 397 PRO GLN ASP TYR LEU ASP ASP LEU THR ALA PHE CYS GLU
SEQRES 31 A 397 GLN VAL TRP ALA GLY ARG LYS
SEQRES 1 B 397 ALA PHE MET ALA LEU ALA TYR SER ASN ILE PRO LEU GLY
SEQRES 2 B 397 ALA THR VAL ILE PRO SER PRO PHE GLN VAL HIS ILE SER
SEQRES 3 B 397 ASP GLU GLN ILE GLU GLU LEU GLN LEU LEU VAL LYS LEU
SEQRES 4 B 397 SER LYS LEU ALA PRO PRO THR TYR GLU GLY LEU GLN GLN
SEQRES 5 B 397 ASP ARG ARG TYR GLY ILE THR ASN GLU TRP LEU ALA ASN
SEQRES 6 B 397 ALA LYS GLU ALA TRP LYS SER PHE ASP TRP ARG PRO ALA
SEQRES 7 B 397 GLU SER ARG ILE ASN SER PHE PRO GLN PHE THR TYR ASP
SEQRES 8 B 397 ILE GLU GLY LEU THR ILE HIS PHE VAL ALA LEU PHE SER
SEQRES 9 B 397 GLU LYS LYS ASP ALA ILE PRO ILE VAL LEU LEU HIS GLY
SEQRES 10 B 397 TRP PRO GLY SER PHE LEU GLU PHE LEU PRO VAL LEU THR
SEQRES 11 B 397 SER ILE ARG ASP LYS TYR SER PRO GLU THR LEU PRO TYR
SEQRES 12 B 397 HIS ILE VAL VAL PRO SER LEU PRO GLY TYR THR PHE SER
SEQRES 13 B 397 SER GLY PRO PRO LEU ASP VAL ASN PHE ASN GLY GLU ASP
SEQRES 14 B 397 THR ALA ARG VAL ILE ASN LYS VAL MET LEU ASN LEU GLY
SEQRES 15 B 397 PHE GLU ASP GLY TYR VAL ALA GLN GLY GLY ASP ILE GLY
SEQRES 16 B 397 SER LYS ILE GLY ARG ILE LEU ALA VAL ASP HIS ASP ALA
SEQRES 17 B 397 CYS LYS ALA VAL HIS LEU ASN ALA CYS TYR MET GLY LYS
SEQRES 18 B 397 PRO SER SER ILE PRO ASP THR ALA ILE THR GLU GLU ASP
SEQRES 19 B 397 LYS ARG ALA LEU ALA ARG ALA GLN TRP PHE ALA THR PHE
SEQRES 20 B 397 GLY SER GLY TYR ALA VAL GLU HIS GLY THR ARG PRO SER
SEQRES 21 B 397 THR ILE GLY ASN ALA LEU SER THR SER PRO VAL ALA LEU
SEQRES 22 B 397 LEU SER TRP ILE GLY GLU LYS PHE LEU ASP TRP ALA GLY
SEQRES 23 B 397 GLU THR ILE PRO LEU GLU THR ILE LEU GLU SER VAL THR
SEQRES 24 B 397 LEU TYR TRP PHE THR GLU THR PHE PRO ARG SER ILE TYR
SEQRES 25 B 397 HIS TYR ARG GLU ASN PHE PRO PRO PRO LYS LEU ARG HIS
SEQRES 26 B 397 THR GLU ASP PRO ARG TRP TYR ILE ARG LYS PRO PHE GLY
SEQRES 27 B 397 PHE SER TYR TYR PRO MET GLU LEU VAL PRO THR PRO ARG
SEQRES 28 B 397 ALA TRP VAL GLU THR THR GLY ASN LEU VAL PHE TRP GLN
SEQRES 29 B 397 ALA HIS GLU LYS GLY GLY HIS PHE ALA ALA LEU GLU ARG
SEQRES 30 B 397 PRO GLN ASP TYR LEU ASP ASP LEU THR ALA PHE CYS GLU
SEQRES 31 B 397 GLN VAL TRP ALA GLY ARG LYS
HET ACT A 401 4
HET GOL B 401 6
HET SO4 B 402 5
HET CL B 403 1
HET NA B 404 1
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 GOL C3 H8 O3
FORMUL 5 SO4 O4 S 2-
FORMUL 6 CL CL 1-
FORMUL 7 NA NA 1+
FORMUL 8 HOH *960(H2 O)
HELIX 1 AA1 SER A 24 SER A 38 1 15
HELIX 2 AA2 TYR A 45 GLN A 49 5 5
HELIX 3 AA3 THR A 57 SER A 70 1 14
HELIX 4 AA4 ASP A 72 ASN A 81 1 10
HELIX 5 AA5 SER A 119 GLU A 122 5 4
HELIX 6 AA6 PHE A 123 TYR A 134 1 12
HELIX 7 AA7 ASN A 164 LEU A 179 1 16
HELIX 8 AA8 ASP A 191 HIS A 204 1 14
HELIX 9 AA9 THR A 229 GLY A 246 1 18
HELIX 10 AB1 SER A 247 ARG A 256 1 10
HELIX 11 AB2 ARG A 256 THR A 266 1 11
HELIX 12 AB3 SER A 267 ALA A 283 1 17
HELIX 13 AB4 PRO A 288 THR A 302 1 15
HELIX 14 AB5 GLU A 303 SER A 308 1 6
HELIX 15 AB6 ILE A 309 PHE A 316 5 8
HELIX 16 AB7 ARG A 322 TYR A 330 5 9
HELIX 17 AB8 PRO A 348 GLU A 353 1 6
HELIX 18 AB9 PHE A 370 ARG A 375 1 6
HELIX 19 AC1 ARG A 375 TRP A 391 1 17
HELIX 20 AC2 SER B 24 SER B 38 1 15
HELIX 21 AC3 TYR B 45 GLN B 49 5 5
HELIX 22 AC4 THR B 57 PHE B 71 1 15
HELIX 23 AC5 ASP B 72 SER B 82 1 11
HELIX 24 AC6 SER B 119 GLU B 122 5 4
HELIX 25 AC7 PHE B 123 TYR B 134 1 12
HELIX 26 AC8 ASN B 164 LEU B 179 1 16
HELIX 27 AC9 ASP B 191 HIS B 204 1 14
HELIX 28 AD1 THR B 229 GLY B 246 1 18
HELIX 29 AD2 SER B 247 ARG B 256 1 10
HELIX 30 AD3 ARG B 256 SER B 265 1 10
HELIX 31 AD4 SER B 267 ALA B 283 1 17
HELIX 32 AD5 PRO B 288 THR B 302 1 15
HELIX 33 AD6 THR B 304 SER B 308 5 5
HELIX 34 AD7 ILE B 309 PHE B 316 5 8
HELIX 35 AD8 ARG B 322 TYR B 330 5 9
HELIX 36 AD9 PRO B 348 THR B 354 1 7
HELIX 37 AE1 PHE B 370 ARG B 375 1 6
HELIX 38 AE2 ARG B 375 TRP B 391 1 17
SHEET 1 AA1 9 SER A 17 PRO A 18 0
SHEET 2 AA1 9 GLN A 85 ILE A 90 -1 O THR A 87 N SER A 17
SHEET 3 AA1 9 LEU A 93 LEU A 100 -1 O ILE A 95 N TYR A 88
SHEET 4 AA1 9 TYR A 141 PRO A 146 -1 O VAL A 145 N VAL A 98
SHEET 5 AA1 9 ILE A 108 LEU A 113 1 N ILE A 110 O HIS A 142
SHEET 6 AA1 9 TYR A 185 GLY A 189 1 O GLN A 188 N LEU A 113
SHEET 7 AA1 9 CYS A 207 LEU A 212 1 O LYS A 208 N TYR A 185
SHEET 8 AA1 9 ILE A 331 TYR A 339 1 O GLY A 336 N LEU A 212
SHEET 9 AA1 9 GLY A 356 ALA A 363 1 O ASN A 357 N ILE A 331
SHEET 1 AA2 9 SER B 17 PRO B 18 0
SHEET 2 AA2 9 GLN B 85 ILE B 90 -1 O THR B 87 N SER B 17
SHEET 3 AA2 9 LEU B 93 LEU B 100 -1 O ILE B 95 N TYR B 88
SHEET 4 AA2 9 TYR B 141 PRO B 146 -1 O VAL B 145 N VAL B 98
SHEET 5 AA2 9 ILE B 108 LEU B 113 1 N ILE B 110 O VAL B 144
SHEET 6 AA2 9 TYR B 185 GLY B 189 1 O VAL B 186 N VAL B 111
SHEET 7 AA2 9 CYS B 207 LEU B 212 1 O LYS B 208 N TYR B 185
SHEET 8 AA2 9 ILE B 331 TYR B 339 1 O GLY B 336 N LEU B 212
SHEET 9 AA2 9 GLY B 356 ALA B 363 1 O ASN B 357 N ILE B 331
LINK O LEU B 112 NA NA B 404 1555 1555 2.71
LINK O PRO B 146 NA NA B 404 1555 1555 2.72
CISPEP 1 TRP A 116 PRO A 117 0 4.15
CISPEP 2 GLY A 156 PRO A 157 0 -5.69
CISPEP 3 PHE A 316 PRO A 317 0 -2.14
CISPEP 4 TRP B 116 PRO B 117 0 4.79
CISPEP 5 GLY B 156 PRO B 157 0 -2.26
CISPEP 6 PHE B 316 PRO B 317 0 -3.95
SITE 1 AC1 4 ARG A 375 PRO A 376 GLN A 377 ASP A 378
SITE 1 AC2 6 ASP B 183 LYS B 208 TRP B 391 ALA B 392
SITE 2 AC2 6 GLY B 393 HOH B 523
SITE 1 AC3 4 ARG B 375 PRO B 376 GLN B 377 ASP B 378
SITE 1 AC4 6 GLN B 188 GLY B 190 ASN B 213 TYR B 379
SITE 2 AC4 6 HOH B 597 HOH B 790
SITE 1 AC5 4 LEU B 112 LEU B 113 HIS B 114 PRO B 146
CRYST1 57.365 51.922 133.488 90.00 90.97 90.00 P 1 21 1 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 0.017432 0.000000 0.000295 0.00000
SCALE2 0.000000 0.019260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007492 0.00000
TER 3149 GLY A 393
TER 6352 GLY B 393
MASTER 318 0 5 38 18 0 7 6 7233 2 18 62
END |