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HEADER HYDROLASE 26-APR-16 5JKJ
TITLE CRYSTAL STRUCTURE OF ESTERASE E22 L374D MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE E22;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ESTERASE E32, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,P.WANG,Q.YAO
REVDAT 1 26-APR-17 5JKJ 0
JRNL AUTH Y.ZHANG,Q.YAO,P.WANG
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION AND CATALYSIS OF
JRNL TITL 2 A NOVEL ESTERASE E22 WITH A HOMOSERINE TRANSACETYLASE-LIKE
JRNL TITL 3 FOLD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 94748
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4757
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 35.4036 - 4.8128 0.99 3107 151 0.1562 0.1718
REMARK 3 2 4.8128 - 3.8215 1.00 3061 138 0.1285 0.1539
REMARK 3 3 3.8215 - 3.3388 0.99 3007 163 0.1380 0.1666
REMARK 3 4 3.3388 - 3.0338 0.99 3011 158 0.1546 0.1821
REMARK 3 5 3.0338 - 2.8164 0.99 2985 185 0.1561 0.1965
REMARK 3 6 2.8164 - 2.6504 0.99 2996 171 0.1633 0.1697
REMARK 3 7 2.6504 - 2.5177 0.99 3005 160 0.1655 0.1976
REMARK 3 8 2.5177 - 2.4081 0.99 3008 173 0.1618 0.1873
REMARK 3 9 2.4081 - 2.3155 1.00 2987 155 0.1536 0.1838
REMARK 3 10 2.3155 - 2.2356 0.99 2989 153 0.1565 0.1788
REMARK 3 11 2.2356 - 2.1657 1.00 2993 167 0.1545 0.1796
REMARK 3 12 2.1657 - 2.1038 1.00 2939 189 0.1486 0.1872
REMARK 3 13 2.1038 - 2.0484 1.00 3045 162 0.1539 0.1667
REMARK 3 14 2.0484 - 1.9984 1.00 2986 170 0.1486 0.1872
REMARK 3 15 1.9984 - 1.9530 1.00 3014 128 0.1529 0.1651
REMARK 3 16 1.9530 - 1.9114 1.00 3022 158 0.1546 0.1945
REMARK 3 17 1.9114 - 1.8732 1.00 2981 157 0.1534 0.1836
REMARK 3 18 1.8732 - 1.8379 1.00 3011 136 0.1482 0.1983
REMARK 3 19 1.8379 - 1.8050 1.00 3035 151 0.1548 0.1825
REMARK 3 20 1.8050 - 1.7744 1.00 2988 165 0.1498 0.1716
REMARK 3 21 1.7744 - 1.7458 1.00 3008 163 0.1483 0.1846
REMARK 3 22 1.7458 - 1.7190 1.00 2975 147 0.1579 0.1798
REMARK 3 23 1.7190 - 1.6937 1.00 3019 181 0.1487 0.1965
REMARK 3 24 1.6937 - 1.6698 1.00 2958 153 0.1477 0.1897
REMARK 3 25 1.6698 - 1.6473 1.00 2994 155 0.1569 0.2012
REMARK 3 26 1.6473 - 1.6259 1.00 3000 163 0.1537 0.1816
REMARK 3 27 1.6259 - 1.6055 1.00 3016 162 0.1546 0.2213
REMARK 3 28 1.6055 - 1.5862 1.00 2955 158 0.1582 0.1850
REMARK 3 29 1.5862 - 1.5678 1.00 3052 158 0.1565 0.2068
REMARK 3 30 1.5678 - 1.5501 0.94 2844 127 0.1504 0.1913
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.920
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 : 0.006 5833
REMARK 3 ANGLE : 0.812 7947
REMARK 3 CHIRALITY : 0.055 892
REMARK 3 PLANARITY : 0.005 1029
REMARK 3 DIHEDRAL : 11.261 3441
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 5JKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220786.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 : 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 : 94773
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 35.394
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 3I1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 20% (W/V) PEG
REMARK 280 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 34.44900
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: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 ASP B 394
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 590 O HOH B 645 1.92
REMARK 500 ND2 ASN B 262 O HOH B 401 2.04
REMARK 500 O HOH A 674 O HOH A 756 2.09
REMARK 500 O HOH B 414 O HOH B 708 2.11
REMARK 500 O HOH B 433 O HOH B 682 2.13
REMARK 500 O HOH A 488 O HOH A 671 2.13
REMARK 500 O HOH A 742 O HOH B 799 2.13
REMARK 500 O HOH A 647 O HOH A 695 2.14
REMARK 500 O HOH B 537 O HOH B 774 2.15
REMARK 500 O HOH A 432 O HOH A 788 2.15
REMARK 500 O HOH B 416 O HOH B 557 2.15
REMARK 500 O HOH A 409 O HOH A 735 2.15
REMARK 500 O HOH A 832 O HOH A 858 2.16
REMARK 500 O HOH B 622 O HOH B 650 2.17
REMARK 500 O HOH B 523 O HOH B 658 2.17
REMARK 500 O HOH A 577 O HOH A 815 2.18
REMARK 500 O HOH A 463 O HOH A 580 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 SER A 175 -120.69 64.36
REMARK 500 ILE A 199 54.57 35.60
REMARK 500 LEU A 252 -153.70 -121.01
REMARK 500 GLN A 318 -159.84 -93.69
REMARK 500 LEU A 342 -62.12 -104.14
REMARK 500 SER B 175 -120.70 62.62
REMARK 500 ILE B 199 57.82 33.45
REMARK 500 LEU B 252 -152.35 -120.64
REMARK 500 GLN B 318 -157.05 -104.86
REMARK 500 LEU B 342 -64.15 -102.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JKF RELATED DB: PDB
DBREF 5JKJ A 25 394 PDB 5JKJ 5JKJ 25 394
DBREF 5JKJ B 25 394 PDB 5JKJ 5JKJ 25 394
SEQRES 1 A 370 MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR
SEQRES 2 A 370 THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY
SEQRES 3 A 370 TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN
SEQRES 4 A 370 VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS
SEQRES 5 A 370 ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY
SEQRES 6 A 370 TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP
SEQRES 7 A 370 THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA
SEQRES 8 A 370 ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY
SEQRES 9 A 370 PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY
SEQRES 10 A 370 LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN
SEQRES 11 A 370 VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS
SEQRES 12 A 370 LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN
SEQRES 13 A 370 ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU
SEQRES 14 A 370 ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA
SEQRES 15 A 370 TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE
SEQRES 16 A 370 THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS
SEQRES 17 A 370 GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET
SEQRES 18 A 370 LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN
SEQRES 19 A 370 GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER
SEQRES 20 A 370 ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL
SEQRES 21 A 370 ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER
SEQRES 22 A 370 MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS
SEQRES 23 A 370 GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN
SEQRES 24 A 370 GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO
SEQRES 25 A 370 ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN
SEQRES 26 A 370 SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER
SEQRES 27 A 370 THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS ASP GLU
SEQRES 28 A 370 GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG
SEQRES 29 A 370 GLN PHE LEU GLU ASN ASP
SEQRES 1 B 370 MET VAL GLU LYS ARG VAL PHE GLU MET PRO HIS PHE THR
SEQRES 2 B 370 THR PHE GLY GLY LYS GLN ILE LYS ASN VAL LYS VAL GLY
SEQRES 3 B 370 TRP GLU ALA TYR GLY THR LEU ASN ASP ALA LYS SER ASN
SEQRES 4 B 370 VAL ILE LEU ILE THR HIS TYR PHE SER GLY SER SER HIS
SEQRES 5 B 370 ALA ALA GLY LYS TYR ASP GLU ASN ASP PRO ALA PRO GLY
SEQRES 6 B 370 TYR TRP ASP SER ILE ILE GLY PRO GLY LYS ALA ILE ASP
SEQRES 7 B 370 THR ASP ARG PHE TYR VAL ILE SER VAL ASP THR LEU ALA
SEQRES 8 B 370 ASN LEU ASN ALA TYR ASP PRO HIS VAL ILE THR THR GLY
SEQRES 9 B 370 PRO THR SER ILE ASN PRO ASP THR GLY LYS PRO TYR GLY
SEQRES 10 B 370 LEU ASP PHE PRO VAL VAL THR ILE ARG ASP PHE VAL ASN
SEQRES 11 B 370 VAL GLN LYS ALA LEU LEU GLU SER LEU GLY ILE SER LYS
SEQRES 12 B 370 LEU TYR ALA VAL ILE GLY PRO SER MET GLY SER MET GLN
SEQRES 13 B 370 ALA ILE ASP TRP ALA SER ALA TYR PRO GLY TRP VAL GLU
SEQRES 14 B 370 ARG MET ILE SER VAL ILE GLY ALA GLY GLN SER ASP ALA
SEQRES 15 B 370 TRP THR THR ALA ALA LEU GLU HIS TRP ALA THR PRO ILE
SEQRES 16 B 370 THR LEU ASP LYS ASN TRP ASN ASN GLY ALA TYR SER LYS
SEQRES 17 B 370 GLU GLN ALA PRO LEU ASN GLY LEU ALA ALA SER LEU MET
SEQRES 18 B 370 LEU ILE THR GLN ASN ALA LEU THR PRO SER PHE PHE ASN
SEQRES 19 B 370 GLN THR GLY ASN THR LEU GLY TYR LYS ASN VAL GLU SER
SEQRES 20 B 370 ALA PRO LEU ASN ASP ILE ARG GLN SER HIS SER ILE VAL
SEQRES 21 B 370 ASN TRP LEU ARG GLU ARG ALA LYS THR ARG ALA LYS SER
SEQRES 22 B 370 MET ASP ALA ASN HIS LEU LEU TYR LEU VAL ARG ALA CYS
SEQRES 23 B 370 GLN LEU PHE VAL ALA GLY HIS GLN GLY ASN LEU GLU GLN
SEQRES 24 B 370 GLY LEU ALA SER ILE LYS ALA LYS THR LEU PHE ILE PRO
SEQRES 25 B 370 ALA GLN THR ASP LEU LEU LEU MET PRO TYR LEU SER GLN
SEQRES 26 B 370 SER ALA HIS GLN GLY LEU THR SER MET ASN ASN ASP SER
SEQRES 27 B 370 THR LEU VAL THR LEU ASN GLY LYS LEU GLY HIS ASP GLU
SEQRES 28 B 370 GLY VAL THR ASN VAL SER ALA GLN ALA GLN ALA ILE ARG
SEQRES 29 B 370 GLN PHE LEU GLU ASN ASP
FORMUL 3 HOH *869(H2 O)
HELIX 1 AA1 TYR A 140 PHE A 144 5 5
HELIX 2 AA2 THR A 148 LEU A 163 1 16
HELIX 3 AA3 SER A 175 TYR A 188 1 14
HELIX 4 AA4 PRO A 189 VAL A 192 5 4
HELIX 5 AA5 ASP A 205 ASP A 222 1 18
HELIX 6 AA6 LYS A 223 ALA A 229 5 7
HELIX 7 AA7 SER A 231 ALA A 235 5 5
HELIX 8 AA8 PRO A 236 ALA A 251 1 16
HELIX 9 AA9 THR A 253 GLY A 265 1 13
HELIX 10 AB1 GLU A 270 ASP A 276 1 7
HELIX 11 AB2 HIS A 281 LYS A 296 1 16
HELIX 12 AB3 ASP A 299 LEU A 312 1 14
HELIX 13 AB4 VAL A 314 GLN A 318 5 5
HELIX 14 AB5 ASN A 320 SER A 327 1 8
HELIX 15 AB6 MET A 344 MET A 358 1 15
HELIX 16 AB7 LEU A 371 HIS A 373 5 3
HELIX 17 AB8 ASP A 374 ASN A 379 1 6
HELIX 18 AB9 VAL A 380 ALA A 382 5 3
HELIX 19 AC1 GLN A 383 GLU A 392 1 10
HELIX 20 AC2 TYR B 140 PHE B 144 5 5
HELIX 21 AC3 THR B 148 LEU B 163 1 16
HELIX 22 AC4 SER B 175 TYR B 188 1 14
HELIX 23 AC5 ASP B 205 ASP B 222 1 18
HELIX 24 AC6 TRP B 225 ALA B 229 5 5
HELIX 25 AC7 SER B 231 ALA B 235 5 5
HELIX 26 AC8 PRO B 236 ALA B 251 1 16
HELIX 27 AC9 THR B 253 GLY B 265 1 13
HELIX 28 AD1 GLU B 270 ASP B 276 1 7
HELIX 29 AD2 HIS B 281 ALA B 295 1 15
HELIX 30 AD3 ASP B 299 LEU B 312 1 14
HELIX 31 AD4 ASN B 320 SER B 327 1 8
HELIX 32 AD5 MET B 344 MET B 358 1 15
HELIX 33 AD6 LEU B 371 HIS B 373 5 3
HELIX 34 AD7 ASP B 374 ASN B 379 1 6
HELIX 35 AD8 VAL B 380 ALA B 382 5 3
HELIX 36 AD9 GLN B 383 GLU B 392 1 10
SHEET 1 AA1 8 ARG A 29 THR A 37 0
SHEET 2 AA1 8 GLN A 43 TYR A 54 -1 O TRP A 51 N ARG A 29
SHEET 3 AA1 8 TYR A 107 VAL A 111 -1 O VAL A 108 N TYR A 54
SHEET 4 AA1 8 VAL A 64 ILE A 67 1 N ILE A 67 O ILE A 109
SHEET 5 AA1 8 ALA A 170 PRO A 174 1 O ILE A 172 N LEU A 66
SHEET 6 AA1 8 ARG A 194 VAL A 198 1 O ILE A 196 N VAL A 171
SHEET 7 AA1 8 LYS A 331 ILE A 335 1 O LEU A 333 N SER A 197
SHEET 8 AA1 8 SER A 362 LEU A 364 1 O THR A 363 N PHE A 334
SHEET 1 AA2 2 ILE A 95 GLY A 96 0
SHEET 2 AA2 2 ILE A 101 ASP A 102 1 O ILE A 101 N GLY A 96
SHEET 1 AA3 8 ARG B 29 THR B 37 0
SHEET 2 AA3 8 GLN B 43 TYR B 54 -1 O TRP B 51 N ARG B 29
SHEET 3 AA3 8 TYR B 107 VAL B 111 -1 O VAL B 108 N TYR B 54
SHEET 4 AA3 8 VAL B 64 ILE B 67 1 N ILE B 67 O ILE B 109
SHEET 5 AA3 8 ALA B 170 PRO B 174 1 O ILE B 172 N LEU B 66
SHEET 6 AA3 8 ARG B 194 VAL B 198 1 O ILE B 196 N VAL B 171
SHEET 7 AA3 8 LYS B 331 ILE B 335 1 O LEU B 333 N SER B 197
SHEET 8 AA3 8 SER B 362 LEU B 364 1 O THR B 363 N PHE B 334
SHEET 1 AA4 2 ILE B 95 GLY B 96 0
SHEET 2 AA4 2 ILE B 101 ASP B 102 1 O ILE B 101 N GLY B 96
CRYST1 58.619 68.898 82.524 90.00 91.11 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 0.017059 0.000000 0.000329 0.00000
SCALE2 0.000000 0.014514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012120 0.00000
TER 2858 ASP A 394
TER 5700 ASN B 393
MASTER 277 0 0 36 20 0 0 6 6559 2 0 58
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