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HEADER HYDROLASE 15-APR-16 5JD6
TITLE CRYSTAL STRUCTURE OF MGS-MCHE2, AN ALPHA/BETA HYDROLASE ENZYME FROM
TITLE 2 THE METAGENOME OF SEDIMENTS FROM THE LAGOON OF MAR CHICA, MOROCCO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGS-MCHE2;
COMPND 3 CHAIN: A;
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;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, METAGENOME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,B.NOCEK,V.YIM,H.CUI,M.MARTINEZ-MARTINEZ,
AUTHOR 2 P.N.GOLYSHIN,M.M.YAKIMA,M.FERRER,A.SAVCHENKO
REVDAT 1 04-MAY-16 5JD6 0
JRNL AUTH M.MARTINEZ-MARTINEZ
JRNL TITL CRYSTAL STRUCTURE OF MGS-MCHE2, AN ALPHA/BETA HYDROLASE
JRNL TITL 2 ENZYME FROM THE METAGENOME OF SEDIMENTS FROM THE LAGOON OF
JRNL TITL 3 MAR CHICA, MOROCCO
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.5
REMARK 3 NUMBER OF REFLECTIONS : 9315
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 516
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 25.8498 - 4.4687 0.92 2892 167 0.1988 0.2201
REMARK 3 2 4.4687 - 3.5499 0.97 3043 159 0.1802 0.2226
REMARK 3 3 3.5499 - 3.1020 0.97 3020 159 0.2262 0.2273
REMARK 3 4 3.1020 - 2.8188 0.94 2943 163 0.2342 0.3008
REMARK 3 5 2.8188 - 2.6169 0.69 2173 109 0.2490 0.3266
REMARK 3 6 2.6169 - 2.4628 0.51 1607 82 0.2702 0.3399
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100
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 : 0.004 1784
REMARK 3 ANGLE : 0.959 2410
REMARK 3 CHIRALITY : 0.073 267
REMARK 3 PLANARITY : 0.003 304
REMARK 3 DIHEDRAL : 15.091 663
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:29)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6862 -24.1802 -2.7114
REMARK 3 T TENSOR
REMARK 3 T11: 0.1897 T22: 0.1580
REMARK 3 T33: 0.3176 T12: 0.1346
REMARK 3 T13: 0.0490 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 4.5600 L22: 3.4217
REMARK 3 L33: 5.5126 L12: 0.0054
REMARK 3 L13: 1.8814 L23: -2.5868
REMARK 3 S TENSOR
REMARK 3 S11: 0.2175 S12: -0.4442 S13: -0.3268
REMARK 3 S21: -0.2632 S22: -0.0094 S23: 0.4483
REMARK 3 S31: 0.0405 S32: -0.1754 S33: -0.0152
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 30:53)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.4083 -22.8925 -8.1313
REMARK 3 T TENSOR
REMARK 3 T11: 0.2728 T22: 0.1247
REMARK 3 T33: 0.3188 T12: 0.0899
REMARK 3 T13: 0.0586 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 7.1399 L22: 6.2394
REMARK 3 L33: 8.2764 L12: -0.5724
REMARK 3 L13: 4.7084 L23: -2.2807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: -0.2935 S13: -0.1514
REMARK 3 S21: -0.1214 S22: 0.2142 S23: 0.3509
REMARK 3 S31: 0.7765 S32: -0.5979 S33: -0.1026
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 54:100)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2377 -13.6633 -0.3309
REMARK 3 T TENSOR
REMARK 3 T11: 0.2845 T22: 0.0898
REMARK 3 T33: 0.2288 T12: 0.0419
REMARK 3 T13: 0.0152 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 5.7360 L22: 6.8884
REMARK 3 L33: 4.2048 L12: -2.0523
REMARK 3 L13: 1.5761 L23: -0.0336
REMARK 3 S TENSOR
REMARK 3 S11: -0.2723 S12: -0.2286 S13: 0.3422
REMARK 3 S21: 0.3723 S22: 0.0989 S23: -0.5348
REMARK 3 S31: -0.4475 S32: 0.2247 S33: 0.0383
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 101:182)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0268 -8.2156 4.8202
REMARK 3 T TENSOR
REMARK 3 T11: 0.5687 T22: 0.2116
REMARK 3 T33: 0.3155 T12: 0.0628
REMARK 3 T13: 0.0317 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.7040 L22: 4.1630
REMARK 3 L33: 4.0968 L12: -1.0978
REMARK 3 L13: 1.3163 L23: 1.5096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.5285 S13: 0.2043
REMARK 3 S21: 0.7390 S22: 0.1066 S23: 0.1575
REMARK 3 S31: -0.4242 S32: -0.3162 S33: -0.0341
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 183:254)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7786 -6.3830 -12.7544
REMARK 3 T TENSOR
REMARK 3 T11: 0.5911 T22: 0.2822
REMARK 3 T33: 0.2434 T12: 0.2151
REMARK 3 T13: -0.0514 T23: 0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 4.3723 L22: 6.6223
REMARK 3 L33: 3.4014 L12: -1.5451
REMARK 3 L13: 1.5252 L23: 0.3194
REMARK 3 S TENSOR
REMARK 3 S11: -0.2944 S12: -0.0685 S13: 0.3182
REMARK 3 S21: -0.3458 S22: 0.0630 S23: 0.2088
REMARK 3 S31: -1.1488 S32: -0.5561 S33: 0.0682
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 5JD6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10194
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 25.848
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.57800
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: PHENIX
REMARK 200 STARTING MODEL: 1CR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULPHATE, 5% ISOPROPANOL.
REMARK 280 CRYOPROTECTANT: PARATONE-N OIL., PH 7, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.25600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.12800
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.12800
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.25600
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: A
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 A 1
REMARK 465 LYS A 2
REMARK 465 TYR A 120
REMARK 465 GLU A 121
REMARK 465 ASN A 122
REMARK 465 ALA A 123
REMARK 465 MET A 124
REMARK 465 GLY A 125
REMARK 465 GLU A 126
REMARK 465 SER A 127
REMARK 465 TYR A 128
REMARK 465 PRO A 129
REMARK 465 ARG A 130
REMARK 465 ARG A 131
REMARK 465 GLY A 132
REMARK 465 ASP A 133
REMARK 465 TYR A 134
REMARK 465 GLU A 135
REMARK 465 PHE A 136
REMARK 465 ILE A 137
REMARK 465 LYS A 138
REMARK 465 LYS A 139
REMARK 465 LYS A 140
REMARK 465 ALA A 141
REMARK 465 GLU A 142
REMARK 465 ALA A 143
REMARK 465 VAL A 144
REMARK 465 PHE A 145
REMARK 465 TYR A 146
REMARK 465 ASP A 147
REMARK 465 PRO A 148
REMARK 465 GLU A 149
REMARK 465 VAL A 150
REMARK 465 ALA A 151
REMARK 465 THR A 152
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 A 18 -35.45 -134.30
REMARK 500 SER A 60 177.61 68.19
REMARK 500 LEU A 62 57.96 -150.67
REMARK 500 SER A 91 -123.03 54.60
REMARK 500 ARG A 166 -58.92 77.07
REMARK 500 HIS A 182 58.84 -93.10
REMARK 500 PRO A 207 153.82 -49.41
REMARK 500 ASP A 253 73.83 57.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JD3 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD4 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD5 RELATED DB: PDB
DBREF 5JD6 A 1 254 PDB 5JD6 5JD6 1 254
SEQRES 1 A 254 MET LYS ASP HIS LEU LYS GLN GLU GLY LYS PHE THR TYR
SEQRES 2 A 254 LEU GLU LYS GLY GLU GLY THR PRO ILE VAL ILE LEU HIS
SEQRES 3 A 254 GLY LEU MET GLY GLY LEU SER ASN PHE ASP GLY VAL ILE
SEQRES 4 A 254 ASP TYR PHE PRO GLU LYS GLY TYR LYS VAL LEU ILE PRO
SEQRES 5 A 254 GLU LEU PRO LEU TYR SER MET SER LEU LEU LYS THR SER
SEQRES 6 A 254 VAL GLY THR PHE ALA ARG TYR LEU LYS GLU PHE VAL ASP
SEQRES 7 A 254 PHE LYS GLY TYR GLU ASN VAL ILE LEU LEU GLY ASN SER
SEQRES 8 A 254 LEU GLY GLY HIS ILE ALA LEU LEU ALA THR LYS MET PHE
SEQRES 9 A 254 PRO GLU ILE VAL GLN ALA LEU VAL ILE THR GLY SER SER
SEQRES 10 A 254 GLY LEU TYR GLU ASN ALA MET GLY GLU SER TYR PRO ARG
SEQRES 11 A 254 ARG GLY ASP TYR GLU PHE ILE LYS LYS LYS ALA GLU ALA
SEQRES 12 A 254 VAL PHE TYR ASP PRO GLU VAL ALA THR LYS GLU ILE VAL
SEQRES 13 A 254 ASP GLU VAL TYR GLU THR VAL SER ASP ARG ASN LYS LEU
SEQRES 14 A 254 VAL LYS THR LEU ALA ILE ALA LYS SER ALA ILE ARG HIS
SEQRES 15 A 254 ASN MET ALA LYS ASP LEU PRO LYS MET LYS THR PRO THR
SEQRES 16 A 254 CYS ILE ILE TRP GLY LYS ASN ASP ASN VAL THR PRO PRO
SEQRES 17 A 254 GLU VAL ALA GLU ASP PHE LYS ARG LEU LEU PRO ASP ALA
SEQRES 18 A 254 ASP LEU TYR TRP ILE ASP LYS CYS GLY HIS ALA ALA MET
SEQRES 19 A 254 MET GLU HIS PRO GLU GLU PHE ASN GLN LEU LEU HIS GLU
SEQRES 20 A 254 TRP PHE LYS GLU ARG ASP PHE
FORMUL 2 HOH *23(H2 O)
HELIX 1 AA1 GLY A 31 ASN A 34 5 4
HELIX 2 AA2 PHE A 35 PHE A 42 1 8
HELIX 3 AA3 PRO A 43 LYS A 45 5 3
HELIX 4 AA4 SER A 65 GLY A 81 1 17
HELIX 5 AA5 LEU A 92 PHE A 104 1 13
HELIX 6 AA6 LYS A 153 GLU A 158 5 6
HELIX 7 AA7 VAL A 159 ASP A 165 1 7
HELIX 8 AA8 LYS A 168 HIS A 182 1 15
HELIX 9 AA9 ASP A 187 MET A 191 5 5
HELIX 10 AB1 PRO A 207 LEU A 218 1 12
HELIX 11 AB2 ALA A 232 HIS A 237 1 6
HELIX 12 AB3 HIS A 237 ASP A 253 1 17
SHEET 1 AA1 8 HIS A 4 GLU A 8 0
SHEET 2 AA1 8 PHE A 11 LYS A 16 -1 O TYR A 13 N LYS A 6
SHEET 3 AA1 8 TYR A 47 PRO A 52 -1 O VAL A 49 N LYS A 16
SHEET 4 AA1 8 THR A 20 LEU A 25 1 N ILE A 22 O LYS A 48
SHEET 5 AA1 8 VAL A 85 SER A 91 1 O LEU A 88 N LEU A 25
SHEET 6 AA1 8 VAL A 108 SER A 116 1 O VAL A 112 N LEU A 87
SHEET 7 AA1 8 THR A 195 GLY A 200 1 O CYS A 196 N ILE A 113
SHEET 8 AA1 8 ALA A 221 ILE A 226 1 O ASP A 222 N ILE A 197
CRYST1 78.968 78.968 78.384 90.00 90.00 120.00 P 32 2 1 6
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 0.012663 0.007311 0.000000 0.00000
SCALE2 0.000000 0.014622 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012758 0.00000
TER 1744 PHE A 254
MASTER 348 0 0 12 8 0 0 6 1766 1 0 20
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