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HEADER HYDROLASE ACTIVATOR 24-DEC-11 3V9A
TITLE CRYSTAL STRUCTURE OF ESTERASE/LIPASE FROM UNCULTURED BACTERIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
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 GENE: ESTE5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, LIPASE, HYDROLASE ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR I.J.KIM,K.H.NAM
REVDAT 1 15-FEB-12 3V9A 0
JRNL AUTH I.J.KIM,K.H.NAM
JRNL TITL CRYSTAL STRUCTURE OF ESTERASE/LIPASE FROM UNCULTURED
JRNL TITL 2 BACTERIUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 16708
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1671
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 47.2522 - 4.7387 0.93 1392 155 0.1793 0.2009
REMARK 3 2 4.7387 - 3.7617 0.95 1315 146 0.1554 0.2138
REMARK 3 3 3.7617 - 3.2864 0.95 1295 144 0.1778 0.2389
REMARK 3 4 3.2864 - 2.9859 0.95 1276 142 0.1924 0.2487
REMARK 3 5 2.9859 - 2.7719 0.95 1277 142 0.1943 0.2732
REMARK 3 6 2.7719 - 2.6085 0.94 1264 140 0.1917 0.2465
REMARK 3 7 2.6085 - 2.4779 0.94 1242 138 0.1806 0.2412
REMARK 3 8 2.4779 - 2.3700 0.94 1240 138 0.1850 0.2318
REMARK 3 9 2.3700 - 2.2788 0.93 1225 135 0.2101 0.2620
REMARK 3 10 2.2788 - 2.2002 0.86 1127 126 0.2653 0.3628
REMARK 3 11 2.2002 - 2.1314 0.94 1236 138 0.2275 0.2750
REMARK 3 12 2.1314 - 2.0705 0.88 1148 127 0.2575 0.2793
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 39.41
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.43130
REMARK 3 B22 (A**2) : 2.43130
REMARK 3 B33 (A**2) : -4.86260
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
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 2278
REMARK 3 ANGLE : 0.916 3092
REMARK 3 CHIRALITY : 0.057 337
REMARK 3 PLANARITY : 0.004 401
REMARK 3 DIHEDRAL : 15.745 833
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2949 15.2404 -0.0296
REMARK 3 T TENSOR
REMARK 3 T11: 0.1424 T22: 0.1418
REMARK 3 T33: 0.1674 T12: -0.0165
REMARK 3 T13: -0.0063 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.1035 L22: 2.1435
REMARK 3 L33: 2.4401 L12: 0.2233
REMARK 3 L13: 0.3856 L23: 0.2373
REMARK 3 S TENSOR
REMARK 3 S11: -0.0410 S12: 0.1741 S13: -0.1020
REMARK 3 S21: -0.0877 S22: 0.1054 S23: 0.0098
REMARK 3 S31: 0.0792 S32: 0.0902 S33: -0.0395
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 3V9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB069756.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16720
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
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: PHENIX.AUTOMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, PH 7.0, 2.0M AMMONIUM
REMARK 280 SULFATE, 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 74.55850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.53000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.27925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.53000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.53000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.83775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.53000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.53000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.27925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.53000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.53000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.83775
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 74.55850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 VAL A 194
REMARK 465 ALA A 195
REMARK 465 PRO A 196
REMARK 465 LEU A 298
REMARK 465 ALA A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 LEU A 302
REMARK 465 GLU A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
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 558 O HOH A 561 1.99
REMARK 500 NH2 ARG A 126 O HOH A 600 2.08
REMARK 500 O HOH A 571 O HOH A 603 2.09
REMARK 500 O HOH A 577 O HOH A 585 2.10
REMARK 500 O HOH A 601 O HOH A 602 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 144 -122.98 57.77
REMARK 500 ASP A 237 56.16 -100.61
REMARK 500 ASP A 265 -0.33 67.25
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FAK RELATED DB: PDB
DBREF 3V9A A 1 297 UNP Q0GMU2 Q0GMU2_9BACT 1 297
SEQADV 3V9A LEU A 298 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A ALA A 299 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A ALA A 300 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A ALA A 301 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A LEU A 302 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A GLU A 303 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 304 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 305 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 306 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 307 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 308 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3V9A HIS A 309 UNP Q0GMU2 EXPRESSION TAG
SEQRES 1 A 309 MET ALA GLY PRO GLU ILE VAL LYS LEU LYS LYS ILE LEU
SEQRES 2 A 309 ARG GLU LYS ALA VAL PRO PRO GLY THR GLU VAL PRO LEU
SEQRES 3 A 309 ASP VAL MET ARG LYS GLY MET GLU LYS VAL ALA PHE LYS
SEQRES 4 A 309 ALA ALA ASP ASP ILE GLN VAL GLU GLN VAL THR VAL ALA
SEQRES 5 A 309 GLY CYS ALA ALA GLU TRP VAL ARG ALA PRO GLY CYS GLN
SEQRES 6 A 309 ALA GLY LYS ALA ILE LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 A 309 VAL MET GLY SER ILE ASN THR HIS ARG SER MET VAL GLY
SEQRES 8 A 309 GLU ILE SER ARG ALA SER GLN ALA ALA ALA LEU LEU LEU
SEQRES 9 A 309 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA
SEQRES 10 A 309 VAL GLU ASP GLY VAL ALA ALA TYR ARG TRP LEU LEU ASP
SEQRES 11 A 309 GLN GLY PHE LYS PRO GLN HIS LEU SER ILE SER GLY ASP
SEQRES 12 A 309 SER ALA GLY GLY GLY LEU VAL LEU ALA VAL LEU VAL SER
SEQRES 13 A 309 ALA ARG ASP GLN GLY LEU PRO MET PRO ALA SER ALA ILE
SEQRES 14 A 309 PRO ILE SER PRO TRP ALA ASP MET THR CYS THR ASN ASP
SEQRES 15 A 309 SER PHE LYS THR ARG ALA GLU ALA ASP PRO MET VAL ALA
SEQRES 16 A 309 PRO GLY GLY ILE ASN LYS MET ALA ALA ARG TYR LEU ASN
SEQRES 17 A 309 GLY ALA ASP ALA LYS HIS PRO TYR ALA SER PRO ASN PHE
SEQRES 18 A 309 ALA ASN LEU LYS GLY LEU PRO PRO LEU LEU ILE HIS VAL
SEQRES 19 A 309 GLY ARG ASP GLU VAL LEU LEU ASP ASP SER ILE LYS LEU
SEQRES 20 A 309 ASP ALA LYS ALA LYS ALA ASP GLY VAL LYS SER THR LEU
SEQRES 21 A 309 GLU ILE TRP ASP ASP MET ILE HIS VAL TRP HIS ALA PHE
SEQRES 22 A 309 HIS PRO MET LEU PRO GLU GLY LYS GLN ALA ILE VAL ARG
SEQRES 23 A 309 VAL GLY GLU PHE MET ARG GLU GLN TRP ALA ALA LEU ALA
SEQRES 24 A 309 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 HOH *106(H2 O)
HELIX 1 1 GLY A 3 ALA A 17 1 15
HELIX 2 2 PRO A 25 VAL A 36 1 12
HELIX 3 3 SER A 82 GLN A 98 1 17
HELIX 4 4 PRO A 115 GLY A 132 1 18
HELIX 5 5 LYS A 134 GLN A 136 5 3
HELIX 6 6 SER A 144 GLN A 160 1 17
HELIX 7 7 ASP A 182 ARG A 187 1 6
HELIX 8 8 GLY A 198 ASN A 208 1 11
HELIX 9 9 SER A 218 ALA A 222 5 5
HELIX 10 10 LEU A 240 ASP A 254 1 15
HELIX 11 11 VAL A 269 HIS A 274 5 6
HELIX 12 12 LEU A 277 ALA A 296 1 20
SHEET 1 A 6 GLN A 45 VAL A 51 0
SHEET 2 A 6 CYS A 54 ARG A 60 -1 O CYS A 54 N VAL A 51
SHEET 3 A 6 ALA A 100 LEU A 104 -1 O ALA A 101 N VAL A 59
SHEET 4 A 6 ALA A 69 LEU A 73 1 N ILE A 70 O LEU A 102
SHEET 5 A 6 LEU A 138 ASP A 143 1 O SER A 141 N LEU A 73
SHEET 6 A 6 SER A 167 ILE A 171 1 O ILE A 171 N GLY A 142
SHEET 1 B 2 LEU A 230 GLY A 235 0
SHEET 2 B 2 SER A 258 TRP A 263 1 O THR A 259 N ILE A 232
CISPEP 1 ALA A 109 PRO A 110 0 0.68
CISPEP 2 PHE A 114 PRO A 115 0 7.25
SITE 1 AC1 6 ASP A 105 TYR A 106 ARG A 107 LEU A 108
SITE 2 AC1 6 HIS A 112 HOH A 521
SITE 1 AC2 4 LYS A 10 ARG A 14 LYS A 39 ALA A 190
SITE 1 AC3 4 PRO A 25 LEU A 26 ARG A 205 HOH A 605
CRYST1 61.060 61.060 149.117 90.00 90.00 90.00 P 41 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 0.016377 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006706 0.00000
TER 2215 ALA A 297
MASTER 306 0 3 12 8 0 4 6 2335 1 15 24
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