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HEADER HYDROLASE 07-MAR-14 4PSU
TITLE CRYSTAL STRUCTURE OF ALPHA/BETA HYDROLASE FROM RHODOPSEUDOMONAS
TITLE 2 PALUSTRIS CGA009
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 258594;
SOURCE 4 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 5 GENE: RPA1511;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NOCEK,M.HAJIGHASEMI,X.XU,H.CUI,A.SAVCHENKO,A.YAKUNIN
REVDAT 1 11-MAR-15 4PSU 0
JRNL AUTH B.NOCEK,M.HAJIGHASEMI,X.XU,H.CUI,A.SAVCHENKO,A.YAKUNIN
JRNL TITL CRYSTAL STRUCTURE OF ALPHA/BETA HYDROLASE FROM
JRNL TITL 2 RHODOPSEUDOMONAS PALUSTRIS CGA009
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 14607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 734
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 31.9647 - 4.5717 0.95 3267 172 0.1604 0.1652
REMARK 3 2 4.5717 - 3.6303 0.99 3348 165 0.1405 0.1857
REMARK 3 3 3.6303 - 3.1719 0.99 3396 181 0.1758 0.2117
REMARK 3 4 3.1719 - 2.8821 0.99 3321 216 0.2095 0.2777
REMARK 3 5 2.8821 - 2.6756 0.93 3133 179 0.2291 0.3062
REMARK 3 6 2.6756 - 2.5180 0.79 2688 115 0.2274 0.3109
REMARK 3 7 2.5180 - 2.3919 0.61 2108 126 0.2255 0.2082
REMARK 3 8 2.3919 - 2.2878 0.48 1606 80 0.2296 0.2821
REMARK 3 9 2.2878 - 2.2000 0.35 1197 70 0.2304 0.3061
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) : 23.770
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 2230
REMARK 3 ANGLE : 0.846 3036
REMARK 3 CHIRALITY : 0.032 342
REMARK 3 PLANARITY : 0.005 391
REMARK 3 DIHEDRAL : 14.562 811
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 4 through 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7100 17.9384 72.2040
REMARK 3 T TENSOR
REMARK 3 T11: 0.1812 T22: 0.1768
REMARK 3 T33: 0.2438 T12: -0.0129
REMARK 3 T13: 0.0044 T23: 0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 0.9480 L22: 1.4107
REMARK 3 L33: 0.9481 L12: -0.2009
REMARK 3 L13: 0.0381 L23: -0.3217
REMARK 3 S TENSOR
REMARK 3 S11: 0.0037 S12: 0.1234 S13: 0.3222
REMARK 3 S21: -0.0752 S22: 0.0589 S23: 0.2249
REMARK 3 S31: 0.0310 S32: -0.1027 S33: -0.1309
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 128 through 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8335 1.0434 77.0525
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.1668
REMARK 3 T33: 0.2460 T12: -0.0091
REMARK 3 T13: 0.0148 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.5079 L22: 0.2196
REMARK 3 L33: 0.6707 L12: -0.1797
REMARK 3 L13: -0.5346 L23: 0.3115
REMARK 3 S TENSOR
REMARK 3 S11: -0.2014 S12: -0.0185 S13: -0.2140
REMARK 3 S21: -0.2038 S22: -0.0326 S23: 0.3230
REMARK 3 S31: 0.1030 S32: 0.1283 S33: -0.2112
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 161 through 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8962 14.4491 92.2976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3244 T22: 0.4076
REMARK 3 T33: 0.2946 T12: 0.0631
REMARK 3 T13: 0.0372 T23: -0.0700
REMARK 3 L TENSOR
REMARK 3 L11: 0.1617 L22: 0.1555
REMARK 3 L33: 0.1905 L12: -0.1518
REMARK 3 L13: -0.0852 L23: 0.0366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: -0.3176 S13: 0.1704
REMARK 3 S21: 0.3186 S22: 0.1135 S23: 0.0391
REMARK 3 S31: 0.1478 S32: 0.0286 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 214 through 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5328 0.4868 73.9388
REMARK 3 T TENSOR
REMARK 3 T11: 0.2413 T22: 0.1876
REMARK 3 T33: 0.2265 T12: -0.0341
REMARK 3 T13: 0.0107 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.2303 L22: 1.6538
REMARK 3 L33: 0.8717 L12: -0.1706
REMARK 3 L13: 0.2728 L23: -0.2794
REMARK 3 S TENSOR
REMARK 3 S11: -0.0855 S12: 0.0145 S13: -0.0555
REMARK 3 S21: -0.1535 S22: 0.0284 S23: 0.0116
REMARK 3 S31: 0.2240 S32: 0.1077 S33: -0.0043
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 4PSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085177.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-13
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 : 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) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL3000
REMARK 200 DATA SCALING SOFTWARE : HKL3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16885
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 32.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
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: SAD
REMARK 200 SOFTWARE USED: HKL3000, MLPHARE,DM, ARP/WARP, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 20%
REMARK 280 PEG3350, 4% JEFFMINE M-600, 1/300 TRYPSIN, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 40.00650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.71250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.85100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.00650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.71250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.85100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.00650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.71250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.85100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.00650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.71250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 46.85100
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 MSE A 2
REMARK 465 SER A 3
REMARK 465 ARG A 84
REMARK 465 GLY A 85
REMARK 465 HIS A 86
REMARK 465 GLU A 293
REMARK 465 ASN A 294
REMARK 465 ILE A 295
REMARK 465 GLU A 296
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 153 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MSE A 159 CG SE CE
REMARK 470 MSE A 162 CG SE CE
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 LYS A 201 CE NZ
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 LYS A 226 CD CE NZ
REMARK 470 LYS A 291 CD CE NZ
REMARK 470 LEU A 292 CG CD1 CD2
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 ALA A 51 -159.07 -109.06
REMARK 500 MSE A 88 49.71 -101.48
REMARK 500 SER A 115 -124.35 58.51
REMARK 500 ALA A 268 -47.21 76.78
REMARK 500 LEU A 272 41.12 -101.06
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 A 455 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH A 456 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH A 464 DISTANCE = 5.58 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 12P A 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12P A 301
DBREF 4PSU A 2 296 UNP Q6N9M9 Q6N9M9_RHOPA 1 295
SEQRES 1 A 295 MSE SER ASP LEU VAL TRP SER ARG ASP GLY LEU ASP TRP
SEQRES 2 A 295 PRO HIS ARG GLU ALA SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 A 295 PHE ARG TRP HIS VAL GLN ARG MSE GLY SER PRO ALA ALA
SEQRES 4 A 295 PRO ALA ILE LEU LEU ILE HIS GLY THR GLY ALA ALA SER
SEQRES 5 A 295 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER ARG HIS
SEQRES 6 A 295 TYR HIS VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 A 295 THR GLN THR PRO ARG GLY HIS ARG MSE SER LEU PRO GLY
SEQRES 8 A 295 MSE ALA SER ASP LEU ALA ALA LEU LEU ARG VAL LEU GLN
SEQRES 9 A 295 VAL ALA PRO GLN LEU VAL VAL GLY HIS SER ALA GLY ALA
SEQRES 10 A 295 ALA ILE LEU ALA ARG MSE CYS LEU ASP GLY SER ILE ASP
SEQRES 11 A 295 PRO LYS ILE LEU PHE SER LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 A 295 TYR GLY GLY PRO ALA ALA SER PHE PHE SER PRO LEU ALA
SEQRES 13 A 295 LYS MSE LEU VAL MSE ASN PRO PHE VAL PRO SER LEU PHE
SEQRES 14 A 295 ALA TRP GLN ALA GLY HIS ARG GLY ALA VAL GLU ARG LEU
SEQRES 15 A 295 ILE GLY ASN THR GLY SER THR ILE ASP PRO ALA GLY ILE
SEQRES 16 A 295 LYS LEU TYR GLY LYS LEU VAL SER SER PRO ASN HIS VAL
SEQRES 17 A 295 ALA ALA ALA LEU ARG MSE MSE ALA ASN TRP ASP LEU GLU
SEQRES 18 A 295 PRO LEU LEU LYS ALA LEU PRO ASN LEU LYS PRO LEU LEU
SEQRES 19 A 295 VAL LEU VAL ALA ALA GLU GLY ASP ARG ALA ILE PRO PRO
SEQRES 20 A 295 SER VAL ALA VAL LYS VAL ARG GLU ILE LEU PRO LYS ALA
SEQRES 21 A 295 VAL ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 A 295 GLU GLU ARG PRO ALA LEU ILE ALA ALA LEU ILE GLU ARG
SEQRES 23 A 295 TYR ALA GLU LYS LEU GLU ASN ILE GLU
MODRES 4PSU MSE A 35 MET SELENOMETHIONINE
MODRES 4PSU MSE A 88 MET SELENOMETHIONINE
MODRES 4PSU MSE A 93 MET SELENOMETHIONINE
MODRES 4PSU MSE A 124 MET SELENOMETHIONINE
MODRES 4PSU MSE A 159 MET SELENOMETHIONINE
MODRES 4PSU MSE A 162 MET SELENOMETHIONINE
MODRES 4PSU MSE A 215 MET SELENOMETHIONINE
MODRES 4PSU MSE A 216 MET SELENOMETHIONINE
HET MSE A 35 13
HET MSE A 88 8
HET MSE A 93 8
HET MSE A 124 8
HET MSE A 159 5
HET MSE A 162 5
HET MSE A 215 8
HET MSE A 216 8
HET 12P A 301 22
HETNAM MSE SELENOMETHIONINE
HETNAM 12P DODECAETHYLENE GLYCOL
HETSYN 12P POLYETHYLENE GLYCOL PEG400
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 12P C24 H50 O13
FORMUL 3 HOH *69(H2 O)
HELIX 1 1 VAL A 6 GLY A 11 1 6
HELIX 2 2 HIS A 16 GLU A 18 5 3
HELIX 3 3 ALA A 52 ARG A 57 5 6
HELIX 4 4 GLY A 58 SER A 64 1 7
HELIX 5 5 SER A 89 GLN A 105 1 17
HELIX 6 6 ALA A 116 GLY A 128 1 13
HELIX 7 7 ALA A 149 ASN A 163 1 15
HELIX 8 8 PRO A 164 ALA A 174 1 11
HELIX 9 9 GLY A 178 ASN A 186 1 9
HELIX 10 10 ASP A 192 SER A 204 1 13
HELIX 11 11 SER A 205 ASN A 218 1 14
HELIX 12 12 LEU A 221 LEU A 228 1 8
HELIX 13 13 PRO A 229 LEU A 231 5 3
HELIX 14 14 PRO A 248 LEU A 258 1 11
HELIX 15 15 LEU A 272 ARG A 277 1 6
HELIX 16 16 ARG A 277 GLU A 290 1 14
SHEET 1 A 8 SER A 20 ALA A 25 0
SHEET 2 A 8 PHE A 28 MSE A 35 -1 O TRP A 30 N ILE A 23
SHEET 3 A 8 HIS A 68 PRO A 72 -1 O ALA A 71 N GLN A 33
SHEET 4 A 8 ALA A 42 ILE A 46 1 N LEU A 45 O VAL A 70
SHEET 5 A 8 LEU A 110 HIS A 114 1 O VAL A 112 N LEU A 44
SHEET 6 A 8 ILE A 134 LEU A 138 1 O PHE A 136 N VAL A 111
SHEET 7 A 8 LEU A 234 ALA A 240 1 O LEU A 234 N LEU A 135
SHEET 8 A 8 VAL A 262 ILE A 266 1 O VAL A 262 N LEU A 237
LINK C ARG A 34 N MSE A 35 1555 1555 1.33
LINK C MSE A 35 N GLY A 36 1555 1555 1.33
LINK C ARG A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N SER A 89 1555 1555 1.33
LINK C GLY A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N ALA A 94 1555 1555 1.33
LINK C ARG A 123 N MSE A 124 1555 1555 1.33
LINK C MSE A 124 N CYS A 125 1555 1555 1.33
LINK C LYS A 158 N MSE A 159 1555 1555 1.33
LINK C MSE A 159 N LEU A 160 1555 1555 1.33
LINK C VAL A 161 N MSE A 162 1555 1555 1.33
LINK C MSE A 162 N ASN A 163 1555 1555 1.33
LINK C ARG A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N MSE A 216 1555 1555 1.33
LINK C MSE A 216 N ALA A 217 1555 1555 1.33
SITE 1 AC1 3 THR A 49 GLY A 50 TYR A 145
CRYST1 80.013 87.425 93.702 90.00 90.00 90.00 I 2 2 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 0.012498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011438 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010672 0.00000
TER 2144 LEU A 292
MASTER 354 0 9 16 8 0 1 6 2218 1 99 23
END |