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HEADER HYDROLASE 09-SEP-11 3TRD
TITLE STRUCTURE OF AN ALPHA-BETA SERINE HYDROLASE HOMOLOGUE FROM COXIELLA
TITLE 2 BURNETII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COXIELLA BURNETII;
SOURCE 3 ORGANISM_TAXID: 777;
SOURCE 4 GENE: CBU_1769;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS CELLULAR PROCESSES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHEUNG,M.FRANKLIN,M.RUDOLPH,M.CASSIDY,E.GARY,F.BURSHTEYN,J.LOVE
REVDAT 1 21-SEP-11 3TRD 0
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 28220
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1437
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 31.2633 - 3.2306 0.98 2827 152 0.1514 0.1694
REMARK 3 2 3.2306 - 2.5646 1.00 2767 136 0.1477 0.1878
REMARK 3 3 2.5646 - 2.2405 1.00 2736 144 0.1457 0.1958
REMARK 3 4 2.2405 - 2.0357 1.00 2704 144 0.1572 0.1756
REMARK 3 5 2.0357 - 1.8898 0.99 2684 149 0.1545 0.1975
REMARK 3 6 1.8898 - 1.7784 0.99 2636 135 0.1630 0.2074
REMARK 3 7 1.7784 - 1.6893 0.98 2638 149 0.1899 0.2233
REMARK 3 8 1.6893 - 1.6158 0.98 2635 135 0.2131 0.2652
REMARK 3 9 1.6158 - 1.5536 0.98 2604 137 0.2666 0.3089
REMARK 3 10 1.5536 - 1.5000 0.96 2552 156 0.3897 0.3852
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.44
REMARK 3 B_SOL : 61.92
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45430
REMARK 3 B22 (A**2) : 2.92920
REMARK 3 B33 (A**2) : -0.73450
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 : 0.006 1691
REMARK 3 ANGLE : 0.992 2295
REMARK 3 CHIRALITY : 0.068 253
REMARK 3 PLANARITY : 0.005 296
REMARK 3 DIHEDRAL : 13.235 602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ -2:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0953 57.4998 -5.9441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1396 T22: 0.0909
REMARK 3 T33: 0.1169 T12: 0.0080
REMARK 3 T13: -0.0214 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.0132 L22: 0.0308
REMARK 3 L33: 0.1442 L12: -0.0058
REMARK 3 L13: 0.0206 L23: 0.0309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.0178 S13: 0.0136
REMARK 3 S21: 0.0509 S22: -0.0134 S23: -0.0677
REMARK 3 S31: -0.1590 S32: -0.0329 S33: 0.0083
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 14:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1963 53.0841 -5.5797
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.1679
REMARK 3 T33: 0.1173 T12: 0.0574
REMARK 3 T13: 0.0272 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.2624 L22: 0.1712
REMARK 3 L33: 0.1895 L12: -0.1982
REMARK 3 L13: -0.0116 L23: -0.0834
REMARK 3 S TENSOR
REMARK 3 S11: -0.1797 S12: -0.2091 S13: 0.2256
REMARK 3 S21: 0.1866 S22: 0.1301 S23: 0.0248
REMARK 3 S31: -0.2022 S32: -0.0903 S33: -0.1669
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 29:162)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5300 44.3929 -16.5611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: 0.0727
REMARK 3 T33: 0.0712 T12: 0.0008
REMARK 3 T13: -0.0040 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.5475 L22: 0.5781
REMARK 3 L33: 0.2864 L12: 0.0776
REMARK 3 L13: 0.0873 L23: 0.1631
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: -0.0039 S13: -0.0060
REMARK 3 S21: 0.0518 S22: 0.0037 S23: -0.0342
REMARK 3 S31: 0.0140 S32: -0.0057 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 163:172)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5938 30.7335 -29.2806
REMARK 3 T TENSOR
REMARK 3 T11: 0.1068 T22: 0.1309
REMARK 3 T33: 0.1973 T12: -0.0008
REMARK 3 T13: -0.0179 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.0135 L22: 0.0122
REMARK 3 L33: 0.0675 L12: -0.0037
REMARK 3 L13: -0.0200 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: 0.1772 S12: 0.0311 S13: -0.2297
REMARK 3 S21: 0.0535 S22: 0.0467 S23: -0.1006
REMARK 3 S31: 0.0405 S32: 0.0858 S33: 0.0044
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 173:192)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1792 39.8740 -25.5981
REMARK 3 T TENSOR
REMARK 3 T11: 0.1020 T22: 0.1185
REMARK 3 T33: 0.1077 T12: -0.0160
REMARK 3 T13: -0.0122 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.0560 L22: 0.0451
REMARK 3 L33: 0.0664 L12: 0.0324
REMARK 3 L13: 0.0218 L23: 0.0708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: -0.0259 S13: -0.0487
REMARK 3 S21: 0.0834 S22: 0.0400 S23: 0.0389
REMARK 3 S31: 0.0350 S32: -0.0334 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 193:205)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8971 44.3773 -17.4637
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.1961
REMARK 3 T33: 0.1642 T12: -0.0033
REMARK 3 T13: 0.0236 T23: -0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 0.0092 L22: 0.0965
REMARK 3 L33: 0.1389 L12: 0.0206
REMARK 3 L13: -0.0297 L23: 0.0095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: 0.0149 S13: -0.0244
REMARK 3 S21: 0.0297 S22: -0.1379 S23: 0.2615
REMARK 3 S31: 0.0590 S32: -0.2904 S33: -0.1144
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 3TRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28456
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.63M SODIUM
REMARK 280 DIHYDROGEN PHOSPHATE, 0.94M DIPOTASSIUM HYDROGEN PHOSPHATE, 0.02M
REMARK 280 SODIUM HYDROXIDE, PH 4.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 24.93050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.25650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.95250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.25650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.93050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.95250
REMARK 290 SMTRY3 4 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: 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 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 469 O HOH A 470 1.93
REMARK 500 O HOH A 252 O HOH A 255 2.10
REMARK 500 O HOH A 265 O HOH A 479 2.18
REMARK 500 O HOH A 263 O HOH A 459 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 SER A 110 -116.10 47.38
REMARK 500
REMARK 500 REMARK: NULL
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 A 209 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 253 O
REMARK 620 2 SER A 74 O 133.3
REMARK 620 3 GLY A 72 O 73.3 93.3
REMARK 620 4 HOH A 354 O 107.8 84.7 178.0
REMARK 620 5 GLY A 70 O 53.1 84.4 93.2 86.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 208 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACT A 206 OXT
REMARK 620 2 SER A 110 OG 76.2
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 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 211
DBREF 3TRD A 1 205 UNP Q83AV9 Q83AV9_COXBU 1 205
SEQADV 3TRD SER A -2 UNP Q83AV9 EXPRESSION TAG
SEQADV 3TRD TYR A -1 UNP Q83AV9 EXPRESSION TAG
SEQADV 3TRD VAL A 0 UNP Q83AV9 EXPRESSION TAG
SEQRES 1 A 208 SER TYR VAL MET THR ASN GLU ASP PHE LEU ILE GLN GLY
SEQRES 2 A 208 PRO VAL GLY GLN LEU GLU VAL MET ILE THR ARG PRO LYS
SEQRES 3 A 208 GLY ILE GLU LYS SER VAL THR GLY ILE ILE CYS HIS PRO
SEQRES 4 A 208 HIS PRO LEU HIS GLY GLY THR MET ASN ASN LYS VAL VAL
SEQRES 5 A 208 THR THR LEU ALA LYS ALA LEU ASP GLU LEU GLY LEU LYS
SEQRES 6 A 208 THR VAL ARG PHE ASN PHE ARG GLY VAL GLY LYS SER GLN
SEQRES 7 A 208 GLY ARG TYR ASP ASN GLY VAL GLY GLU VAL GLU ASP LEU
SEQRES 8 A 208 LYS ALA VAL LEU ARG TRP VAL GLU HIS HIS TRP SER GLN
SEQRES 9 A 208 ASP ASP ILE TRP LEU ALA GLY PHE SER PHE GLY ALA TYR
SEQRES 10 A 208 ILE SER ALA LYS VAL ALA TYR ASP GLN LYS VAL ALA GLN
SEQRES 11 A 208 LEU ILE SER VAL ALA PRO PRO VAL PHE TYR GLU GLY PHE
SEQRES 12 A 208 ALA SER LEU THR GLN MET ALA SER PRO TRP LEU ILE VAL
SEQRES 13 A 208 GLN GLY ASP GLN ASP GLU VAL VAL PRO PHE GLU GLN VAL
SEQRES 14 A 208 LYS ALA PHE VAL ASN GLN ILE SER SER PRO VAL GLU PHE
SEQRES 15 A 208 VAL VAL MET SER GLY ALA SER HIS PHE PHE HIS GLY ARG
SEQRES 16 A 208 LEU ILE GLU LEU ARG GLU LEU LEU VAL ARG ASN LEU ALA
HET ACT A 206 4
HET ACT A 207 4
HET NA A 208 1
HET NA A 209 1
HET PO4 A 210 5
HET PO4 A 211 5
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 NA 2(NA 1+)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 8 HOH *269(H2 O)
HELIX 1 1 HIS A 37 GLY A 41 5 5
HELIX 2 2 ASN A 46 LEU A 59 1 14
HELIX 3 3 VAL A 82 TRP A 99 1 18
HELIX 4 4 SER A 110 GLN A 123 1 14
HELIX 5 5 TYR A 137 ALA A 141 5 5
HELIX 6 6 PRO A 162 ILE A 173 1 12
HELIX 7 7 ARG A 192 ALA A 205 1 14
SHEET 1 A 8 PHE A 6 GLN A 9 0
SHEET 2 A 8 GLN A 14 THR A 20 -1 O VAL A 17 N PHE A 6
SHEET 3 A 8 LYS A 62 PHE A 66 -1 O ARG A 65 N MET A 18
SHEET 4 A 8 VAL A 29 CYS A 34 1 N ILE A 33 O VAL A 64
SHEET 5 A 8 ASP A 103 PHE A 109 1 O ASP A 103 N THR A 30
SHEET 6 A 8 GLN A 127 VAL A 131 1 O GLN A 127 N LEU A 106
SHEET 7 A 8 TRP A 150 GLY A 155 1 O VAL A 153 N SER A 130
SHEET 8 A 8 GLU A 178 MET A 182 1 O VAL A 180 N ILE A 152
LINK NA NA A 209 O HOH A 253 1555 1555 2.65
LINK OXT ACT A 206 NA NA A 208 1555 1555 2.71
LINK O SER A 74 NA NA A 209 1555 1555 2.75
LINK O GLY A 72 NA NA A 209 1555 1555 2.81
LINK NA NA A 209 O HOH A 354 1555 1555 2.82
LINK OG SER A 110 NA NA A 208 1555 1555 2.97
LINK O GLY A 70 NA NA A 209 1555 1555 3.17
SITE 1 AC1 9 TYR A -1 HIS A 37 SER A 110 PHE A 136
SITE 2 AC1 9 TYR A 137 VAL A 160 SER A 183 NA A 208
SITE 3 AC1 9 HOH A 320
SITE 1 AC2 5 THR A 43 ASN A 45 HOH A 289 HOH A 428
SITE 2 AC2 5 HOH A 451
SITE 1 AC3 5 TYR A -1 HIS A 37 SER A 110 PHE A 111
SITE 2 AC3 5 ACT A 206
SITE 1 AC4 6 GLY A 70 GLY A 72 SER A 74 HOH A 253
SITE 2 AC4 6 HOH A 333 HOH A 354
SITE 1 AC5 10 SER A -2 TYR A -1 ASN A 46 LYS A 47
SITE 2 AC5 10 HOH A 248 HOH A 274 HOH A 304 HOH A 366
SITE 3 AC5 10 HOH A 444 HOH A 448
SITE 1 AC6 12 SER A -2 ARG A 21 GLU A 26 GLY A 41
SITE 2 AC6 12 LYS A 62 TRP A 99 HOH A 215 HOH A 237
SITE 3 AC6 12 HOH A 238 HOH A 267 HOH A 378 HOH A 405
CRYST1 49.861 55.905 62.513 90.00 90.00 90.00 P 21 21 21 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 0.020056 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015997 0.00000
TER 1637 ALA A 205
MASTER 368 0 6 7 8 0 15 6 1922 1 27 16
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