HEADER HYDROLASE 07-MAR-11 3R09
TITLE CRYSTAL STRUCTURE OF PROBABLE HAD FAMILY HYDROLASE FROM PSEUDOMONAS
TITLE 2 FLUORESCENS PF-5 WITH BOUND MG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, HALOACID DEHALOGENASE-LIKE FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE HAD FAMILY HYDROLASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 220664;
SOURCE 4 STRAIN: PF-5 / ATCC BAA-477;
SOURCE 5 GENE: PF-5, PFL_5400;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26
KEYWDS STRUCTURAL GENOMICS, ENZYME FUNCTION INTITIATIVE, UNKNOWN FUNCTION,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, NYSGXRC, HALOALKANE DEHALOGENASE FAMILY,
KEYWDS 4 POSSIBLE HYDROLASE, ENZYME FUNCTION INITIATIVE, EFI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.VETTING,Y.PATSKOVSKY,R.TORO,J.FREEMAN,S.MILLER,J.M.SAUDER,
AUTHOR 2 S.K.BURLEY,D.DUNAWAY-MARIANO,K.N.ALLEN,J.A.GERLT,S.C.ALMO,ENZYME
AUTHOR 3 FUNCTION INITIATIVE (EFI),NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 4 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 7 06-DEC-23 3R09 1 REMARK
REVDAT 6 13-SEP-23 3R09 1 REMARK
REVDAT 5 10-FEB-21 3R09 1 AUTHOR JRNL REMARK SEQADV
REVDAT 5 2 1 LINK
REVDAT 4 21-NOV-18 3R09 1 AUTHOR
REVDAT 3 20-NOV-13 3R09 1 JRNL TITLE
REVDAT 2 16-NOV-11 3R09 1 VERSN HETATM
REVDAT 1 20-APR-11 3R09 0
JRNL AUTH M.W.VETTING,Y.PATSKOVSKY,R.TORO,J.FREEMAN,S.MILLER,
JRNL AUTH 2 J.M.SAUDER,S.K.BURLEY,D.DUNAWAY-MARIANO,K.N.ALLEN,J.A.GERLT,
JRNL AUTH 3 S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PROBABLE HAD FAMILY HYDROLASE FROM
JRNL TITL 2 PSEUDOMONAS FLUORESCENS PF-5 WITH BOUND MG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 17198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 857
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 32.0561 - 3.9950 0.99 2996 159 0.1689 0.1744
REMARK 3 2 3.9950 - 3.1718 0.99 2797 145 0.1738 0.2072
REMARK 3 3 3.1718 - 2.7711 0.99 2715 144 0.1838 0.2453
REMARK 3 4 2.7711 - 2.5179 0.98 2681 143 0.1874 0.1881
REMARK 3 5 2.5179 - 2.3375 0.96 2605 136 0.1982 0.2694
REMARK 3 6 2.3375 - 2.1997 0.95 2547 130 0.1940 0.2381
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 : 0.37
REMARK 3 B_SOL : 33.54
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.82820
REMARK 3 B22 (A**2) : 0.82820
REMARK 3 B33 (A**2) : -1.65640
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 1577
REMARK 3 ANGLE : 0.925 2157
REMARK 3 CHIRALITY : 0.060 242
REMARK 3 PLANARITY : 0.005 285
REMARK 3 DIHEDRAL : 12.691 577
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2:23)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5088 6.0248 19.5366
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.0585
REMARK 3 T33: 0.1025 T12: 0.0859
REMARK 3 T13: 0.0371 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0169 L22: 0.0263
REMARK 3 L33: 0.0162 L12: 0.0075
REMARK 3 L13: -0.0080 L23: -0.0214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.0157 S13: 0.0034
REMARK 3 S21: -0.0187 S22: 0.0210 S23: -0.0087
REMARK 3 S31: 0.0088 S32: -0.0005 S33: -0.0053
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 24:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0748 -7.8634 -2.2895
REMARK 3 T TENSOR
REMARK 3 T11: 0.2181 T22: 0.0724
REMARK 3 T33: 0.1468 T12: 0.0183
REMARK 3 T13: -0.0474 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0380 L22: 0.0113
REMARK 3 L33: 0.0056 L12: -0.0059
REMARK 3 L13: -0.0137 L23: 0.0025
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: -0.0124 S13: 0.0109
REMARK 3 S21: -0.0025 S22: 0.0295 S23: -0.0612
REMARK 3 S31: 0.0238 S32: 0.0362 S33: 0.0212
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 61:85)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.0637 -1.8676 16.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.2295 T22: 0.1160
REMARK 3 T33: 0.1582 T12: 0.0532
REMARK 3 T13: 0.0136 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.0772 L22: 0.0345
REMARK 3 L33: 0.0333 L12: 0.0462
REMARK 3 L13: 0.0047 L23: 0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0663 S12: 0.0059 S13: -0.0564
REMARK 3 S21: 0.0112 S22: 0.0548 S23: 0.0129
REMARK 3 S31: 0.0318 S32: -0.0135 S33: 0.0029
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 86:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2451 7.5974 20.9798
REMARK 3 T TENSOR
REMARK 3 T11: 0.1681 T22: 0.0953
REMARK 3 T33: 0.1372 T12: 0.0827
REMARK 3 T13: -0.0440 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.0037 L22: 0.0032
REMARK 3 L33: 0.0113 L12: -0.0034
REMARK 3 L13: 0.0064 L23: -0.0054
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0074 S13: -0.0221
REMARK 3 S21: -0.0082 S22: -0.0032 S23: 0.0081
REMARK 3 S31: 0.0032 S32: -0.0035 S33: -0.0106
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 97:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1659 6.7817 18.8018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1755 T22: 0.1231
REMARK 3 T33: 0.2082 T12: 0.0461
REMARK 3 T13: -0.0268 T23: -0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 0.1025 L22: 0.0762
REMARK 3 L33: 0.2163 L12: -0.0791
REMARK 3 L13: -0.1161 L23: 0.0757
REMARK 3 S TENSOR
REMARK 3 S11: -0.0837 S12: -0.0052 S13: -0.0852
REMARK 3 S21: 0.0116 S22: -0.0650 S23: 0.1033
REMARK 3 S31: -0.0054 S32: -0.1120 S33: 0.0511
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 140:187)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1554 15.8212 17.4592
REMARK 3 T TENSOR
REMARK 3 T11: 0.3177 T22: 0.0355
REMARK 3 T33: 0.0997 T12: 0.1586
REMARK 3 T13: 0.0254 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.0137 L22: 0.0143
REMARK 3 L33: 0.0013 L12: -0.0021
REMARK 3 L13: -0.0005 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.0009 S13: -0.0099
REMARK 3 S21: -0.0578 S22: -0.0096 S23: 0.0362
REMARK 3 S31: -0.0711 S32: -0.0252 S33: -0.0099
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 188:198)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.8318 8.2115 27.4667
REMARK 3 T TENSOR
REMARK 3 T11: 0.2015 T22: 0.1643
REMARK 3 T33: 0.1361 T12: 0.0923
REMARK 3 T13: 0.0219 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.0548 L22: 0.0620
REMARK 3 L33: 0.0213 L12: -0.0334
REMARK 3 L13: -0.0149 L23: 0.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.0202 S13: 0.0002
REMARK 3 S21: 0.0060 S22: 0.0084 S23: -0.0047
REMARK 3 S31: -0.0119 S32: 0.0060 S33: -0.0015
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 3R09 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 20.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 51.1000
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 15.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.800
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: 3M9L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 10 MM HEPES PH 8.5, 150 MM
REMARK 280 NACL, 10% GLYCEROL, 5 MM DTT, 10 MM MGCL2, RESERVOIR (2.5 M NAK
REMARK 280 PHOSPHATE PH 5.0, 150 MM NACITRATE), SOAK (1.5 M MGSO4, 200 MM
REMARK 280 MES PH 5.3, 20% GLYCEROL, 10 MIN, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 83.76333
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 167.52667
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 125.64500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 209.40833
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 41.88167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.76333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 167.52667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 209.40833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 125.64500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 41.88167
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: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 212 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 GLY A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
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 MSE A 13 -76.13 -100.92
REMARK 500 MSE A 13 -75.93 -103.41
REMARK 500 ASP A 174 -149.98 -134.52
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 MG A 206 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 12 OD2
REMARK 620 2 ASP A 14 O 74.4
REMARK 620 3 ASP A 152 OD1 83.3 90.0
REMARK 620 4 HOH A 314 O 89.1 82.7 170.7
REMARK 620 5 HOH A 342 O 151.4 77.2 99.8 84.3
REMARK 620 6 HOH A 343 O 100.0 152.9 116.0 70.6 103.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 207
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M9L RELATED DB: PDB
REMARK 900 SAME PROTEIN WITHOUT MG BOUND
REMARK 900 RELATED ID: NYSGXRC-22261A RELATED DB: TARGETDB
DBREF 3R09 A 1 197 UNP Q4K5L5 Q4K5L5_PSEF5 1 197
SEQADV 3R09 GLU A 198 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 GLY A 199 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 200 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 201 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 202 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 203 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 204 UNP Q4K5L5 EXPRESSION TAG
SEQADV 3R09 HIS A 205 UNP Q4K5L5 EXPRESSION TAG
SEQRES 1 A 205 MSE SER LEU SER GLU ILE LYS HIS TRP VAL PHE ASP MSE
SEQRES 2 A 205 ASP GLY THR LEU THR ILE ALA VAL HIS ASP PHE ALA ALA
SEQRES 3 A 205 ILE ARG GLU ALA LEU SER ILE PRO ALA GLU ASP ASP ILE
SEQRES 4 A 205 LEU THR HIS LEU ALA ALA LEU PRO ALA ASP GLU SER ALA
SEQRES 5 A 205 ALA LYS HIS ALA TRP LEU LEU GLU HIS GLU ARG ASP LEU
SEQRES 6 A 205 ALA GLN GLY SER ARG PRO ALA PRO GLY ALA VAL GLU LEU
SEQRES 7 A 205 VAL ARG GLU LEU ALA GLY ARG GLY TYR ARG LEU GLY ILE
SEQRES 8 A 205 LEU THR ARG ASN ALA ARG GLU LEU ALA HIS VAL THR LEU
SEQRES 9 A 205 GLU ALA ILE GLY LEU ALA ASP CYS PHE ALA GLU ALA ASP
SEQRES 10 A 205 VAL LEU GLY ARG ASP GLU ALA PRO PRO LYS PRO HIS PRO
SEQRES 11 A 205 GLY GLY LEU LEU LYS LEU ALA GLU ALA TRP ASP VAL SER
SEQRES 12 A 205 PRO SER ARG MSE VAL MSE VAL GLY ASP TYR ARG PHE ASP
SEQRES 13 A 205 LEU ASP CYS GLY ARG ALA ALA GLY THR ARG THR VAL LEU
SEQRES 14 A 205 VAL ASN LEU PRO ASP ASN PRO TRP PRO GLU LEU THR ASP
SEQRES 15 A 205 TRP HIS ALA ARG ASP CYS ALA GLN LEU ARG ASP LEU LEU
SEQRES 16 A 205 SER ALA GLU GLY HIS HIS HIS HIS HIS HIS
MODRES 3R09 MSE A 13 MET SELENOMETHIONINE
MODRES 3R09 MSE A 147 MET SELENOMETHIONINE
MODRES 3R09 MSE A 149 MET SELENOMETHIONINE
HET MSE A 13 16
HET MSE A 147 8
HET MSE A 149 8
HET MG A 206 1
HET SO4 A 207 5
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 MG MG 2+
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *158(H2 O)
HELIX 1 1 SER A 2 ILE A 6 5 5
HELIX 2 2 ASP A 23 LEU A 31 1 9
HELIX 3 3 ASP A 38 LEU A 46 1 9
HELIX 4 4 PRO A 47 HIS A 61 1 15
HELIX 5 5 HIS A 61 LEU A 65 1 5
HELIX 6 6 GLY A 74 ARG A 85 1 12
HELIX 7 7 ALA A 96 ILE A 107 1 12
HELIX 8 8 LEU A 109 PHE A 113 5 5
HELIX 9 9 ALA A 114 ALA A 116 5 3
HELIX 10 10 PRO A 130 ASP A 141 1 12
HELIX 11 11 SER A 143 SER A 145 5 3
HELIX 12 12 TYR A 153 GLY A 164 1 12
HELIX 13 13 TRP A 177 THR A 181 5 5
HELIX 14 14 ASP A 187 GLU A 198 1 12
SHEET 1 A 6 VAL A 118 LEU A 119 0
SHEET 2 A 6 ARG A 88 LEU A 92 1 N ILE A 91 O LEU A 119
SHEET 3 A 6 HIS A 8 PHE A 11 1 N TRP A 9 O GLY A 90
SHEET 4 A 6 MSE A 147 GLY A 151 1 O VAL A 150 N VAL A 10
SHEET 5 A 6 ARG A 166 VAL A 170 1 O VAL A 168 N MSE A 149
SHEET 6 A 6 TRP A 183 ALA A 185 1 O ALA A 185 N LEU A 169
SHEET 1 B 2 THR A 18 HIS A 22 0
SHEET 2 B 2 ALA A 66 PRO A 71 -1 O ARG A 70 N ILE A 19
LINK C ASP A 12 N AMSE A 13 1555 1555 1.33
LINK C ASP A 12 N BMSE A 13 1555 1555 1.33
LINK C AMSE A 13 N ASP A 14 1555 1555 1.33
LINK C BMSE A 13 N ASP A 14 1555 1555 1.33
LINK C ARG A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N VAL A 148 1555 1555 1.33
LINK C VAL A 148 N MSE A 149 1555 1555 1.33
LINK C MSE A 149 N VAL A 150 1555 1555 1.34
LINK OD2 ASP A 12 MG MG A 206 1555 1555 2.29
LINK O ASP A 14 MG MG A 206 1555 1555 2.35
LINK OD1 ASP A 152 MG MG A 206 1555 1555 2.53
LINK MG MG A 206 O HOH A 314 1555 1555 2.45
LINK MG MG A 206 O HOH A 342 1555 1555 2.25
LINK MG MG A 206 O HOH A 343 1555 1555 2.36
CISPEP 1 LYS A 127 PRO A 128 0 4.22
SITE 1 AC1 7 ASP A 12 ASP A 14 ASP A 152 ASP A 156
SITE 2 AC1 7 HOH A 314 HOH A 342 HOH A 343
SITE 1 AC2 3 HIS A 8 ARG A 146 HOH A 219
CRYST1 66.299 66.299 251.290 90.00 90.00 120.00 P 61 2 2 12
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 0.015083 0.008708 0.000000 0.00000
SCALE2 0.000000 0.017417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003979 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
