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HEADER HYDROLASE 11-APR-14 4Q3K
TITLE CRYSTAL STRUCTURE OF MGS-M1, AN ALPHA/BETA HYDROLASE ENZYME FROM A
TITLE 2 MEDEE BASIN DEEP-SEA METAGENOME LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGS-M1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P15-TV LIC
KEYWDS METAGENOME, METAGENOMIC LIBRARY, ALPHA AND BETA PROTEINS, ALPHA/BETA
KEYWDS 2 HYDROLASE SUPERFAMILY, ESTERASE/LIPASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,H.CUI,M.ALCAIDE,M.FERRER,A.SAVCHENKO
REVDAT 1 25-FEB-15 4Q3K 0
JRNL AUTH M.ALCAIDE,P.J.STOGIOS,A.LAFRAYA,A.TCHIGVINTSEV,R.FLICK,
JRNL AUTH 2 R.BARGIELA,T.N.CHERNIKOVA,O.N.REVA,T.HAI,C.C.LEGGEWIE,
JRNL AUTH 3 N.KATZKE,V.LA CONO,R.MATESANZ,M.JEBBAR,K.E.JAEGER,
JRNL AUTH 4 M.M.YAKIMOV,A.F.YAKUNIN,P.N.GOLYSHIN,O.V.GOLYSHINA,
JRNL AUTH 5 A.SAVCHENKO,M.FERRER
JRNL TITL PRESSURE ADAPTATION IS LINKED TO THERMAL ADAPTATION IN
JRNL TITL 2 SALT-SATURATED MARINE HABITATS.
JRNL REF ENVIRON MICROBIOL 2014
JRNL REFN
JRNL PMID 25330254
JRNL DOI 10.1111/1462-2920.12660
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9PRE_1669)
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) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.2
REMARK 3 NUMBER OF REFLECTIONS : 63864
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1869
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 28.3010 - 4.5208 0.94 4907 156 0.1258 0.1498
REMARK 3 2 4.5208 - 3.5906 0.92 4776 155 0.1081 0.1321
REMARK 3 3 3.5906 - 3.1374 0.91 4739 151 0.1218 0.1824
REMARK 3 4 3.1374 - 2.8508 0.91 4722 157 0.1388 0.1475
REMARK 3 5 2.8508 - 2.6467 0.90 4722 147 0.1418 0.1865
REMARK 3 6 2.6467 - 2.4907 0.89 4601 150 0.1404 0.1974
REMARK 3 7 2.4907 - 2.3660 0.88 4590 137 0.1386 0.1769
REMARK 3 8 2.3660 - 2.2631 0.87 4594 151 0.1294 0.1882
REMARK 3 9 2.2631 - 2.1760 0.87 4510 148 0.1326 0.1607
REMARK 3 10 2.1760 - 2.1009 0.85 4466 142 0.1354 0.2139
REMARK 3 11 2.1009 - 2.0353 0.85 4406 141 0.1437 0.1905
REMARK 3 12 2.0353 - 1.9771 0.85 4387 144 0.1606 0.2084
REMARK 3 13 1.9771 - 1.9251 0.84 4385 140 0.1671 0.2002
REMARK 3 14 1.9251 - 1.8781 0.83 4370 144 0.1739 0.2132
REMARK 3 15 1.8781 - 1.8354 0.83 4291 138 0.1862 0.2410
REMARK 3 16 1.8354 - 1.7964 0.82 4278 140 0.1934 0.3096
REMARK 3 17 1.7964 - 1.7604 0.81 4308 134 0.2170 0.2671
REMARK 3 18 1.7604 - 1.7272 0.80 4155 131 0.2282 0.2758
REMARK 3 19 1.7272 - 1.6964 0.81 4236 132 0.2407 0.2956
REMARK 3 20 1.6964 - 1.6676 0.80 4166 129 0.2793 0.3170
REMARK 3 21 1.6676 - 1.6407 0.78 4019 126 0.2944 0.3168
REMARK 3 22 1.6407 - 1.6155 0.74 3924 129 0.2892 0.3186
REMARK 3 23 1.6155 - 1.5917 0.69 3553 118 0.2968 0.3194
REMARK 3 24 1.5917 - 1.5693 0.58 3080 101 0.2966 0.3280
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.480
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 : 0.009 4062
REMARK 3 ANGLE : 1.230 5534
REMARK 3 CHIRALITY : 0.053 612
REMARK 3 PLANARITY : 0.006 715
REMARK 3 DIHEDRAL : 13.169 1528
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resi -1:74
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6985 96.9240 12.8916
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.1399
REMARK 3 T33: 0.1308 T12: -0.0105
REMARK 3 T13: 0.0015 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 1.7950 L22: 1.0182
REMARK 3 L33: 3.3241 L12: -0.1210
REMARK 3 L13: 0.8961 L23: -0.4580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0367 S12: 0.0338 S13: 0.1286
REMARK 3 S21: 0.0255 S22: -0.0110 S23: -0.0094
REMARK 3 S31: -0.1490 S32: 0.3143 S33: 0.0568
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resi 75:145
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1835 99.0465 25.0075
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1749
REMARK 3 T33: 0.1285 T12: 0.0078
REMARK 3 T13: -0.0039 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 2.2577 L22: 1.0016
REMARK 3 L33: 1.9502 L12: 0.3103
REMARK 3 L13: 0.1181 L23: -0.2173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.3265 S13: 0.0866
REMARK 3 S21: 0.0456 S22: 0.0225 S23: -0.0115
REMARK 3 S31: -0.0101 S32: 0.0786 S33: -0.0209
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain A and resi 146:239
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8769 93.2559 19.4398
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.1378
REMARK 3 T33: 0.1372 T12: -0.0057
REMARK 3 T13: 0.0024 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 2.3878 L22: 1.0397
REMARK 3 L33: 1.7502 L12: -0.0307
REMARK 3 L13: 0.3864 L23: 0.0776
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: -0.2479 S13: -0.1251
REMARK 3 S21: 0.0782 S22: -0.0101 S23: 0.0045
REMARK 3 S31: 0.0610 S32: -0.0711 S33: -0.0070
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain B and resi -1:74
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3479 92.7930 -5.5306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1187 T22: 0.1635
REMARK 3 T33: 0.1313 T12: 0.0115
REMARK 3 T13: -0.0026 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.4238 L22: 1.0432
REMARK 3 L33: 2.4545 L12: 0.5276
REMARK 3 L13: -0.9197 L23: -0.8071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: 0.0365 S13: -0.0811
REMARK 3 S21: -0.0133 S22: -0.0594 S23: -0.0639
REMARK 3 S31: 0.0303 S32: 0.3149 S33: 0.0605
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain B and resi 75:145
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1829 90.5466 -18.2744
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.2426
REMARK 3 T33: 0.1470 T12: 0.0207
REMARK 3 T13: 0.0051 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 2.7350 L22: 0.9294
REMARK 3 L33: 1.8152 L12: -0.6154
REMARK 3 L13: 0.0507 L23: 0.0723
REMARK 3 S TENSOR
REMARK 3 S11: 0.0623 S12: 0.4131 S13: -0.1320
REMARK 3 S21: -0.0842 S22: -0.1011 S23: -0.0181
REMARK 3 S31: 0.0682 S32: 0.3117 S33: 0.0498
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain B and resi 146:239
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9204 96.8711 -16.8415
REMARK 3 T TENSOR
REMARK 3 T11: 0.1075 T22: 0.1752
REMARK 3 T33: 0.1189 T12: 0.0036
REMARK 3 T13: -0.0018 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 2.3155 L22: 1.2574
REMARK 3 L33: 1.6963 L12: 0.1485
REMARK 3 L13: 0.3076 L23: 0.1831
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.2808 S13: 0.0360
REMARK 3 S21: -0.0708 S22: -0.0369 S23: -0.0077
REMARK 3 S31: -0.0510 S32: 0.1012 S33: -0.0100
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 4Q3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085559.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
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 : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63876
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 30.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.48500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.PHASER)
REMARK 200 STARTING MODEL: PDB ENTRY 3HXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POTASSIUM FLUORIDE, 20% PEG3350.
REMARK 280 CRYOPROTECTANT:12% GLYCEROL., PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 39.49550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.35800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.49550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.35800
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 300 REMARK: THE AUTHORS HAVE INDICATED THAT THE BIOLOGICAL UNIT IS
REMARK 300 UNKNOWN AT THIS TIME
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 717 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 598 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 413 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 486 LIES ON A SPECIAL POSITION.
REMARK 450
REMARK 450 SOURCE
REMARK 450 THE SAMPLE WAS EXTRACTED FROM MEDEE BASIN DEEP-SEA AND ANALYZED BY
REMARK 450 USING METAGENOME LIBRARY TECHNIQUE
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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
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 ASN A 9 -166.18 -161.24
REMARK 500 ALA A 52 -97.10 -118.18
REMARK 500 LYS A 74 -127.05 58.31
REMARK 500 SER A 113 -118.15 54.37
REMARK 500 TYR A 137 59.10 37.22
REMARK 500 LEU A 140 -36.57 -132.48
REMARK 500 TRP A 147 74.55 -154.43
REMARK 500 SER A 204 -134.39 52.75
REMARK 500 ASN B 9 -163.15 -165.00
REMARK 500 ALA B 52 -98.83 -120.12
REMARK 500 LYS B 74 -128.55 55.78
REMARK 500 SER B 113 -115.92 56.50
REMARK 500 TYR B 137 58.80 36.08
REMARK 500 TRP B 147 69.22 -159.99
REMARK 500 SER B 204 -132.36 52.18
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q3L RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3M RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3N RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3O RELATED DB: PDB
DBREF 4Q3K A -20 239 PDB 4Q3K 4Q3K -20 239
DBREF 4Q3K B -20 239 PDB 4Q3K 4Q3K -20 239
SEQRES 1 A 260 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 260 ARG GLU ASN LEU TYR PHE GLN GLY MET ASN ILE SER LYS
SEQRES 3 A 260 ILE THR ILE ASN GLN HIS VAL GLY VAL THR LEU THR CYS
SEQRES 4 A 260 TYR VAL GLN ASP VAL SER GLN GLU MET SER ASN MET SER
SEQRES 5 A 260 LYS ARG PRO ALA MET LEU ILE PHE PRO GLY GLY GLY TYR
SEQRES 6 A 260 GLN PHE CYS SER ASP ARG GLU ALA GLU PRO ILE ALA LEU
SEQRES 7 A 260 SER TYR LEU ALA LYS GLY TYR ASN ALA PHE VAL LEU ARG
SEQRES 8 A 260 TYR SER VAL LYS GLU HIS ALA VAL PHE PRO ARG PRO LEU
SEQRES 9 A 260 ILE ASP ALA GLU ASP ALA LEU SER TYR LEU LYS ASP ASN
SEQRES 10 A 260 ALA HIS ALA LEU HIS ILE ASN PRO ASP LYS ILE ALA VAL
SEQRES 11 A 260 ILE GLY PHE SER ALA GLY GLY HIS LEU ALA THR THR LEU
SEQRES 12 A 260 ALA THR GLU GLY LYS VAL ARG PRO ASN ALA VAL VAL LEU
SEQRES 13 A 260 GLY TYR PRO ALA LEU ILE ARG HIS GLU LYS TYR TRP ASN
SEQRES 14 A 260 PHE PRO THR PRO LYS VAL ASP GLN GLN THR PRO GLU MET
SEQRES 15 A 260 PHE VAL PHE HIS THR PHE GLU ASP ASP LEU VAL PRO LEU
SEQRES 16 A 260 SER HIS PRO LEU TYR ILE VAL GLU GLU LEU SER LYS ALA
SEQRES 17 A 260 ASN ILE PRO VAL GLU PHE HIS LEU PHE LYS SER GLY VAL
SEQRES 18 A 260 HIS GLY LEU SER LEU GLY ASN LYS ILE VAL SER ASN GLY
SEQRES 19 A 260 LEU ASP LYS MET ILE GLU ASP ASP VAL GLN VAL TRP PHE
SEQRES 20 A 260 ASP LEU SER CYS ARG TRP LEU ASP LYS VAL LEU ASP LEU
SEQRES 1 B 260 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 260 ARG GLU ASN LEU TYR PHE GLN GLY MET ASN ILE SER LYS
SEQRES 3 B 260 ILE THR ILE ASN GLN HIS VAL GLY VAL THR LEU THR CYS
SEQRES 4 B 260 TYR VAL GLN ASP VAL SER GLN GLU MET SER ASN MET SER
SEQRES 5 B 260 LYS ARG PRO ALA MET LEU ILE PHE PRO GLY GLY GLY TYR
SEQRES 6 B 260 GLN PHE CYS SER ASP ARG GLU ALA GLU PRO ILE ALA LEU
SEQRES 7 B 260 SER TYR LEU ALA LYS GLY TYR ASN ALA PHE VAL LEU ARG
SEQRES 8 B 260 TYR SER VAL LYS GLU HIS ALA VAL PHE PRO ARG PRO LEU
SEQRES 9 B 260 ILE ASP ALA GLU ASP ALA LEU SER TYR LEU LYS ASP ASN
SEQRES 10 B 260 ALA HIS ALA LEU HIS ILE ASN PRO ASP LYS ILE ALA VAL
SEQRES 11 B 260 ILE GLY PHE SER ALA GLY GLY HIS LEU ALA THR THR LEU
SEQRES 12 B 260 ALA THR GLU GLY LYS VAL ARG PRO ASN ALA VAL VAL LEU
SEQRES 13 B 260 GLY TYR PRO ALA LEU ILE ARG HIS GLU LYS TYR TRP ASN
SEQRES 14 B 260 PHE PRO THR PRO LYS VAL ASP GLN GLN THR PRO GLU MET
SEQRES 15 B 260 PHE VAL PHE HIS THR PHE GLU ASP ASP LEU VAL PRO LEU
SEQRES 16 B 260 SER HIS PRO LEU TYR ILE VAL GLU GLU LEU SER LYS ALA
SEQRES 17 B 260 ASN ILE PRO VAL GLU PHE HIS LEU PHE LYS SER GLY VAL
SEQRES 18 B 260 HIS GLY LEU SER LEU GLY ASN LYS ILE VAL SER ASN GLY
SEQRES 19 B 260 LEU ASP LYS MET ILE GLU ASP ASP VAL GLN VAL TRP PHE
SEQRES 20 B 260 ASP LEU SER CYS ARG TRP LEU ASP LYS VAL LEU ASP LEU
HET CL A 301 1
HET F A 302 1
HET PGE A 303 10
HET CL B 301 1
HET F B 302 1
HET PGE B 303 10
HET PGE B 304 10
HETNAM CL CHLORIDE ION
HETNAM F FLUORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 CL 2(CL 1-)
FORMUL 4 F 2(F 1-)
FORMUL 5 PGE 3(C6 H14 O4)
FORMUL 10 HOH *662(H2 O)
HELIX 1 1 MET A 27 SER A 31 5 5
HELIX 2 2 SER A 48 GLU A 51 5 4
HELIX 3 3 ALA A 52 LYS A 62 1 11
HELIX 4 4 VAL A 73 ALA A 77 5 5
HELIX 5 5 PRO A 80 ASN A 96 1 17
HELIX 6 6 SER A 113 GLY A 126 1 14
HELIX 7 7 LEU A 174 ALA A 187 1 14
HELIX 8 8 ASN A 207 SER A 211 5 5
HELIX 9 9 LEU A 214 ILE A 218 5 5
HELIX 10 10 VAL A 224 LEU A 237 1 14
HELIX 11 11 SER B 24 SER B 31 5 8
HELIX 12 12 SER B 48 GLU B 51 5 4
HELIX 13 13 ALA B 52 LYS B 62 1 11
HELIX 14 14 VAL B 73 ALA B 77 5 5
HELIX 15 15 PRO B 80 ASN B 96 1 17
HELIX 16 16 ASN B 96 HIS B 101 1 6
HELIX 17 17 SER B 113 GLY B 126 1 14
HELIX 18 18 LEU B 174 ALA B 187 1 14
HELIX 19 19 ASN B 207 SER B 211 5 5
HELIX 20 20 LEU B 214 ILE B 218 5 5
HELIX 21 21 VAL B 224 LEU B 237 1 14
SHEET 1 A 8 ASN A 2 ILE A 6 0
SHEET 2 A 8 THR A 15 VAL A 20 -1 O CYS A 18 N SER A 4
SHEET 3 A 8 ASN A 65 ARG A 70 -1 O ALA A 66 N TYR A 19
SHEET 4 A 8 ARG A 33 PHE A 39 1 N ILE A 38 O PHE A 67
SHEET 5 A 8 ILE A 102 PHE A 112 1 O ILE A 110 N PHE A 39
SHEET 6 A 8 ALA A 132 GLY A 136 1 O VAL A 134 N VAL A 109
SHEET 7 A 8 MET A 161 THR A 166 1 O PHE A 162 N LEU A 135
SHEET 8 A 8 VAL A 191 PHE A 196 1 O HIS A 194 N VAL A 163
SHEET 1 B 8 ASN B 2 ILE B 6 0
SHEET 2 B 8 THR B 15 VAL B 20 -1 O CYS B 18 N SER B 4
SHEET 3 B 8 ASN B 65 ARG B 70 -1 O ALA B 66 N TYR B 19
SHEET 4 B 8 ARG B 33 PHE B 39 1 N ILE B 38 O PHE B 67
SHEET 5 B 8 ILE B 102 PHE B 112 1 O ALA B 108 N LEU B 37
SHEET 6 B 8 ALA B 132 GLY B 136 1 O VAL B 134 N VAL B 109
SHEET 7 B 8 MET B 161 THR B 166 1 O PHE B 162 N LEU B 135
SHEET 8 B 8 VAL B 191 PHE B 196 1 O HIS B 194 N VAL B 163
CISPEP 1 PHE A 79 PRO A 80 0 11.71
CISPEP 2 PHE B 79 PRO B 80 0 11.67
SITE 1 AC1 2 ASP A 170 HIS A 201
SITE 1 AC2 4 GLY A 42 GLY A 43 SER A 113 ALA A 114
SITE 1 AC3 3 TYR A 146 ASP A 170 LEU A 171
SITE 1 AC4 3 ASP B 170 LEU B 171 HIS B 201
SITE 1 AC5 4 GLY B 42 GLY B 43 SER B 113 ALA B 114
SITE 1 AC6 1 LEU B 171
SITE 1 AC7 7 GLY B 43 TYR B 44 GLN B 45 LYS B 74
SITE 2 AC7 7 ALA B 77 PHE B 149 HOH B 686
CRYST1 78.991 82.716 77.377 90.00 109.32 90.00 C 1 2 1 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 0.012660 0.000000 0.004438 0.00000
SCALE2 0.000000 0.012090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013695 0.00000
TER 1958 LEU A 239
TER 3919 LEU B 239
MASTER 437 0 7 21 16 0 8 6 4515 2 30 40
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