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HEADER HYDROLASE 04-AUG-20 7COF
TITLE CHOLESTEROL ESTERASE FROM BURKHOLDERIA STABILIS (ORTHORHOMBIC CRYSTAL
TITLE 2 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHOLESTEROL ESTERASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA STABILIS;
SOURCE 3 ORGANISM_TAXID: 95485
KEYWDS CHOLESTEROL ESTERASE, LIPASE, BURKHOLDERIA STABILIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YASUTAKE,T.TAMURA
REVDAT 1 16-DEC-20 7COF 0
JRNL AUTH Y.YASUTAKE,K.KONISHI,S.MURAMATSU,K.YOSHIDA,S.ABURATANI,
JRNL AUTH 2 S.I.SAKASEGAWA,T.TAMURA
JRNL TITL BACTERIAL TRIACYLGLYCEROL LIPASE IS A POTENTIAL CHOLESTEROL
JRNL TITL 2 ESTERASE: IDENTIFICATION OF A KEY DETERMINANT FOR
JRNL TITL 3 STEROL-BINDING SPECIFICITY.
JRNL REF INT.J.BIOL.MACROMOL. V. 167 578 2021
JRNL REFN ISSN 0141-8130
JRNL DOI 10.1016/J.IJBIOMAC.2020.11.184
REMARK 2
REMARK 2 RESOLUTION. 1.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 103377
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.099
REMARK 3 R VALUE (WORKING SET) : 0.098
REMARK 3 FREE R VALUE : 0.118
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5062
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 32.0120 - 3.3675 1.00 3752 206 0.1561 0.1678
REMARK 3 2 3.3675 - 2.6733 1.00 3616 175 0.1212 0.1320
REMARK 3 3 2.6733 - 2.3355 0.99 3589 175 0.1021 0.1212
REMARK 3 4 2.3355 - 2.1220 1.00 3550 195 0.0935 0.1085
REMARK 3 5 2.1220 - 1.9699 1.00 3591 176 0.0901 0.1054
REMARK 3 6 1.9699 - 1.8538 1.00 3528 185 0.0856 0.1065
REMARK 3 7 1.8538 - 1.7610 1.00 3553 167 0.0837 0.1069
REMARK 3 8 1.7610 - 1.6843 1.00 3573 164 0.0768 0.1033
REMARK 3 9 1.6843 - 1.6195 1.00 3513 180 0.0744 0.0975
REMARK 3 10 1.6195 - 1.5636 1.00 3526 186 0.0728 0.0920
REMARK 3 11 1.5636 - 1.5147 1.00 3561 170 0.0678 0.0909
REMARK 3 12 1.5147 - 1.4714 1.00 3521 191 0.0698 0.0975
REMARK 3 13 1.4714 - 1.4327 1.00 3518 185 0.0748 0.0979
REMARK 3 14 1.4327 - 1.3977 1.00 3488 208 0.0730 0.1067
REMARK 3 15 1.3977 - 1.3659 1.00 3502 157 0.0777 0.1024
REMARK 3 16 1.3659 - 1.3369 1.00 3567 166 0.0818 0.0987
REMARK 3 17 1.3369 - 1.3101 1.00 3522 171 0.0780 0.0968
REMARK 3 18 1.3101 - 1.2854 1.00 3467 174 0.0801 0.1261
REMARK 3 19 1.2854 - 1.2624 0.99 3534 199 0.0805 0.1136
REMARK 3 20 1.2624 - 1.2410 1.00 3449 185 0.0816 0.1029
REMARK 3 21 1.2410 - 1.2210 1.00 3501 202 0.0812 0.0993
REMARK 3 22 1.2210 - 1.2022 1.00 3501 172 0.0810 0.1081
REMARK 3 23 1.2022 - 1.1846 1.00 3506 177 0.0853 0.1037
REMARK 3 24 1.1846 - 1.1679 0.95 3306 192 0.0884 0.1217
REMARK 3 25 1.1679 - 1.1521 0.87 3041 160 0.0937 0.1265
REMARK 3 26 1.1521 - 1.1371 0.79 2749 150 0.0967 0.1009
REMARK 3 27 1.1371 - 1.1229 0.70 2452 137 0.1120 0.1323
REMARK 3 28 1.1229 - 1.1094 0.64 2246 100 0.1188 0.1356
REMARK 3 29 1.1094 - 1.0965 0.55 1923 95 0.1406 0.1541
REMARK 3 30 1.0965 - 1.0842 0.34 1170 62 0.1656 0.2093
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) : 0.050
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 8.180
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 : 0.011 2500
REMARK 3 ANGLE : 1.314 3435
REMARK 3 CHIRALITY : 0.375 404
REMARK 3 PLANARITY : 0.010 448
REMARK 3 DIHEDRAL : 14.551 877
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 7COF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1300017961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103889
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 6.020
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
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 : 7.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1YS1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE, PEG2250, 2-PROPANOL, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 73.58850
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 73.58850
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 29.12050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.68250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.12050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.68250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.58850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.12050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 30.68250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.58850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.12050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 30.68250
REMARK 290 SMTRY3 8 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 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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 585 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 785 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 309 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
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 THR A 18 -13.56 76.64
REMARK 500 SER A 87 -134.80 61.15
REMARK 500 THR A 217 -106.79 -120.05
REMARK 500 LEU A 234 -54.83 74.50
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 242 OD2
REMARK 620 2 ASP A 288 OD1 165.9
REMARK 620 3 GLN A 292 O 88.8 99.7
REMARK 620 4 VAL A 296 O 93.3 98.6 85.1
REMARK 620 5 HOH A 536 O 82.1 86.3 91.9 174.6
REMARK 620 6 HOH A 566 O 88.9 82.5 177.6 95.6 87.2
REMARK 620 N 1 2 3 4 5
DBREF1 7COF A 1 320 UNP A0A1Y1BQV9_9BURK
DBREF2 7COF A A0A1Y1BQV9 45 364
SEQRES 1 A 320 ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU
SEQRES 2 A 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 A 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 A 320 HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 A 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 A 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 A 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 A 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 A 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 A 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 A 320 PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL
SEQRES 12 A 320 ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR
SEQRES 13 A 320 ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR
SEQRES 14 A 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 A 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 A 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 A 320 TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE
SEQRES 18 A 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 A 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 A 320 LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER
SEQRES 21 A 320 GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU
SEQRES 22 A 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 A 320 ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 A 320 PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 A 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA A 401 1
HET GOL A 402 12
HET GOL A 403 12
HET IMD A 404 10
HET IPA A 405 12
HET IPA A 406 12
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM IMD IMIDAZOLE
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IPA 2-PROPANOL
FORMUL 2 CA CA 2+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 IMD C3 H5 N2 1+
FORMUL 6 IPA 2(C3 H8 O)
FORMUL 8 HOH *309(H2 O)
HELIX 1 AA1 ALA A 24 VAL A 26 5 3
HELIX 2 AA2 GLY A 32 HIS A 40 1 9
HELIX 3 AA3 GLY A 60 GLY A 77 1 18
HELIX 4 AA4 SER A 87 ALA A 100 1 14
HELIX 5 AA5 SER A 117 TYR A 129 1 13
HELIX 6 AA6 GLY A 133 SER A 151 1 19
HELIX 7 AA7 ASP A 159 THR A 168 1 10
HELIX 8 AA8 THR A 168 TYR A 179 1 12
HELIX 9 AA9 ASP A 236 ASP A 242 1 7
HELIX 10 AB1 PRO A 243 ARG A 258 1 16
HELIX 11 AB2 SER A 268 LEU A 273 1 6
HELIX 12 AB3 ILE A 287 ASN A 291 5 5
HELIX 13 AB4 ASP A 303 ALA A 318 1 16
SHEET 1 AA1 6 VAL A 44 VAL A 46 0
SHEET 2 AA1 6 ILE A 11 VAL A 14 1 N LEU A 13 O TYR A 45
SHEET 3 AA1 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 14
SHEET 4 AA1 6 VAL A 104 ILE A 110 1 O ALA A 105 N VAL A 81
SHEET 5 AA1 6 ASN A 202 GLY A 211 1 O LEU A 205 N VAL A 107
SHEET 6 AA1 6 THR A 196 VAL A 199 -1 N GLU A 197 O HIS A 204
SHEET 1 AA2 6 VAL A 44 VAL A 46 0
SHEET 2 AA2 6 ILE A 11 VAL A 14 1 N LEU A 13 O TYR A 45
SHEET 3 AA2 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 14
SHEET 4 AA2 6 VAL A 104 ILE A 110 1 O ALA A 105 N VAL A 81
SHEET 5 AA2 6 ASN A 202 GLY A 211 1 O LEU A 205 N VAL A 107
SHEET 6 AA2 6 GLN A 276 TYR A 282 1 O LEU A 278 N SER A 208
SHEET 1 AA3 2 LYS A 22 TYR A 23 0
SHEET 2 AA3 2 LEU A 27 GLU A 28 -1 O LEU A 27 N TYR A 23
SHEET 1 AA4 2 ILE A 214 VAL A 220 0
SHEET 2 AA4 2 VAL A 223 ASP A 228 -1 O GLY A 225 N LEU A 218
SSBOND 1 CYS A 190 CYS A 270 1555 1555 2.03
LINK OD2 ASP A 242 CA CA A 401 1555 1555 2.31
LINK OD1 ASP A 288 CA CA A 401 1555 1555 2.28
LINK O GLN A 292 CA CA A 401 1555 1555 2.37
LINK O VAL A 296 CA CA A 401 1555 1555 2.32
LINK CA CA A 401 O HOH A 536 1555 1555 2.32
LINK CA CA A 401 O HOH A 566 1555 1555 2.38
CISPEP 1 GLN A 292 LEU A 293 0 -9.78
CRYST1 58.241 61.365 147.177 90.00 90.00 90.00 C 2 2 21 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 0.017170 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006795 0.00000
TER 4620 VAL A 320
MASTER 302 0 6 13 16 0 0 6 2680 1 68 25
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