| 7cog-pdb | HEADER HYDROLASE 04-AUG-20 7COG
TITLE CHOLESTEROL ESTERASE FROM BURKHOLDERIA STABILIS (MONOCLINIC CRYSTAL
TITLE 2 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CHOLESTEROL ESTERASE;
COMPND 5 OTHER_DETAILS: WP_096474789.1
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 7COG 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. 2.10 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 71684
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 3554
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 29.9501 - 5.6866 0.95 3583 168 0.2210 0.2517
REMARK 3 2 5.6866 - 4.5186 0.94 3473 188 0.1991 0.1993
REMARK 3 3 4.5186 - 3.9489 0.94 3382 193 0.1943 0.2035
REMARK 3 4 3.9489 - 3.5885 0.95 3434 182 0.2127 0.2813
REMARK 3 5 3.5885 - 3.3316 0.94 3378 209 0.2302 0.2735
REMARK 3 6 3.3316 - 3.1354 0.95 3395 182 0.2335 0.2826
REMARK 3 7 3.1354 - 2.9786 0.95 3422 183 0.2357 0.2572
REMARK 3 8 2.9786 - 2.8490 0.95 3407 180 0.2349 0.2545
REMARK 3 9 2.8490 - 2.7394 0.96 3413 156 0.2373 0.2460
REMARK 3 10 2.7394 - 2.6449 0.95 3373 189 0.2431 0.2646
REMARK 3 11 2.6449 - 2.5623 0.95 3394 177 0.2447 0.3018
REMARK 3 12 2.5623 - 2.4891 0.95 3353 168 0.2457 0.2726
REMARK 3 13 2.4891 - 2.4236 0.95 3410 192 0.2624 0.2925
REMARK 3 14 2.4236 - 2.3645 0.96 3423 149 0.2695 0.2589
REMARK 3 15 2.3645 - 2.3107 0.95 3395 177 0.2759 0.2751
REMARK 3 16 2.3107 - 2.2616 0.95 3345 171 0.2768 0.3099
REMARK 3 17 2.2616 - 2.2164 0.94 3379 188 0.2866 0.2915
REMARK 3 18 2.2164 - 2.1745 0.95 3390 165 0.2958 0.3593
REMARK 3 19 2.1745 - 2.1357 0.94 3329 174 0.2959 0.3327
REMARK 3 20 2.1357 - 2.0995 0.94 3413 150 0.2939 0.2942
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.520
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 : 0.002 9576
REMARK 3 ANGLE : 0.499 13120
REMARK 3 CHIRALITY : 0.040 1560
REMARK 3 PLANARITY : 0.003 1708
REMARK 3 DIHEDRAL : 9.253 5536
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 7COG 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_1300017935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.098
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.360
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 2.310
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: 1YS1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PEG4000, 2-PROPANOL,
REMARK 280 PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.54600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 13000 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 350
REMARK 350 BIOMOLECULE: 2
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: 13070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
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: 13430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
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: 12910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 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 ASP A 2 -163.47 -160.48
REMARK 500 THR A 18 -0.98 63.59
REMARK 500 SER A 87 -126.00 60.26
REMARK 500 SER A 219 118.41 -173.72
REMARK 500 PHE A 221 -4.62 73.17
REMARK 500 LEU A 234 -39.13 69.55
REMARK 500 LEU A 266 -20.68 -141.35
REMARK 500 ASP B 2 -158.03 -98.03
REMARK 500 ALA B 5 24.02 -140.03
REMARK 500 THR B 18 -15.92 63.44
REMARK 500 TYR B 23 -98.39 -31.99
REMARK 500 ALA B 24 -169.47 -77.23
REMARK 500 VAL B 26 -26.81 142.99
REMARK 500 ASP B 56 -167.40 -113.61
REMARK 500 SER B 87 -133.78 60.49
REMARK 500 THR B 150 41.28 -102.29
REMARK 500 ASP B 159 91.69 -161.62
REMARK 500 THR B 217 -55.78 -120.89
REMARK 500 LEU B 234 -45.80 74.28
REMARK 500 SER B 279 145.29 -174.43
REMARK 500 SER C 87 -131.62 59.80
REMARK 500 THR C 217 -105.73 -114.62
REMARK 500 LEU C 234 -53.13 70.20
REMARK 500 VAL D 26 -67.06 -121.04
REMARK 500 SER D 87 -132.73 59.83
REMARK 500 THR D 217 -91.06 -123.05
REMARK 500 LEU D 218 -160.50 -124.58
REMARK 500 PHE D 221 -127.65 62.12
REMARK 500 LEU D 234 -38.47 74.85
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 167.7
REMARK 620 3 GLN A 292 O 87.5 93.7
REMARK 620 4 VAL A 296 O 92.3 100.0 85.2
REMARK 620 5 HOH A 518 O 73.1 94.6 90.9 165.0
REMARK 620 6 HOH A 520 O 93.0 85.9 179.2 94.2 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 242 OD2
REMARK 620 2 ASP B 288 OD1 172.9
REMARK 620 3 GLN B 292 O 82.8 92.2
REMARK 620 4 VAL B 296 O 82.9 91.2 78.1
REMARK 620 5 HOH B 506 O 98.9 85.4 172.4 94.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 242 OD2
REMARK 620 2 ASP C 288 OD1 159.9
REMARK 620 3 GLN C 292 O 95.4 94.3
REMARK 620 4 VAL C 296 O 101.4 95.9 91.7
REMARK 620 5 HOH C 508 O 74.0 88.6 89.1 175.3
REMARK 620 6 HOH C 511 O 85.4 81.5 167.7 100.2 79.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 242 OD2
REMARK 620 2 ASP D 288 OD1 179.2
REMARK 620 3 GLN D 292 O 90.8 88.4
REMARK 620 4 VAL D 296 O 87.0 93.0 80.4
REMARK 620 5 HOH D 504 O 93.2 86.6 84.4 164.9
REMARK 620 6 HOH D 516 O 107.0 73.8 162.2 99.9 94.5
REMARK 620 N 1 2 3 4 5
DBREF1 7COG A 1 320 UNP A0A1Y1BQV9_9BURK
DBREF2 7COG A A0A1Y1BQV9 45 364
DBREF1 7COG B 1 320 UNP A0A1Y1BQV9_9BURK
DBREF2 7COG B A0A1Y1BQV9 45 364
DBREF1 7COG C 1 320 UNP A0A1Y1BQV9_9BURK
DBREF2 7COG C A0A1Y1BQV9 45 364
DBREF1 7COG D 1 320 UNP A0A1Y1BQV9_9BURK
DBREF2 7COG D 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
SEQRES 1 B 320 ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU
SEQRES 2 B 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 B 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 B 320 HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 B 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 B 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 B 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 B 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 B 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 B 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 B 320 PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL
SEQRES 12 B 320 ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR
SEQRES 13 B 320 ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR
SEQRES 14 B 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 B 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 B 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 B 320 TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE
SEQRES 18 B 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 B 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 B 320 LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER
SEQRES 21 B 320 GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU
SEQRES 22 B 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 B 320 ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 B 320 PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 B 320 ASN ARG LEU LYS LEU ALA GLY VAL
SEQRES 1 C 320 ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU
SEQRES 2 C 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 C 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 C 320 HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 C 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 C 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 C 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 C 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 C 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 C 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 C 320 PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL
SEQRES 12 C 320 ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR
SEQRES 13 C 320 ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR
SEQRES 14 C 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 C 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 C 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 C 320 TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE
SEQRES 18 C 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 C 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 C 320 LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER
SEQRES 21 C 320 GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU
SEQRES 22 C 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 C 320 ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 C 320 PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 C 320 ASN ARG LEU LYS LEU ALA GLY VAL
SEQRES 1 D 320 ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU
SEQRES 2 D 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 D 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 D 320 HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 D 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 D 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 D 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 D 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 D 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 D 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 D 320 PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL
SEQRES 12 D 320 ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR
SEQRES 13 D 320 ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR
SEQRES 14 D 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 D 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 D 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 D 320 TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE
SEQRES 18 D 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 D 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 D 320 LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER
SEQRES 21 D 320 GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU
SEQRES 22 D 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 D 320 ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 D 320 PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 D 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA A 401 1
HET CA B 401 1
HET CA C 401 1
HET CA D 401 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *88(H2 O)
HELIX 1 AA1 ALA A 24 VAL A 26 5 3
HELIX 2 AA2 GLY A 32 GLN A 39 1 8
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 ALA A 128 1 12
HELIX 6 AA6 GLY A 133 SER A 151 1 19
HELIX 7 AA7 ASP A 159 LEU A 167 1 9
HELIX 8 AA8 THR A 168 TYR A 179 1 12
HELIX 9 AA9 PRO A 237 ASP A 242 1 6
HELIX 10 AB1 PRO A 243 ASN A 257 1 15
HELIX 11 AB2 LYS A 269 LEU A 273 5 5
HELIX 12 AB3 ILE A 287 ASN A 291 5 5
HELIX 13 AB4 ASP A 303 GLY A 319 1 17
HELIX 14 AB5 GLY B 32 HIS B 40 1 9
HELIX 15 AB6 GLY B 60 GLY B 77 1 18
HELIX 16 AB7 SER B 87 ALA B 100 1 14
HELIX 17 AB8 SER B 117 LEU B 127 1 11
HELIX 18 AB9 ALA B 128 ASP B 130 5 3
HELIX 19 AC1 GLY B 133 THR B 150 1 18
HELIX 20 AC2 ASP B 159 LEU B 167 1 9
HELIX 21 AC3 THR B 168 TYR B 179 1 12
HELIX 22 AC4 PRO B 237 ASP B 242 1 6
HELIX 23 AC5 ASP B 242 ARG B 258 1 17
HELIX 24 AC6 ASP B 303 GLY B 319 1 17
HELIX 25 AC7 GLY C 32 HIS C 40 1 9
HELIX 26 AC8 GLY C 60 GLY C 77 1 18
HELIX 27 AC9 GLN C 88 ALA C 100 1 13
HELIX 28 AD1 SER C 117 TYR C 129 1 13
HELIX 29 AD2 GLY C 133 THR C 150 1 18
HELIX 30 AD3 ASP C 159 LEU C 167 1 9
HELIX 31 AD4 THR C 168 TYR C 179 1 12
HELIX 32 AD5 PRO C 237 ASP C 242 1 6
HELIX 33 AD6 PRO C 243 ASN C 257 1 15
HELIX 34 AD7 ILE C 287 ASN C 291 5 5
HELIX 35 AD8 ASP C 303 GLY C 319 1 17
HELIX 36 AD9 ALA D 24 VAL D 26 5 3
HELIX 37 AE1 GLY D 32 HIS D 40 1 9
HELIX 38 AE2 GLY D 60 GLY D 77 1 18
HELIX 39 AE3 GLN D 88 ALA D 100 1 13
HELIX 40 AE4 SER D 117 ALA D 128 1 12
HELIX 41 AE5 GLY D 133 THR D 150 1 18
HELIX 42 AE6 ASP D 159 LEU D 167 1 9
HELIX 43 AE7 THR D 168 TYR D 179 1 12
HELIX 44 AE8 PRO D 237 ASP D 242 1 6
HELIX 45 AE9 PRO D 243 ASN D 257 1 15
HELIX 46 AF1 SER D 268 LEU D 273 1 6
HELIX 47 AF2 HIS D 286 ASN D 291 5 6
HELIX 48 AF3 ASP D 303 GLY D 319 1 17
SHEET 1 AA1 6 VAL A 44 VAL A 46 0
SHEET 2 AA1 6 ILE A 11 VAL A 14 1 N ILE A 11 O TYR A 45
SHEET 3 AA1 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 12
SHEET 4 AA1 6 VAL A 104 ILE A 110 1 O THR A 108 N GLY A 85
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 ILE A 11 O TYR A 45
SHEET 3 AA2 6 VAL A 81 HIS A 86 1 O VAL A 84 N VAL A 12
SHEET 4 AA2 6 VAL A 104 ILE A 110 1 O THR A 108 N GLY A 85
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 THR A 217 0
SHEET 2 AA4 2 GLY A 225 ASP A 228 -1 O THR A 227 N GLN A 215
SHEET 1 AA5 6 VAL B 44 VAL B 46 0
SHEET 2 AA5 6 ILE B 11 VAL B 14 1 N ILE B 11 O TYR B 45
SHEET 3 AA5 6 VAL B 81 HIS B 86 1 O VAL B 84 N VAL B 14
SHEET 4 AA5 6 VAL B 104 ILE B 110 1 O ILE B 110 N GLY B 85
SHEET 5 AA5 6 ASN B 202 TRP B 209 1 O TYR B 207 N VAL B 107
SHEET 6 AA5 6 THR B 196 VAL B 199 -1 N GLU B 197 O HIS B 204
SHEET 1 AA6 6 VAL B 44 VAL B 46 0
SHEET 2 AA6 6 ILE B 11 VAL B 14 1 N ILE B 11 O TYR B 45
SHEET 3 AA6 6 VAL B 81 HIS B 86 1 O VAL B 84 N VAL B 14
SHEET 4 AA6 6 VAL B 104 ILE B 110 1 O ILE B 110 N GLY B 85
SHEET 5 AA6 6 ASN B 202 TRP B 209 1 O TYR B 207 N VAL B 107
SHEET 6 AA6 6 GLN B 276 SER B 279 1 O LEU B 278 N SER B 208
SHEET 1 AA7 2 ILE B 214 VAL B 220 0
SHEET 2 AA7 2 VAL B 223 ASP B 228 -1 O GLY B 225 N LEU B 218
SHEET 1 AA8 6 VAL C 44 VAL C 46 0
SHEET 2 AA8 6 ILE C 11 VAL C 14 1 N ILE C 11 O TYR C 45
SHEET 3 AA8 6 VAL C 81 HIS C 86 1 O VAL C 84 N VAL C 14
SHEET 4 AA8 6 VAL C 104 ILE C 110 1 O THR C 108 N LEU C 83
SHEET 5 AA8 6 ASN C 202 GLY C 211 1 O LEU C 205 N VAL C 107
SHEET 6 AA8 6 THR C 196 VAL C 199 -1 N GLU C 197 O HIS C 204
SHEET 1 AA9 6 VAL C 44 VAL C 46 0
SHEET 2 AA9 6 ILE C 11 VAL C 14 1 N ILE C 11 O TYR C 45
SHEET 3 AA9 6 VAL C 81 HIS C 86 1 O VAL C 84 N VAL C 14
SHEET 4 AA9 6 VAL C 104 ILE C 110 1 O THR C 108 N LEU C 83
SHEET 5 AA9 6 ASN C 202 GLY C 211 1 O LEU C 205 N VAL C 107
SHEET 6 AA9 6 GLN C 276 TYR C 282 1 O LEU C 278 N SER C 208
SHEET 1 AB1 2 ILE C 214 VAL C 220 0
SHEET 2 AB1 2 VAL C 223 ASP C 228 -1 O GLY C 225 N THR C 217
SHEET 1 AB2 6 VAL D 44 VAL D 46 0
SHEET 2 AB2 6 ILE D 11 VAL D 14 1 N ILE D 11 O TYR D 45
SHEET 3 AB2 6 VAL D 81 HIS D 86 1 O VAL D 84 N VAL D 14
SHEET 4 AB2 6 VAL D 104 ILE D 110 1 O THR D 108 N GLY D 85
SHEET 5 AB2 6 ASN D 202 GLY D 211 1 O LEU D 205 N VAL D 107
SHEET 6 AB2 6 THR D 196 VAL D 199 -1 N GLU D 197 O HIS D 204
SHEET 1 AB3 6 VAL D 44 VAL D 46 0
SHEET 2 AB3 6 ILE D 11 VAL D 14 1 N ILE D 11 O TYR D 45
SHEET 3 AB3 6 VAL D 81 HIS D 86 1 O VAL D 84 N VAL D 14
SHEET 4 AB3 6 VAL D 104 ILE D 110 1 O THR D 108 N GLY D 85
SHEET 5 AB3 6 ASN D 202 GLY D 211 1 O LEU D 205 N VAL D 107
SHEET 6 AB3 6 GLN D 276 TYR D 282 1 O GLN D 276 N LEU D 206
SHEET 1 AB4 2 LYS D 22 TYR D 23 0
SHEET 2 AB4 2 LEU D 27 GLU D 28 -1 O LEU D 27 N TYR D 23
SHEET 1 AB5 2 ILE D 214 VAL D 220 0
SHEET 2 AB5 2 VAL D 223 ASP D 228 -1 O THR D 227 N GLN D 215
SSBOND 1 CYS A 190 CYS A 270 1555 1555 2.03
SSBOND 2 CYS B 190 CYS B 270 1555 1555 2.03
SSBOND 3 CYS C 190 CYS C 270 1555 1555 2.04
SSBOND 4 CYS D 190 CYS D 270 1555 1555 2.03
LINK OD2 ASP A 242 CA CA A 401 1555 1555 2.39
LINK OD1 ASP A 288 CA CA A 401 1555 1555 2.36
LINK O GLN A 292 CA CA A 401 1555 1555 2.53
LINK O VAL A 296 CA CA A 401 1555 1555 2.45
LINK CA CA A 401 O HOH A 518 1555 1555 2.43
LINK CA CA A 401 O HOH A 520 1555 1555 2.45
LINK OD2 ASP B 242 CA CA B 401 1555 1555 2.44
LINK OD1 ASP B 288 CA CA B 401 1555 1555 2.37
LINK O GLN B 292 CA CA B 401 1555 1555 2.66
LINK O VAL B 296 CA CA B 401 1555 1555 2.48
LINK CA CA B 401 O HOH B 506 1555 1555 2.70
LINK OD2 ASP C 242 CA CA C 401 1555 1555 2.41
LINK OD1 ASP C 288 CA CA C 401 1555 1555 2.28
LINK O GLN C 292 CA CA C 401 1555 1555 2.39
LINK O VAL C 296 CA CA C 401 1555 1555 2.35
LINK CA CA C 401 O HOH C 508 1555 1555 2.41
LINK CA CA C 401 O HOH C 511 1555 1555 2.57
LINK OD2 ASP D 242 CA CA D 401 1555 1555 2.36
LINK OD1 ASP D 288 CA CA D 401 1555 1555 2.34
LINK O GLN D 292 CA CA D 401 1555 1555 2.61
LINK O VAL D 296 CA CA D 401 1555 1555 2.45
LINK CA CA D 401 O HOH D 504 1555 1555 2.50
LINK CA CA D 401 O HOH D 516 1555 1555 2.51
CISPEP 1 GLN A 292 LEU A 293 0 1.28
CISPEP 2 GLN B 292 LEU B 293 0 1.30
CISPEP 3 GLN C 292 LEU C 293 0 0.38
CISPEP 4 GLN D 292 LEU D 293 0 2.03
CRYST1 186.292 47.092 70.082 90.00 90.05 90.00 P 1 21 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 0.005368 0.000000 0.000005 0.00000
SCALE2 0.000000 0.021235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014269 0.00000
TER 2346 VAL A 320
TER 4692 VAL B 320
TER 7038 VAL C 320
TER 9384 VAL D 320
MASTER 332 0 4 48 60 0 0 6 9472 4 39 100
END
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