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HEADER HYDROLASE 11-FEB-19 6NY9
TITLE ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN 10 FROM MOUSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYCOPHENOLIC ACID ACYL-GLUCURONIDE ESTERASE, MITOCHONDRIAL;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN 10,
COMPND 5 ABHYDROLASE DOMAIN-CONTAINING PROTEIN 10;
COMPND 6 EC: 3.1.1.93;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ABHD10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS ALPHA/BETA HYDROLASE, DEPALMITOYLASE, MITOCHONDRIA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.CAO,P.A.RICE,B.C.DICKINSON
REVDAT 1 22-JAN-20 6NY9 0
JRNL AUTH Y.CAO,Q.TIAN,R.S.KATHAYAT,S.A.AZIZI,P.A.RICE,B.C.DICKINSON
JRNL TITL ABHD10 REGULATES MITOCHONDRIAL REDOX HOMEOSTASIS THROUGH
JRNL TITL 2 S-DEPALMITOYLATION OF PRDX5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 48620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1879
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 74.6800 - 3.9000 1.00 4209 167 0.1894 0.2316
REMARK 3 2 3.9000 - 3.0900 1.00 3951 158 0.1639 0.1911
REMARK 3 3 3.0900 - 2.7000 1.00 3917 157 0.1780 0.1782
REMARK 3 4 2.7000 - 2.4600 0.99 3848 154 0.1818 0.2005
REMARK 3 5 2.4600 - 2.2800 0.99 3817 154 0.1841 0.1848
REMARK 3 6 2.2800 - 2.1400 0.97 3721 148 0.1937 0.1942
REMARK 3 7 2.1400 - 2.0400 0.97 3747 149 0.1979 0.2316
REMARK 3 8 2.0400 - 1.9500 0.95 3607 145 0.2048 0.2306
REMARK 3 9 1.9500 - 1.8700 0.92 3499 147 0.2338 0.2777
REMARK 3 10 1.8700 - 1.8100 0.89 3395 138 0.2377 0.2717
REMARK 3 11 1.8100 - 1.7500 0.82 3098 122 0.2809 0.2531
REMARK 3 12 1.7500 - 1.7000 0.80 3052 122 0.2947 0.3514
REMARK 3 13 1.7000 - 1.6600 0.76 2880 118 0.3090 0.3534
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.192
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.014
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.19
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 2004
REMARK 3 ANGLE : 1.034 2714
REMARK 3 CHIRALITY : 0.058 307
REMARK 3 PLANARITY : 0.007 343
REMARK 3 DIHEDRAL : 12.507 1209
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4151 -34.2370 17.0272
REMARK 3 T TENSOR
REMARK 3 T11: 0.0840 T22: 0.1670
REMARK 3 T33: 0.1172 T12: -0.0177
REMARK 3 T13: 0.0195 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.2537 L22: 1.4300
REMARK 3 L33: 1.8217 L12: 0.1177
REMARK 3 L13: 0.6179 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: -0.1173 S13: 0.0371
REMARK 3 S21: 0.0557 S22: 0.0152 S23: 0.1586
REMARK 3 S31: 0.0068 S32: -0.2702 S33: 0.0243
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 6NY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239636.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52270
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.657
REMARK 200 RESOLUTION RANGE LOW (A) : 56.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.10820
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.13-2998
REMARK 200 STARTING MODEL: 3LLC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08 M STRONTIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.04 M SODIUM CACODYLATE TRIHYDRATE PH 6.4, 25% V/V (+/-)-2-
REMARK 280 METHYL-2,4-PENTANEDIOL (MPD), 0.012 M SPERMINE
REMARK 280 TETRAHYDROCHLORIDE, LIQUID DIFFUSION, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
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 74.79850
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 74.79850
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 74.79850
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 0.00000
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 0.00000
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 74.79850
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 74.79850
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 74.79850
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -189.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 49.69400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -86.07253
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 99.38800
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 SR SR B 305 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 405 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 600 LIES ON A SPECIAL POSITION.
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 B 100 -116.95 56.59
REMARK 500 ALA B 126 51.64 -97.66
REMARK 500 PHE B 163 -48.80 -133.78
REMARK 500 ASP B 226 -168.65 -105.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 605 DISTANCE = 5.95 ANGSTROMS
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 SR B 302 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 7 OD1
REMARK 620 2 ARG B 8 O 97.5
REMARK 620 3 HOH B 410 O 131.5 67.8
REMARK 620 4 HOH B 567 O 109.7 135.1 67.4
REMARK 620 5 HOH B 540 O 154.3 76.7 70.1 90.9
REMARK 620 6 HOH B 542 O 81.1 143.9 137.8 77.1 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR B 303 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 429 O
REMARK 620 2 HOH B 451 O 77.7
REMARK 620 3 HOH B 518 O 67.6 70.5
REMARK 620 4 HOH B 429 O 84.0 139.2 133.9
REMARK 620 5 HOH B 403 O 94.5 75.5 144.1 70.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SR B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SR B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SR B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SR B 305
DBREF 6NY9 B 1 250 UNP Q6PE15 ABHDA_MOUSE 44 293
SEQRES 1 B 250 ALA SER LEU SER PHE LEU ASN ARG SER GLU LEU PRO ASN
SEQRES 2 B 250 LEU ALA TYR LYS ARG LEU LYS GLY LYS THR PRO GLY ILE
SEQRES 3 B 250 ILE PHE ILE PRO GLY TYR LEU SER ASN MET ASN GLY ILE
SEQRES 4 B 250 LYS ALA VAL ALA VAL GLU GLU PHE CYS LYS SER LEU GLY
SEQRES 5 B 250 HIS ALA PHE ILE ARG PHE ASP TYR SER GLY ILE GLY SER
SEQRES 6 B 250 SER ASP GLY ASN LEU ALA GLU CYS THR VAL GLY LYS TRP
SEQRES 7 B 250 ARG LYS ASP VAL LEU SER ILE LEU ASP ASP VAL ALA GLU
SEQRES 8 B 250 GLY PRO GLN ILE LEU VAL GLY SER SER LEU GLY GLY TRP
SEQRES 9 B 250 LEU MET LEU HIS ALA ALA ILE ALA ARG PRO GLU LYS VAL
SEQRES 10 B 250 ILE ALA LEU ILE GLY ILE ALA THR ALA ALA ASP GLY LEU
SEQRES 11 B 250 VAL THR GLN TYR HIS ALA LEU PRO VAL GLU THR GLN LYS
SEQRES 12 B 250 GLU ILE GLU MET LYS GLY GLU TRP THR LEU PRO SER ARG
SEQRES 13 B 250 TYR ASN LYS GLU GLY TYR PHE ARG ILE PRO TYR SER PHE
SEQRES 14 B 250 ILE LYS GLU ALA GLU HIS HIS CYS LEU LEU HIS SER PRO
SEQRES 15 B 250 ILE PRO VAL THR CYS PRO VAL ARG LEU LEU HIS GLY MET
SEQRES 16 B 250 LYS ASP GLU ILE VAL PRO TRP GLN ARG SER LEU GLN VAL
SEQRES 17 B 250 ALA ASP ARG ILE VAL SER PRO ASP VAL ASP VAL ILE LEU
SEQRES 18 B 250 ARG LYS GLN GLY ASP HIS ARG MET LYS GLU LYS ALA ASP
SEQRES 19 B 250 ILE HIS LEU LEU ILE CYS THR ILE ASP ASP LEU ILE ASP
SEQRES 20 B 250 LYS LEU SER
HET MPD B 301 22
HET SR B 302 1
HET SR B 303 1
HET SR B 304 1
HET SR B 305 1
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SR STRONTIUM ION
FORMUL 2 MPD C6 H14 O2
FORMUL 3 SR 4(SR 2+)
FORMUL 7 HOH *205(H2 O)
HELIX 1 AA1 GLY B 38 GLY B 52 1 15
HELIX 2 AA2 ASN B 69 CYS B 73 5 5
HELIX 3 AA3 THR B 74 VAL B 89 1 16
HELIX 4 AA4 SER B 100 ARG B 113 1 14
HELIX 5 AA5 LEU B 130 LEU B 137 1 8
HELIX 6 AA6 PRO B 138 GLY B 149 1 12
HELIX 7 AA7 PRO B 154 LYS B 159 1 6
HELIX 8 AA8 TYR B 167 GLU B 174 1 8
HELIX 9 AA9 HIS B 175 CYS B 177 5 3
HELIX 10 AB1 TRP B 202 ILE B 212 1 11
HELIX 11 AB2 GLU B 231 SER B 250 1 20
SHEET 1 AA1 8 LEU B 3 LEU B 6 0
SHEET 2 AA1 8 LEU B 14 LEU B 19 -1 O LEU B 14 N LEU B 6
SHEET 3 AA1 8 HIS B 53 PHE B 58 -1 O PHE B 55 N LEU B 19
SHEET 4 AA1 8 LYS B 22 ILE B 29 1 N LYS B 22 O ALA B 54
SHEET 5 AA1 8 GLN B 94 SER B 99 1 O ILE B 95 N GLY B 25
SHEET 6 AA1 8 VAL B 117 ILE B 123 1 O ILE B 121 N LEU B 96
SHEET 7 AA1 8 VAL B 189 GLY B 194 1 O LEU B 192 N GLY B 122
SHEET 8 AA1 8 VAL B 217 ARG B 222 1 O ILE B 220 N LEU B 191
SHEET 1 AA2 2 GLU B 150 THR B 152 0
SHEET 2 AA2 2 ARG B 164 PRO B 166 -1 O ILE B 165 N TRP B 151
LINK OD1 ASN B 7 SR SR B 302 1555 1555 2.39
LINK O ARG B 8 SR SR B 302 1555 1555 2.48
LINK O HIS B 135 SR SR B 304 1555 1555 2.40
LINK SR SR B 302 O HOH B 410 1555 1555 2.31
LINK SR SR B 302 O HOH B 567 1555 1555 2.97
LINK SR SR B 302 O HOH B 540 1555 1555 2.62
LINK SR SR B 302 O HOH B 542 1555 1555 2.44
LINK SR SR B 303 O HOH B 429 1555 1555 2.92
LINK SR SR B 303 O HOH B 451 1555 1555 2.64
LINK SR SR B 303 O HOH B 518 1555 1555 2.79
LINK SR SR B 303 O HOH B 429 1555 12545 2.69
LINK SR SR B 303 O HOH B 403 1555 12545 2.95
CISPEP 1 THR B 23 PRO B 24 0 2.38
SITE 1 AC1 2 SER B 100 HOH B 408
SITE 1 AC2 8 ASN B 7 ARG B 8 GLU B 10 ASN B 13
SITE 2 AC2 8 HOH B 410 HOH B 540 HOH B 542 HOH B 567
SITE 1 AC3 4 HOH B 403 HOH B 429 HOH B 451 HOH B 518
SITE 1 AC4 1 HIS B 135
SITE 1 AC5 2 ASP B 243 HOH B 401
CRYST1 99.388 99.388 149.597 90.00 90.00 120.00 P 63 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 0.010062 0.005809 0.000000 0.00000
SCALE2 0.000000 0.011618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006685 0.00000
TER 3951 SER B 250
MASTER 349 0 5 11 10 0 6 6 2171 1 36 20
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