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HEADER HYDROLASE 31-AUG-22 8AXC
TITLE CRYSTAL STRUCTURE OF MOUSE CES2C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLCARNITINE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ACH M1,CARBOXYLESTERASE 2,CES 2,CARBOXYLIC ESTER HYDROLASE,
COMPND 5 PEROXISOME PROLIFERATOR-INDUCIBLE ACYLCARNITINE HYDROLASE;
COMPND 6 EC: 3.1.1.28,3.1.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CES2C, CES2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS CARBOXYLESTERASE 2C; PROTEIN STRUCTURE; LIPID METABOLISM; X-RAY
KEYWDS 2 CRYSTALLOGRAPHY; ALPHA/BETA-HYDROLASE FOLD; BIOCHEMISTRY; LIPID
KEYWDS 3 HYDROLYSIS; NON-ALCOHOLIC FATTY LIVER DISEASE; MOLNUPIRAVIR,
KEYWDS 4 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.EISNER,L.RIEGLER-BERKET,C.RODRIGUEZ GAMEZ,T.SAGMEISTER,G.CHALHOUB,
AUTHOR 2 B.DARNHOFER,J.PANIKKAVEETIL JAWAHARLAL,R.BIRNER-GRUENBERGER,
AUTHOR 3 T.PAVKOV-KELLER,G.HAEMMERLE,G.SCHOISWOHL,M.OBERER
REVDAT 1 16-NOV-22 8AXC 0
JRNL AUTH H.EISNER,L.RIEGLER-BERKET,C.F.GAMEZ,T.SAGMEISTER,G.CHALHOUB,
JRNL AUTH 2 B.DARNHOFER,P.J.JAZLEENA,R.BIRNER-GRUENBERGER,
JRNL AUTH 3 T.PAVKOV-KELLER,G.HAEMMERLE,G.SCHOISWOHL,M.OBERER
JRNL TITL THE CRYSTAL STRUCTURE OF MOUSE CES2C, A POTENTIAL ORTHOLOG
JRNL TITL 2 OF HUMAN CES2, SHOWS STRUCTURAL SIMILARITIES IN SUBSTRATE
JRNL TITL 3 REGULATION AND PRODUCT RELEASE TO HUMAN CES1
JRNL REF INT J MOL SCI V. 23 2022
JRNL REFN ESSN 1422-0067
JRNL DOI 10.3390/IJMS232113101
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 145757
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.037
REMARK 3 FREE R VALUE TEST SET COUNT : 7342
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9992
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 528
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16161
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 1517
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00900
REMARK 3 B22 (A**2) : 0.00800
REMARK 3 B33 (A**2) : -0.01700
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.153
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16996 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 15644 ; 0.035 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23158 ; 1.534 ; 1.635
REMARK 3 BOND ANGLES OTHERS (DEGREES): 36170 ; 2.303 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2132 ; 6.685 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 861 ;31.540 ;22.985
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2737 ;11.596 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 79 ;18.778 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2143 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19500 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3868 ; 0.011 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3337 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 60 ; 0.265 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8130 ; 0.163 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1126 ; 0.161 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8435 ; 2.951 ; 3.182
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8434 ; 2.948 ; 3.182
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10582 ; 4.246 ; 4.750
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10583 ; 4.247 ; 4.751
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8561 ; 4.097 ; 3.687
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8560 ; 4.096 ; 3.688
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12559 ; 6.358 ; 5.314
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12559 ; 6.357 ; 5.314
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 6
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 29 A 549 NULL
REMARK 3 1 B 29 B 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 2 A 31 A 550 NULL
REMARK 3 2 C 31 C 550 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 A 30 A 549 NULL
REMARK 3 3 D 30 D 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 4 B 31 B 550 NULL
REMARK 3 4 C 31 C 550 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 5 B 30 B 560 NULL
REMARK 3 5 D 30 D 560 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 6 C 31 C 549 NULL
REMARK 3 6 D 31 D 549 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8AXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1292120886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.012100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 49.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09060
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53280
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 1MX9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION CONDITION 0.5 UL WITH
REMARK 280 PEG 8000, 0.2 M AMMONIUM SULFATE 0.1 M SODIUM CACODYLATE, PH-6.5,
REMARK 280 30 % W/V AND 0.5 UL 10MG/ML PROTEIN IN 150MM NACL, 20MM TRIS
REMARK 280 HCL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 49.02600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.87800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.79750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.87800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.02600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.79750
REMARK 290 SMTRY3 4 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 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 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 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 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 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 1
REMARK 465 THR A 2
REMARK 465 ARG A 3
REMARK 465 ASN A 4
REMARK 465 GLN A 5
REMARK 465 LEU A 6
REMARK 465 HIS A 7
REMARK 465 ASN A 8
REMARK 465 TRP A 9
REMARK 465 LEU A 10
REMARK 465 ASN A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 PHE A 14
REMARK 465 PHE A 15
REMARK 465 GLY A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 LEU A 20
REMARK 465 LEU A 21
REMARK 465 ILE A 22
REMARK 465 HIS A 23
REMARK 465 VAL A 24
REMARK 465 GLN A 25
REMARK 465 GLY A 26
REMARK 465 GLN A 27
REMARK 465 ASP A 28
REMARK 465 GLY A 108
REMARK 465 LEU A 109
REMARK 465 PRO A 110
REMARK 465 ASP A 111
REMARK 465 MET A 112
REMARK 465 LYS A 113
REMARK 465 LEU A 551
REMARK 465 LYS A 552
REMARK 465 ALA A 553
REMARK 465 SER A 554
REMARK 465 GLN A 555
REMARK 465 ASP A 556
REMARK 465 LYS A 557
REMARK 465 HIS A 558
REMARK 465 ARG A 559
REMARK 465 GLU A 560
REMARK 465 LEU A 561
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ARG B 3
REMARK 465 ASN B 4
REMARK 465 GLN B 5
REMARK 465 LEU B 6
REMARK 465 HIS B 7
REMARK 465 ASN B 8
REMARK 465 TRP B 9
REMARK 465 LEU B 10
REMARK 465 ASN B 11
REMARK 465 ALA B 12
REMARK 465 GLY B 13
REMARK 465 PHE B 14
REMARK 465 PHE B 15
REMARK 465 GLY B 16
REMARK 465 LEU B 17
REMARK 465 LEU B 18
REMARK 465 LEU B 19
REMARK 465 LEU B 20
REMARK 465 LEU B 21
REMARK 465 ILE B 22
REMARK 465 HIS B 23
REMARK 465 VAL B 24
REMARK 465 GLN B 25
REMARK 465 GLY B 26
REMARK 465 GLN B 27
REMARK 465 ASP B 28
REMARK 465 LEU B 561
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ARG C 3
REMARK 465 ASN C 4
REMARK 465 GLN C 5
REMARK 465 LEU C 6
REMARK 465 HIS C 7
REMARK 465 ASN C 8
REMARK 465 TRP C 9
REMARK 465 LEU C 10
REMARK 465 ASN C 11
REMARK 465 ALA C 12
REMARK 465 GLY C 13
REMARK 465 PHE C 14
REMARK 465 PHE C 15
REMARK 465 GLY C 16
REMARK 465 LEU C 17
REMARK 465 LEU C 18
REMARK 465 LEU C 19
REMARK 465 LEU C 20
REMARK 465 LEU C 21
REMARK 465 ILE C 22
REMARK 465 HIS C 23
REMARK 465 VAL C 24
REMARK 465 GLN C 25
REMARK 465 GLY C 26
REMARK 465 GLN C 27
REMARK 465 ASP C 28
REMARK 465 SER C 29
REMARK 465 PRO C 30
REMARK 465 LYS C 51
REMARK 465 ASP C 52
REMARK 465 THR C 53
REMARK 465 LYS C 54
REMARK 465 ASN C 105
REMARK 465 GLU C 106
REMARK 465 ALA C 107
REMARK 465 GLY C 108
REMARK 465 LEU C 109
REMARK 465 PRO C 110
REMARK 465 ASP C 111
REMARK 465 MET C 112
REMARK 465 LYS C 113
REMARK 465 MET C 114
REMARK 465 MET C 115
REMARK 465 LEU C 116
REMARK 465 SER C 117
REMARK 465 LEU C 551
REMARK 465 LYS C 552
REMARK 465 ALA C 553
REMARK 465 SER C 554
REMARK 465 GLN C 555
REMARK 465 ASP C 556
REMARK 465 LYS C 557
REMARK 465 HIS C 558
REMARK 465 ARG C 559
REMARK 465 GLU C 560
REMARK 465 LEU C 561
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ARG D 3
REMARK 465 ASN D 4
REMARK 465 GLN D 5
REMARK 465 LEU D 6
REMARK 465 HIS D 7
REMARK 465 ASN D 8
REMARK 465 TRP D 9
REMARK 465 LEU D 10
REMARK 465 ASN D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 PHE D 14
REMARK 465 PHE D 15
REMARK 465 GLY D 16
REMARK 465 LEU D 17
REMARK 465 LEU D 18
REMARK 465 LEU D 19
REMARK 465 LEU D 20
REMARK 465 LEU D 21
REMARK 465 ILE D 22
REMARK 465 HIS D 23
REMARK 465 VAL D 24
REMARK 465 GLN D 25
REMARK 465 GLY D 26
REMARK 465 GLN D 27
REMARK 465 ASP D 28
REMARK 465 SER D 29
REMARK 465 LYS D 51
REMARK 465 ASP D 52
REMARK 465 LEU D 104
REMARK 465 ASN D 105
REMARK 465 GLU D 106
REMARK 465 ALA D 107
REMARK 465 GLY D 108
REMARK 465 LEU D 109
REMARK 465 PRO D 110
REMARK 465 ASP D 111
REMARK 465 MET D 112
REMARK 465 LYS D 113
REMARK 465 MET D 114
REMARK 465 MET D 115
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HD21 ASN C 503 H TRP C 510 1.12
REMARK 500 OD1 ASP D 286 O HOH D 701 1.26
REMARK 500 H VAL B 224 HD2 HIS B 250 1.30
REMARK 500 H VAL D 224 HD2 HIS D 250 1.30
REMARK 500 H VAL C 224 HD2 HIS C 250 1.32
REMARK 500 OD1 ASN B 100 O HOH B 701 1.73
REMARK 500 OE2 GLU B 31 O HOH B 702 1.80
REMARK 500 OD2 ASP B 286 OD2 ASP D 286 1.82
REMARK 500 OE1 GLU B 79 OE1 GLU C 79 1.90
REMARK 500 OD1 ASN C 100 O HOH C 701 2.05
REMARK 500 OD1 ASN D 100 O HOH D 702 2.08
REMARK 500 OD1 ASP B 286 NE2 GLN B 288 2.11
REMARK 500 O ALA B 107 O HOH B 703 2.17
REMARK 500 OE1 GLU C 138 O HOH C 702 2.17
REMARK 500 OE1 GLU B 79 CD GLU C 79 2.17
REMARK 500 CG ASP D 286 O HOH D 701 2.18
REMARK 500 OE1 GLU A 31 O HOH A 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 79 CD GLU A 79 OE1 0.068
REMARK 500 GLU C 79 CD GLU C 79 OE2 0.072
REMARK 500
REMARK 500 REMARK: NULL
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 D 292 NE - CZ - NH2 ANGL. DEV. = 3.6 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 MET A 115 55.03 37.52
REMARK 500 GLU A 138 119.69 -37.72
REMARK 500 PHE A 186 10.94 -142.01
REMARK 500 ALA A 194 81.40 -158.78
REMARK 500 SER A 230 -115.68 59.07
REMARK 500 LEU A 261 109.72 -55.09
REMARK 500 CYS A 282 50.17 -102.87
REMARK 500 ASP A 346 55.75 -143.09
REMARK 500 TRP A 350 -67.50 -152.43
REMARK 500 PHE A 418 -53.10 -120.55
REMARK 500 LYS A 456 -121.70 -95.54
REMARK 500 ASP A 514 -156.76 -133.25
REMARK 500 LYS A 542 -62.91 -123.70
REMARK 500 ASP B 111 -14.33 86.43
REMARK 500 GLU B 138 120.81 -38.36
REMARK 500 ALA B 194 81.66 -158.91
REMARK 500 SER B 230 -116.55 58.75
REMARK 500 CYS B 282 49.38 -100.81
REMARK 500 ASP B 346 54.96 -144.07
REMARK 500 TRP B 350 -65.25 -154.01
REMARK 500 PHE B 418 -52.49 -121.55
REMARK 500 LYS B 456 -123.18 -97.09
REMARK 500 ASP B 514 -158.02 -141.86
REMARK 500 LYS B 542 -64.16 -123.21
REMARK 500 GLU C 138 120.19 -37.35
REMARK 500 PHE C 186 12.28 -142.88
REMARK 500 ALA C 194 81.33 -157.74
REMARK 500 SER C 230 -115.53 59.38
REMARK 500 ASP C 346 56.46 -142.98
REMARK 500 TRP C 350 -67.26 -152.57
REMARK 500 PHE C 418 -53.26 -120.20
REMARK 500 LYS C 456 -122.00 -96.91
REMARK 500 ASP C 514 -158.14 -132.74
REMARK 500 LYS C 542 -63.19 -123.66
REMARK 500 GLU D 138 118.31 -34.25
REMARK 500 PHE D 186 12.75 -141.14
REMARK 500 ALA D 194 81.03 -158.98
REMARK 500 SER D 230 -116.87 58.95
REMARK 500 CYS D 282 53.10 -90.46
REMARK 500 ASP D 346 54.52 -142.74
REMARK 500 TRP D 350 -66.72 -153.29
REMARK 500 LYS D 456 -120.81 -95.85
REMARK 500 ASP D 514 -156.29 -141.27
REMARK 500 LYS D 542 -62.95 -123.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8AXC A 1 561 UNP Q91WG0 EST2C_MOUSE 1 561
DBREF 8AXC B 1 561 UNP Q91WG0 EST2C_MOUSE 1 561
DBREF 8AXC C 1 561 UNP Q91WG0 EST2C_MOUSE 1 561
DBREF 8AXC D 1 561 UNP Q91WG0 EST2C_MOUSE 1 561
SEQRES 1 A 561 MET THR ARG ASN GLN LEU HIS ASN TRP LEU ASN ALA GLY
SEQRES 2 A 561 PHE PHE GLY LEU LEU LEU LEU LEU ILE HIS VAL GLN GLY
SEQRES 3 A 561 GLN ASP SER PRO GLU ALA ASN PRO ILE ARG ASN THR HIS
SEQRES 4 A 561 THR GLY GLN ILE GLN GLY SER LEU ILE HIS VAL LYS ASP
SEQRES 5 A 561 THR LYS ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE
SEQRES 6 A 561 ALA LYS PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO
SEQRES 7 A 561 GLU ALA PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR
SEQRES 8 A 561 ALA HIS PRO ALA MET CYS LEU GLN ASN LEU ASP MET LEU
SEQRES 9 A 561 ASN GLU ALA GLY LEU PRO ASP MET LYS MET MET LEU SER
SEQRES 10 A 561 SER PHE PRO MET SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 11 A 561 TYR THR PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO
SEQRES 12 A 561 VAL MET VAL TRP ILE HIS GLY GLY ALA LEU VAL ILE GLY
SEQRES 13 A 561 MET ALA SER MET PHE ASP GLY SER LEU LEU THR VAL ASN
SEQRES 14 A 561 GLU ASP LEU VAL VAL VAL THR ILE GLN TYR ARG LEU GLY
SEQRES 15 A 561 VAL LEU GLY PHE PHE SER THR GLY ASP GLN HIS ALA ARG
SEQRES 16 A 561 GLY ASN TRP GLY TYR LEU ASP GLN ALA ALA ALA LEU ARG
SEQRES 17 A 561 TRP VAL GLN GLN ASN ILE ALA HIS PHE GLY GLY ASN PRO
SEQRES 18 A 561 ASP ARG VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR
SEQRES 19 A 561 SER VAL SER SER HIS VAL VAL SER PRO MET SER GLN GLY
SEQRES 20 A 561 LEU PHE HIS GLY ALA ILE MET GLU SER GLY VAL ALA LEU
SEQRES 21 A 561 LEU PRO ASP LEU ILE SER GLU THR SER GLU MET VAL SER
SEQRES 22 A 561 THR THR VAL ALA LYS LEU SER GLY CYS GLU ALA MET ASP
SEQRES 23 A 561 SER GLN ALA LEU VAL ARG CYS LEU ARG GLY LYS SER GLU
SEQRES 24 A 561 ALA GLU ILE LEU ALA ILE ASN LYS VAL PHE LYS MET ILE
SEQRES 25 A 561 PRO ALA VAL VAL ASP GLY GLU PHE PHE PRO ARG HIS PRO
SEQRES 26 A 561 LYS GLU LEU LEU ALA SER GLU ASP PHE HIS PRO VAL PRO
SEQRES 27 A 561 SER ILE ILE GLY VAL ASN ASN ASP GLU PHE GLY TRP SER
SEQRES 28 A 561 ILE PRO VAL VAL MET GLY SER ALA GLN MET ILE LYS GLY
SEQRES 29 A 561 ILE THR ARG GLU ASN LEU GLN ALA VAL LEU LYS ASP THR
SEQRES 30 A 561 ALA VAL GLN MET MET LEU PRO PRO GLU CYS SER ASP LEU
SEQRES 31 A 561 LEU MET GLU GLU TYR MET GLY ASP THR GLU ASP ALA GLN
SEQRES 32 A 561 THR LEU GLN ILE GLN PHE THR GLU MET MET GLY ASP PHE
SEQRES 33 A 561 MET PHE VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN
SEQRES 34 A 561 ARG SER HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS
SEQRES 35 A 561 PRO PRO SER TYR PHE LYS ASP VAL ARG PRO PRO HIS VAL
SEQRES 36 A 561 LYS ALA ASP HIS ALA ASP GLU ILE PRO PHE VAL PHE ALA
SEQRES 37 A 561 SER PHE PHE TRP GLY MET LYS LEU ASP PHE THR GLU GLU
SEQRES 38 A 561 GLU GLU LEU LEU SER ARG ARG MET MET LYS TYR TRP ALA
SEQRES 39 A 561 ASN PHE ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU
SEQRES 40 A 561 PRO TYR TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU
SEQRES 41 A 561 GLN LEU ASP ILE GLN PRO ALA VAL GLY ARG ALA LEU LYS
SEQRES 42 A 561 ALA GLY ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN
SEQRES 43 A 561 LYS ILE GLN GLU LEU LYS ALA SER GLN ASP LYS HIS ARG
SEQRES 44 A 561 GLU LEU
SEQRES 1 B 561 MET THR ARG ASN GLN LEU HIS ASN TRP LEU ASN ALA GLY
SEQRES 2 B 561 PHE PHE GLY LEU LEU LEU LEU LEU ILE HIS VAL GLN GLY
SEQRES 3 B 561 GLN ASP SER PRO GLU ALA ASN PRO ILE ARG ASN THR HIS
SEQRES 4 B 561 THR GLY GLN ILE GLN GLY SER LEU ILE HIS VAL LYS ASP
SEQRES 5 B 561 THR LYS ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE
SEQRES 6 B 561 ALA LYS PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO
SEQRES 7 B 561 GLU ALA PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR
SEQRES 8 B 561 ALA HIS PRO ALA MET CYS LEU GLN ASN LEU ASP MET LEU
SEQRES 9 B 561 ASN GLU ALA GLY LEU PRO ASP MET LYS MET MET LEU SER
SEQRES 10 B 561 SER PHE PRO MET SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 11 B 561 TYR THR PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO
SEQRES 12 B 561 VAL MET VAL TRP ILE HIS GLY GLY ALA LEU VAL ILE GLY
SEQRES 13 B 561 MET ALA SER MET PHE ASP GLY SER LEU LEU THR VAL ASN
SEQRES 14 B 561 GLU ASP LEU VAL VAL VAL THR ILE GLN TYR ARG LEU GLY
SEQRES 15 B 561 VAL LEU GLY PHE PHE SER THR GLY ASP GLN HIS ALA ARG
SEQRES 16 B 561 GLY ASN TRP GLY TYR LEU ASP GLN ALA ALA ALA LEU ARG
SEQRES 17 B 561 TRP VAL GLN GLN ASN ILE ALA HIS PHE GLY GLY ASN PRO
SEQRES 18 B 561 ASP ARG VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR
SEQRES 19 B 561 SER VAL SER SER HIS VAL VAL SER PRO MET SER GLN GLY
SEQRES 20 B 561 LEU PHE HIS GLY ALA ILE MET GLU SER GLY VAL ALA LEU
SEQRES 21 B 561 LEU PRO ASP LEU ILE SER GLU THR SER GLU MET VAL SER
SEQRES 22 B 561 THR THR VAL ALA LYS LEU SER GLY CYS GLU ALA MET ASP
SEQRES 23 B 561 SER GLN ALA LEU VAL ARG CYS LEU ARG GLY LYS SER GLU
SEQRES 24 B 561 ALA GLU ILE LEU ALA ILE ASN LYS VAL PHE LYS MET ILE
SEQRES 25 B 561 PRO ALA VAL VAL ASP GLY GLU PHE PHE PRO ARG HIS PRO
SEQRES 26 B 561 LYS GLU LEU LEU ALA SER GLU ASP PHE HIS PRO VAL PRO
SEQRES 27 B 561 SER ILE ILE GLY VAL ASN ASN ASP GLU PHE GLY TRP SER
SEQRES 28 B 561 ILE PRO VAL VAL MET GLY SER ALA GLN MET ILE LYS GLY
SEQRES 29 B 561 ILE THR ARG GLU ASN LEU GLN ALA VAL LEU LYS ASP THR
SEQRES 30 B 561 ALA VAL GLN MET MET LEU PRO PRO GLU CYS SER ASP LEU
SEQRES 31 B 561 LEU MET GLU GLU TYR MET GLY ASP THR GLU ASP ALA GLN
SEQRES 32 B 561 THR LEU GLN ILE GLN PHE THR GLU MET MET GLY ASP PHE
SEQRES 33 B 561 MET PHE VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN
SEQRES 34 B 561 ARG SER HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS
SEQRES 35 B 561 PRO PRO SER TYR PHE LYS ASP VAL ARG PRO PRO HIS VAL
SEQRES 36 B 561 LYS ALA ASP HIS ALA ASP GLU ILE PRO PHE VAL PHE ALA
SEQRES 37 B 561 SER PHE PHE TRP GLY MET LYS LEU ASP PHE THR GLU GLU
SEQRES 38 B 561 GLU GLU LEU LEU SER ARG ARG MET MET LYS TYR TRP ALA
SEQRES 39 B 561 ASN PHE ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU
SEQRES 40 B 561 PRO TYR TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU
SEQRES 41 B 561 GLN LEU ASP ILE GLN PRO ALA VAL GLY ARG ALA LEU LYS
SEQRES 42 B 561 ALA GLY ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN
SEQRES 43 B 561 LYS ILE GLN GLU LEU LYS ALA SER GLN ASP LYS HIS ARG
SEQRES 44 B 561 GLU LEU
SEQRES 1 C 561 MET THR ARG ASN GLN LEU HIS ASN TRP LEU ASN ALA GLY
SEQRES 2 C 561 PHE PHE GLY LEU LEU LEU LEU LEU ILE HIS VAL GLN GLY
SEQRES 3 C 561 GLN ASP SER PRO GLU ALA ASN PRO ILE ARG ASN THR HIS
SEQRES 4 C 561 THR GLY GLN ILE GLN GLY SER LEU ILE HIS VAL LYS ASP
SEQRES 5 C 561 THR LYS ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE
SEQRES 6 C 561 ALA LYS PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO
SEQRES 7 C 561 GLU ALA PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR
SEQRES 8 C 561 ALA HIS PRO ALA MET CYS LEU GLN ASN LEU ASP MET LEU
SEQRES 9 C 561 ASN GLU ALA GLY LEU PRO ASP MET LYS MET MET LEU SER
SEQRES 10 C 561 SER PHE PRO MET SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 11 C 561 TYR THR PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO
SEQRES 12 C 561 VAL MET VAL TRP ILE HIS GLY GLY ALA LEU VAL ILE GLY
SEQRES 13 C 561 MET ALA SER MET PHE ASP GLY SER LEU LEU THR VAL ASN
SEQRES 14 C 561 GLU ASP LEU VAL VAL VAL THR ILE GLN TYR ARG LEU GLY
SEQRES 15 C 561 VAL LEU GLY PHE PHE SER THR GLY ASP GLN HIS ALA ARG
SEQRES 16 C 561 GLY ASN TRP GLY TYR LEU ASP GLN ALA ALA ALA LEU ARG
SEQRES 17 C 561 TRP VAL GLN GLN ASN ILE ALA HIS PHE GLY GLY ASN PRO
SEQRES 18 C 561 ASP ARG VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR
SEQRES 19 C 561 SER VAL SER SER HIS VAL VAL SER PRO MET SER GLN GLY
SEQRES 20 C 561 LEU PHE HIS GLY ALA ILE MET GLU SER GLY VAL ALA LEU
SEQRES 21 C 561 LEU PRO ASP LEU ILE SER GLU THR SER GLU MET VAL SER
SEQRES 22 C 561 THR THR VAL ALA LYS LEU SER GLY CYS GLU ALA MET ASP
SEQRES 23 C 561 SER GLN ALA LEU VAL ARG CYS LEU ARG GLY LYS SER GLU
SEQRES 24 C 561 ALA GLU ILE LEU ALA ILE ASN LYS VAL PHE LYS MET ILE
SEQRES 25 C 561 PRO ALA VAL VAL ASP GLY GLU PHE PHE PRO ARG HIS PRO
SEQRES 26 C 561 LYS GLU LEU LEU ALA SER GLU ASP PHE HIS PRO VAL PRO
SEQRES 27 C 561 SER ILE ILE GLY VAL ASN ASN ASP GLU PHE GLY TRP SER
SEQRES 28 C 561 ILE PRO VAL VAL MET GLY SER ALA GLN MET ILE LYS GLY
SEQRES 29 C 561 ILE THR ARG GLU ASN LEU GLN ALA VAL LEU LYS ASP THR
SEQRES 30 C 561 ALA VAL GLN MET MET LEU PRO PRO GLU CYS SER ASP LEU
SEQRES 31 C 561 LEU MET GLU GLU TYR MET GLY ASP THR GLU ASP ALA GLN
SEQRES 32 C 561 THR LEU GLN ILE GLN PHE THR GLU MET MET GLY ASP PHE
SEQRES 33 C 561 MET PHE VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN
SEQRES 34 C 561 ARG SER HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS
SEQRES 35 C 561 PRO PRO SER TYR PHE LYS ASP VAL ARG PRO PRO HIS VAL
SEQRES 36 C 561 LYS ALA ASP HIS ALA ASP GLU ILE PRO PHE VAL PHE ALA
SEQRES 37 C 561 SER PHE PHE TRP GLY MET LYS LEU ASP PHE THR GLU GLU
SEQRES 38 C 561 GLU GLU LEU LEU SER ARG ARG MET MET LYS TYR TRP ALA
SEQRES 39 C 561 ASN PHE ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU
SEQRES 40 C 561 PRO TYR TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU
SEQRES 41 C 561 GLN LEU ASP ILE GLN PRO ALA VAL GLY ARG ALA LEU LYS
SEQRES 42 C 561 ALA GLY ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN
SEQRES 43 C 561 LYS ILE GLN GLU LEU LYS ALA SER GLN ASP LYS HIS ARG
SEQRES 44 C 561 GLU LEU
SEQRES 1 D 561 MET THR ARG ASN GLN LEU HIS ASN TRP LEU ASN ALA GLY
SEQRES 2 D 561 PHE PHE GLY LEU LEU LEU LEU LEU ILE HIS VAL GLN GLY
SEQRES 3 D 561 GLN ASP SER PRO GLU ALA ASN PRO ILE ARG ASN THR HIS
SEQRES 4 D 561 THR GLY GLN ILE GLN GLY SER LEU ILE HIS VAL LYS ASP
SEQRES 5 D 561 THR LYS ALA GLY VAL HIS THR PHE LEU GLY ILE PRO PHE
SEQRES 6 D 561 ALA LYS PRO PRO VAL GLY PRO LEU ARG PHE ALA PRO PRO
SEQRES 7 D 561 GLU ALA PRO GLU PRO TRP SER GLY VAL ARG ASP GLY THR
SEQRES 8 D 561 ALA HIS PRO ALA MET CYS LEU GLN ASN LEU ASP MET LEU
SEQRES 9 D 561 ASN GLU ALA GLY LEU PRO ASP MET LYS MET MET LEU SER
SEQRES 10 D 561 SER PHE PRO MET SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 11 D 561 TYR THR PRO ALA HIS ALA HIS GLU GLY SER ASN LEU PRO
SEQRES 12 D 561 VAL MET VAL TRP ILE HIS GLY GLY ALA LEU VAL ILE GLY
SEQRES 13 D 561 MET ALA SER MET PHE ASP GLY SER LEU LEU THR VAL ASN
SEQRES 14 D 561 GLU ASP LEU VAL VAL VAL THR ILE GLN TYR ARG LEU GLY
SEQRES 15 D 561 VAL LEU GLY PHE PHE SER THR GLY ASP GLN HIS ALA ARG
SEQRES 16 D 561 GLY ASN TRP GLY TYR LEU ASP GLN ALA ALA ALA LEU ARG
SEQRES 17 D 561 TRP VAL GLN GLN ASN ILE ALA HIS PHE GLY GLY ASN PRO
SEQRES 18 D 561 ASP ARG VAL THR ILE PHE GLY GLU SER ALA GLY GLY THR
SEQRES 19 D 561 SER VAL SER SER HIS VAL VAL SER PRO MET SER GLN GLY
SEQRES 20 D 561 LEU PHE HIS GLY ALA ILE MET GLU SER GLY VAL ALA LEU
SEQRES 21 D 561 LEU PRO ASP LEU ILE SER GLU THR SER GLU MET VAL SER
SEQRES 22 D 561 THR THR VAL ALA LYS LEU SER GLY CYS GLU ALA MET ASP
SEQRES 23 D 561 SER GLN ALA LEU VAL ARG CYS LEU ARG GLY LYS SER GLU
SEQRES 24 D 561 ALA GLU ILE LEU ALA ILE ASN LYS VAL PHE LYS MET ILE
SEQRES 25 D 561 PRO ALA VAL VAL ASP GLY GLU PHE PHE PRO ARG HIS PRO
SEQRES 26 D 561 LYS GLU LEU LEU ALA SER GLU ASP PHE HIS PRO VAL PRO
SEQRES 27 D 561 SER ILE ILE GLY VAL ASN ASN ASP GLU PHE GLY TRP SER
SEQRES 28 D 561 ILE PRO VAL VAL MET GLY SER ALA GLN MET ILE LYS GLY
SEQRES 29 D 561 ILE THR ARG GLU ASN LEU GLN ALA VAL LEU LYS ASP THR
SEQRES 30 D 561 ALA VAL GLN MET MET LEU PRO PRO GLU CYS SER ASP LEU
SEQRES 31 D 561 LEU MET GLU GLU TYR MET GLY ASP THR GLU ASP ALA GLN
SEQRES 32 D 561 THR LEU GLN ILE GLN PHE THR GLU MET MET GLY ASP PHE
SEQRES 33 D 561 MET PHE VAL ILE PRO ALA LEU GLN VAL ALA HIS PHE GLN
SEQRES 34 D 561 ARG SER HIS ALA PRO VAL TYR PHE TYR GLU PHE GLN HIS
SEQRES 35 D 561 PRO PRO SER TYR PHE LYS ASP VAL ARG PRO PRO HIS VAL
SEQRES 36 D 561 LYS ALA ASP HIS ALA ASP GLU ILE PRO PHE VAL PHE ALA
SEQRES 37 D 561 SER PHE PHE TRP GLY MET LYS LEU ASP PHE THR GLU GLU
SEQRES 38 D 561 GLU GLU LEU LEU SER ARG ARG MET MET LYS TYR TRP ALA
SEQRES 39 D 561 ASN PHE ALA ARG HIS GLY ASN PRO ASN SER GLU GLY LEU
SEQRES 40 D 561 PRO TYR TRP PRO VAL MET ASP HIS ASP GLU GLN TYR LEU
SEQRES 41 D 561 GLN LEU ASP ILE GLN PRO ALA VAL GLY ARG ALA LEU LYS
SEQRES 42 D 561 ALA GLY ARG LEU GLN PHE TRP THR LYS THR LEU PRO GLN
SEQRES 43 D 561 LYS ILE GLN GLU LEU LYS ALA SER GLN ASP LYS HIS ARG
SEQRES 44 D 561 GLU LEU
HET CL A 601 1
HET NCA A 602 13
HET NCA A 603 13
HET CL B 601 1
HET NCA B 602 13
HET NCA B 603 13
HET SO4 C 601 5
HET CL C 602 1
HET NCA C 603 13
HET CL D 601 1
HET NCA D 602 13
HETNAM CL CHLORIDE ION
HETNAM NCA NICOTINAMIDE
HETNAM SO4 SULFATE ION
FORMUL 5 CL 4(CL 1-)
FORMUL 6 NCA 6(C6 H6 N2 O)
FORMUL 11 SO4 O4 S 2-
FORMUL 16 HOH *1517(H2 O)
HELIX 1 AA1 VAL A 70 ARG A 74 5 5
HELIX 2 AA2 ASN A 100 ALA A 107 1 8
HELIX 3 AA3 MET A 115 PHE A 119 5 5
HELIX 4 AA4 MET A 157 PHE A 161 5 5
HELIX 5 AA5 GLY A 163 ASP A 171 1 9
HELIX 6 AA6 LEU A 181 PHE A 187 1 7
HELIX 7 AA7 ASN A 197 ILE A 214 1 18
HELIX 8 AA8 ALA A 215 PHE A 217 5 3
HELIX 9 AA9 SER A 230 SER A 242 1 13
HELIX 10 AB1 PRO A 243 GLN A 246 5 4
HELIX 11 AB2 LEU A 261 ILE A 265 5 5
HELIX 12 AB3 SER A 269 GLY A 281 1 13
HELIX 13 AB4 ASP A 286 GLY A 296 1 11
HELIX 14 AB5 SER A 298 LYS A 307 1 10
HELIX 15 AB6 HIS A 324 SER A 331 1 8
HELIX 16 AB7 TRP A 350 MET A 356 1 7
HELIX 17 AB8 SER A 358 GLY A 364 1 7
HELIX 18 AB9 ASN A 369 MET A 381 1 13
HELIX 19 AC1 PRO A 384 GLU A 386 5 3
HELIX 20 AC2 CYS A 387 MET A 396 1 10
HELIX 21 AC3 ASP A 401 PHE A 418 1 18
HELIX 22 AC4 PHE A 418 SER A 431 1 14
HELIX 23 AC5 PRO A 444 LYS A 448 5 5
HELIX 24 AC6 GLU A 462 ALA A 468 1 7
HELIX 25 AC7 PHE A 470 MET A 474 5 5
HELIX 26 AC8 THR A 479 GLY A 500 1 22
HELIX 27 AC9 LYS A 533 LYS A 542 1 10
HELIX 28 AD1 LYS A 542 GLU A 550 1 9
HELIX 29 AD2 VAL B 70 ARG B 74 5 5
HELIX 30 AD3 ASN B 100 GLY B 108 5 9
HELIX 31 AD4 MET B 115 PHE B 119 5 5
HELIX 32 AD5 MET B 157 PHE B 161 5 5
HELIX 33 AD6 GLY B 163 ASP B 171 1 9
HELIX 34 AD7 LEU B 181 PHE B 187 1 7
HELIX 35 AD8 ASN B 197 ILE B 214 1 18
HELIX 36 AD9 ALA B 215 PHE B 217 5 3
HELIX 37 AE1 SER B 230 SER B 242 1 13
HELIX 38 AE2 PRO B 243 GLN B 246 5 4
HELIX 39 AE3 LEU B 261 ILE B 265 5 5
HELIX 40 AE4 SER B 269 GLY B 281 1 13
HELIX 41 AE5 ASP B 286 GLY B 296 1 11
HELIX 42 AE6 SER B 298 LYS B 307 1 10
HELIX 43 AE7 HIS B 324 SER B 331 1 8
HELIX 44 AE8 TRP B 350 MET B 356 1 7
HELIX 45 AE9 SER B 358 GLY B 364 1 7
HELIX 46 AF1 ASN B 369 MET B 381 1 13
HELIX 47 AF2 PRO B 384 GLU B 386 5 3
HELIX 48 AF3 CYS B 387 MET B 396 1 10
HELIX 49 AF4 ASP B 401 PHE B 418 1 18
HELIX 50 AF5 PHE B 418 SER B 431 1 14
HELIX 51 AF6 PRO B 444 LYS B 448 5 5
HELIX 52 AF7 GLU B 462 ALA B 468 1 7
HELIX 53 AF8 PHE B 470 MET B 474 5 5
HELIX 54 AF9 THR B 479 GLY B 500 1 22
HELIX 55 AG1 LYS B 533 LYS B 542 1 10
HELIX 56 AG2 LYS B 542 GLU B 560 1 19
HELIX 57 AG3 VAL C 70 ARG C 74 5 5
HELIX 58 AG4 MET C 157 PHE C 161 5 5
HELIX 59 AG5 GLY C 163 ASP C 171 1 9
HELIX 60 AG6 LEU C 181 PHE C 187 1 7
HELIX 61 AG7 ASN C 197 ILE C 214 1 18
HELIX 62 AG8 ALA C 215 PHE C 217 5 3
HELIX 63 AG9 SER C 230 SER C 242 1 13
HELIX 64 AH1 PRO C 243 GLN C 246 5 4
HELIX 65 AH2 LEU C 261 ILE C 265 5 5
HELIX 66 AH3 SER C 269 GLY C 281 1 13
HELIX 67 AH4 ASP C 286 GLY C 296 1 11
HELIX 68 AH5 SER C 298 LYS C 307 1 10
HELIX 69 AH6 HIS C 324 SER C 331 1 8
HELIX 70 AH7 TRP C 350 MET C 356 1 7
HELIX 71 AH8 SER C 358 GLY C 364 1 7
HELIX 72 AH9 ASN C 369 MET C 381 1 13
HELIX 73 AI1 PRO C 384 GLU C 386 5 3
HELIX 74 AI2 CYS C 387 MET C 396 1 10
HELIX 75 AI3 ASP C 401 PHE C 418 1 18
HELIX 76 AI4 PHE C 418 SER C 431 1 14
HELIX 77 AI5 PRO C 444 LYS C 448 5 5
HELIX 78 AI6 GLU C 462 ALA C 468 1 7
HELIX 79 AI7 PHE C 470 MET C 474 5 5
HELIX 80 AI8 THR C 479 GLY C 500 1 22
HELIX 81 AI9 LYS C 533 LYS C 542 1 10
HELIX 82 AJ1 LYS C 542 GLU C 550 1 9
HELIX 83 AJ2 VAL D 70 ARG D 74 5 5
HELIX 84 AJ3 MET D 157 PHE D 161 5 5
HELIX 85 AJ4 GLY D 163 ASP D 171 1 9
HELIX 86 AJ5 LEU D 181 PHE D 187 1 7
HELIX 87 AJ6 ASN D 197 ILE D 214 1 18
HELIX 88 AJ7 ALA D 215 PHE D 217 5 3
HELIX 89 AJ8 SER D 230 SER D 242 1 13
HELIX 90 AJ9 PRO D 243 GLN D 246 5 4
HELIX 91 AK1 LEU D 261 ILE D 265 5 5
HELIX 92 AK2 SER D 269 GLY D 281 1 13
HELIX 93 AK3 ASP D 286 GLY D 296 1 11
HELIX 94 AK4 SER D 298 LYS D 307 1 10
HELIX 95 AK5 HIS D 324 SER D 331 1 8
HELIX 96 AK6 TRP D 350 MET D 356 1 7
HELIX 97 AK7 SER D 358 GLY D 364 1 7
HELIX 98 AK8 ASN D 369 MET D 381 1 13
HELIX 99 AK9 PRO D 384 GLU D 386 5 3
HELIX 100 AL1 CYS D 387 MET D 396 1 10
HELIX 101 AL2 ASP D 401 PHE D 418 1 18
HELIX 102 AL3 PHE D 418 SER D 431 1 14
HELIX 103 AL4 PRO D 444 LYS D 448 5 5
HELIX 104 AL5 GLU D 462 ALA D 468 1 7
HELIX 105 AL6 PHE D 470 MET D 474 5 5
HELIX 106 AL7 THR D 479 GLY D 500 1 22
HELIX 107 AL8 LYS D 533 LYS D 542 1 10
HELIX 108 AL9 LYS D 542 LEU D 561 1 20
SHEET 1 AA1 3 ILE A 35 ARG A 36 0
SHEET 2 AA1 3 GLN A 42 GLN A 44 -1 O ILE A 43 N ARG A 36
SHEET 3 AA1 3 VAL A 87 ASP A 89 1 O ARG A 88 N GLN A 44
SHEET 1 AA211 SER A 46 ILE A 48 0
SHEET 2 AA211 VAL A 57 PRO A 64 -1 O VAL A 57 N ILE A 48
SHEET 3 AA211 TYR A 127 PRO A 133 -1 O THR A 132 N HIS A 58
SHEET 4 AA211 VAL A 173 ILE A 177 -1 O VAL A 174 N TYR A 131
SHEET 5 AA211 LEU A 142 ILE A 148 1 N TRP A 147 O VAL A 175
SHEET 6 AA211 GLY A 219 GLU A 229 1 O ASN A 220 N LEU A 142
SHEET 7 AA211 GLY A 251 GLU A 255 1 O GLU A 255 N GLY A 228
SHEET 8 AA211 SER A 339 ASN A 344 1 O ILE A 340 N MET A 254
SHEET 9 AA211 VAL A 435 PHE A 440 1 O PHE A 440 N VAL A 343
SHEET 10 AA211 GLN A 518 LEU A 522 1 O LEU A 520 N PHE A 437
SHEET 11 AA211 ALA A 527 ARG A 530 -1 O ALA A 527 N GLN A 521
SHEET 1 AA3 3 ILE B 35 ARG B 36 0
SHEET 2 AA3 3 GLN B 42 GLN B 44 -1 O ILE B 43 N ARG B 36
SHEET 3 AA3 3 VAL B 87 ASP B 89 1 O ARG B 88 N GLN B 44
SHEET 1 AA411 SER B 46 ILE B 48 0
SHEET 2 AA411 VAL B 57 PRO B 64 -1 O VAL B 57 N ILE B 48
SHEET 3 AA411 TYR B 127 PRO B 133 -1 O THR B 132 N HIS B 58
SHEET 4 AA411 VAL B 173 ILE B 177 -1 O VAL B 174 N TYR B 131
SHEET 5 AA411 LEU B 142 ILE B 148 1 N TRP B 147 O VAL B 175
SHEET 6 AA411 GLY B 219 GLU B 229 1 O ASN B 220 N LEU B 142
SHEET 7 AA411 GLY B 251 GLU B 255 1 O GLU B 255 N GLY B 228
SHEET 8 AA411 SER B 339 ASN B 344 1 O ILE B 340 N MET B 254
SHEET 9 AA411 VAL B 435 PHE B 440 1 O PHE B 440 N VAL B 343
SHEET 10 AA411 GLN B 518 LEU B 522 1 O LEU B 520 N PHE B 437
SHEET 11 AA411 ALA B 527 ARG B 530 -1 O ALA B 527 N GLN B 521
SHEET 1 AA5 3 ILE C 35 ARG C 36 0
SHEET 2 AA5 3 GLN C 42 GLN C 44 -1 O ILE C 43 N ARG C 36
SHEET 3 AA5 3 VAL C 87 ASP C 89 1 O ARG C 88 N GLN C 44
SHEET 1 AA611 SER C 46 ILE C 48 0
SHEET 2 AA611 VAL C 57 PRO C 64 -1 O VAL C 57 N ILE C 48
SHEET 3 AA611 TYR C 127 PRO C 133 -1 O THR C 132 N HIS C 58
SHEET 4 AA611 VAL C 173 ILE C 177 -1 O VAL C 174 N TYR C 131
SHEET 5 AA611 LEU C 142 ILE C 148 1 N TRP C 147 O VAL C 175
SHEET 6 AA611 GLY C 219 GLU C 229 1 O ASN C 220 N LEU C 142
SHEET 7 AA611 GLY C 251 GLU C 255 1 O GLU C 255 N GLY C 228
SHEET 8 AA611 SER C 339 ASN C 344 1 O ILE C 340 N MET C 254
SHEET 9 AA611 VAL C 435 PHE C 440 1 O PHE C 440 N VAL C 343
SHEET 10 AA611 GLN C 518 LEU C 522 1 O LEU C 520 N PHE C 437
SHEET 11 AA611 ALA C 527 ARG C 530 -1 O ALA C 527 N GLN C 521
SHEET 1 AA7 3 ILE D 35 ARG D 36 0
SHEET 2 AA7 3 GLN D 42 GLN D 44 -1 O ILE D 43 N ARG D 36
SHEET 3 AA7 3 VAL D 87 ASP D 89 1 O ARG D 88 N GLN D 44
SHEET 1 AA811 SER D 46 HIS D 49 0
SHEET 2 AA811 GLY D 56 PRO D 64 -1 O VAL D 57 N ILE D 48
SHEET 3 AA811 TYR D 127 PRO D 133 -1 O ILE D 130 N PHE D 60
SHEET 4 AA811 VAL D 173 ILE D 177 -1 O VAL D 174 N TYR D 131
SHEET 5 AA811 LEU D 142 ILE D 148 1 N TRP D 147 O VAL D 175
SHEET 6 AA811 GLY D 219 GLU D 229 1 O THR D 225 N VAL D 144
SHEET 7 AA811 GLY D 251 GLU D 255 1 O GLU D 255 N GLY D 228
SHEET 8 AA811 SER D 339 ASN D 344 1 O ILE D 340 N MET D 254
SHEET 9 AA811 VAL D 435 PHE D 440 1 O PHE D 440 N VAL D 343
SHEET 10 AA811 GLN D 518 LEU D 522 1 O LEU D 520 N PHE D 437
SHEET 11 AA811 ALA D 527 ARG D 530 -1 O ALA D 527 N GLN D 521
SSBOND 1 CYS A 97 CYS A 125 1555 1555 2.01
SSBOND 2 CYS A 282 CYS A 293 1555 1555 2.06
SSBOND 3 CYS B 97 CYS B 125 1555 1555 2.01
SSBOND 4 CYS B 282 CYS B 293 1555 1555 2.05
SSBOND 5 CYS C 97 CYS C 125 1555 1555 2.05
SSBOND 6 CYS C 282 CYS C 293 1555 1555 2.12
SSBOND 7 CYS D 97 CYS D 125 1555 1555 2.02
SSBOND 8 CYS D 282 CYS D 293 1555 1555 2.05
CRYST1 98.052 143.595 183.756 90.00 90.00 90.00 P 21 21 21 16
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 0.010199 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005442 0.00000
TER 7970 GLU A 550
TER 16248 GLU B 560
TER 24047 GLU C 550
TER 32038 LEU D 561
MASTER 613 0 11 108 56 0 0 617741 4 99 176
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