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HEADER HYDROLASE 27-MAY-09 3HLK
TITLE CRYSTAL STRUCTURE OF HUMAN MITOCHONDRIAL ACYL-COA
TITLE 2 THIOESTERASE (ACOT2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COENZYME A THIOESTERASE 2, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYL-COA THIOESTERASE 2, ACYL-COENZYME A THIOESTER
COMPND 5 HYDROLASE 2A, LONG-CHAIN ACYL-COA THIOESTERASE 2, ZAP128,
COMPND 6 CTE-IA;
COMPND 7 EC: 3.1.2.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACOT2, PTE2, PTE2A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, ALTERNATIVE SPLICING, HYDROLASE,
KEYWDS 2 MITOCHONDRION, POLYMORPHISM, SERINE ESTERASE, TRANSIT
KEYWDS 3 PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.MANDEL,B.TWEEL,L.TONG
REVDAT 1 23-JUN-09 3HLK 0
JRNL AUTH C.R.MANDEL,B.TWEEL,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN MITOCHONDRIAL ACYL-COA
JRNL TITL 2 THIOESTERASE (ACOT2)
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. 2009
JRNL REFN ESSN 1090-2104
JRNL PMID 19497300
JRNL DOI 10.1016/J.BBRC.2009.05.122
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 62312
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3310
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4262
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 442
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : -0.75000
REMARK 3 B12 (A**2) : 0.25000
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): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.697
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6557 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8903 ; 1.249 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 815 ; 5.939 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 288 ;31.446 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1065 ;15.743 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;17.690 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 957 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5066 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2811 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4344 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 463 ; 0.144 ; 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): 43 ; 0.277 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.194 ; 0.200
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): 4219 ; 0.800 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6558 ; 1.318 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2664 ; 1.734 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2345 ; 2.731 ; 4.500
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 : NULL
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
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 THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3HLK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
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 : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67802
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.0148
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.799
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHAKE&BAKE THEN SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 MM AMMONIUM CITRATE, 22%
REMARK 280 PEG3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 43.98333
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 87.96667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.96667
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 43.98333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 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 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 B 538 LIES ON A SPECIAL POSITION.
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 GLY A 46
REMARK 465 SER A 47
REMARK 465 PRO A 48
REMARK 465 GLN A 49
REMARK 465 LEU A 50
REMARK 465 ARG A 51
REMARK 465 GLN A 52
REMARK 465 VAL A 53
REMARK 465 GLY A 54
REMARK 465 GLN A 55
REMARK 465 ILE A 56
REMARK 465 ILE A 57
REMARK 465 LEU A 436
REMARK 465 HIS A 437
REMARK 465 ALA A 438
REMARK 465 LEU A 439
REMARK 465 VAL A 440
REMARK 465 GLY A 441
REMARK 465 SER A 442
REMARK 465 GLY A 473
REMARK 465 GLY A 474
REMARK 465 HIS A 475
REMARK 465 GLU A 476
REMARK 465 GLY A 477
REMARK 465 THR A 478
REMARK 465 ILE A 479
REMARK 465 PRO A 480
REMARK 465 SER A 481
REMARK 465 LYS A 482
REMARK 465 VAL A 483
REMARK 465 LEU A 484
REMARK 465 GLU A 485
REMARK 465 HIS A 486
REMARK 465 HIS A 487
REMARK 465 HIS A 488
REMARK 465 HIS A 489
REMARK 465 HIS A 490
REMARK 465 HIS A 491
REMARK 465 GLY B 46
REMARK 465 SER B 47
REMARK 465 PRO B 48
REMARK 465 GLN B 49
REMARK 465 LEU B 50
REMARK 465 ARG B 51
REMARK 465 GLN B 52
REMARK 465 VAL B 53
REMARK 465 GLY B 54
REMARK 465 GLN B 55
REMARK 465 ILE B 56
REMARK 465 HIS B 437
REMARK 465 ALA B 438
REMARK 465 LEU B 439
REMARK 465 VAL B 440
REMARK 465 GLY B 441
REMARK 465 GLY B 473
REMARK 465 GLY B 474
REMARK 465 HIS B 475
REMARK 465 GLU B 476
REMARK 465 GLY B 477
REMARK 465 THR B 478
REMARK 465 ILE B 479
REMARK 465 PRO B 480
REMARK 465 SER B 481
REMARK 465 LYS B 482
REMARK 465 VAL B 483
REMARK 465 LEU B 484
REMARK 465 GLU B 485
REMARK 465 HIS B 486
REMARK 465 HIS B 487
REMARK 465 HIS B 488
REMARK 465 HIS B 489
REMARK 465 HIS B 490
REMARK 465 HIS B 491
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 O ALA A 376 O HOH A 685 2.11
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 ASP A 353 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 356 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LEU B 100 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ASP B 353 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 366 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 459 CB - CG - OD2 ANGL. DEV. = 5.4 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 GLU A 91 19.89 59.24
REMARK 500 LEU A 152 -5.07 85.37
REMARK 500 GLU A 256 -127.77 46.89
REMARK 500 SER A 294 -130.06 56.19
REMARK 500 LYS A 330 -120.89 46.54
REMARK 500 THR A 347 147.76 -170.59
REMARK 500 ASP A 349 -151.25 -118.21
REMARK 500 TYR A 428 -2.68 67.82
REMARK 500 ARG B 74 109.67 -58.48
REMARK 500 TYR B 252 -8.18 -150.30
REMARK 500 GLU B 256 -130.72 56.60
REMARK 500 SER B 294 -136.39 68.79
REMARK 500 LYS B 330 -118.27 50.00
REMARK 500 THR B 347 143.89 -174.09
REMARK 500 PRO B 372 67.55 -69.08
REMARK 500 TYR B 428 -2.28 77.63
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 A 649 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH B 660 DISTANCE = 11.77 ANGSTROMS
REMARK 525 HOH B 684 DISTANCE = 9.91 ANGSTROMS
DBREF 3HLK A 46 483 UNP P49753 ACOT2_HUMAN 46 483
DBREF 3HLK B 46 483 UNP P49753 ACOT2_HUMAN 46 483
SEQADV 3HLK LEU A 484 UNP P49753 EXPRESSION TAG
SEQADV 3HLK GLU A 485 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 486 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 487 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 488 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 489 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 490 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS A 491 UNP P49753 EXPRESSION TAG
SEQADV 3HLK LEU B 484 UNP P49753 EXPRESSION TAG
SEQADV 3HLK GLU B 485 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 486 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 487 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 488 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 489 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 490 UNP P49753 EXPRESSION TAG
SEQADV 3HLK HIS B 491 UNP P49753 EXPRESSION TAG
SEQRES 1 A 446 GLY SER PRO GLN LEU ARG GLN VAL GLY GLN ILE ILE ARG
SEQRES 2 A 446 VAL PRO ALA ARG MSE ALA ALA THR LEU ILE LEU GLU PRO
SEQRES 3 A 446 ALA GLY ARG CYS CYS TRP ASP GLU PRO VAL ARG ILE ALA
SEQRES 4 A 446 VAL ARG GLY LEU ALA PRO GLU GLN PRO VAL THR LEU ARG
SEQRES 5 A 446 ALA SER LEU ARG ASP GLU LYS GLY ALA LEU PHE GLN ALA
SEQRES 6 A 446 HIS ALA ARG TYR ARG ALA ASP THR LEU GLY GLU LEU ASP
SEQRES 7 A 446 LEU GLU ARG ALA PRO ALA LEU GLY GLY SER PHE ALA GLY
SEQRES 8 A 446 LEU GLU PRO MSE GLY LEU LEU TRP ALA LEU GLU PRO GLU
SEQRES 9 A 446 LYS PRO LEU VAL ARG LEU VAL LYS ARG ASP VAL ARG THR
SEQRES 10 A 446 PRO LEU ALA VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP
SEQRES 11 A 446 PRO ASP PRO GLY ARG LEU LEU CYS GLN THR ARG HIS GLU
SEQRES 12 A 446 ARG TYR PHE LEU PRO PRO GLY VAL ARG ARG GLU PRO VAL
SEQRES 13 A 446 ARG VAL GLY ARG VAL ARG GLY THR LEU PHE LEU PRO PRO
SEQRES 14 A 446 GLU PRO GLY PRO PHE PRO GLY ILE VAL ASP MSE PHE GLY
SEQRES 15 A 446 THR GLY GLY GLY LEU LEU GLU TYR ARG ALA SER LEU LEU
SEQRES 16 A 446 ALA GLY LYS GLY PHE ALA VAL MSE ALA LEU ALA TYR TYR
SEQRES 17 A 446 ASN TYR GLU ASP LEU PRO LYS THR MSE GLU THR LEU HIS
SEQRES 18 A 446 LEU GLU TYR PHE GLU GLU ALA MSE ASN TYR LEU LEU SER
SEQRES 19 A 446 HIS PRO GLU VAL LYS GLY PRO GLY VAL GLY LEU LEU GLY
SEQRES 20 A 446 ILE SER LYS GLY GLY GLU LEU CYS LEU SER MSE ALA SER
SEQRES 21 A 446 PHE LEU LYS GLY ILE THR ALA ALA VAL VAL ILE ASN GLY
SEQRES 22 A 446 SER VAL ALA ASN VAL GLY GLY THR LEU ARG TYR LYS GLY
SEQRES 23 A 446 GLU THR LEU PRO PRO VAL GLY VAL ASN ARG ASN ARG ILE
SEQRES 24 A 446 LYS VAL THR LYS ASP GLY TYR ALA ASP ILE VAL ASP VAL
SEQRES 25 A 446 LEU ASN SER PRO LEU GLU GLY PRO ASP GLN LYS SER PHE
SEQRES 26 A 446 ILE PRO VAL GLU ARG ALA GLU SER THR PHE LEU PHE LEU
SEQRES 27 A 446 VAL GLY GLN ASP ASP HIS ASN TRP LYS SER GLU PHE TYR
SEQRES 28 A 446 ALA ASN GLU ALA CYS LYS ARG LEU GLN ALA HIS GLY ARG
SEQRES 29 A 446 ARG LYS PRO GLN ILE ILE CYS TYR PRO GLU THR GLY HIS
SEQRES 30 A 446 TYR ILE GLU PRO PRO TYR PHE PRO LEU CYS ARG ALA SER
SEQRES 31 A 446 LEU HIS ALA LEU VAL GLY SER PRO ILE ILE TRP GLY GLY
SEQRES 32 A 446 GLU PRO ARG ALA HIS ALA MSE ALA GLN VAL ASP ALA TRP
SEQRES 33 A 446 LYS GLN LEU GLN THR PHE PHE HIS LYS HIS LEU GLY GLY
SEQRES 34 A 446 HIS GLU GLY THR ILE PRO SER LYS VAL LEU GLU HIS HIS
SEQRES 35 A 446 HIS HIS HIS HIS
SEQRES 1 B 446 GLY SER PRO GLN LEU ARG GLN VAL GLY GLN ILE ILE ARG
SEQRES 2 B 446 VAL PRO ALA ARG MSE ALA ALA THR LEU ILE LEU GLU PRO
SEQRES 3 B 446 ALA GLY ARG CYS CYS TRP ASP GLU PRO VAL ARG ILE ALA
SEQRES 4 B 446 VAL ARG GLY LEU ALA PRO GLU GLN PRO VAL THR LEU ARG
SEQRES 5 B 446 ALA SER LEU ARG ASP GLU LYS GLY ALA LEU PHE GLN ALA
SEQRES 6 B 446 HIS ALA ARG TYR ARG ALA ASP THR LEU GLY GLU LEU ASP
SEQRES 7 B 446 LEU GLU ARG ALA PRO ALA LEU GLY GLY SER PHE ALA GLY
SEQRES 8 B 446 LEU GLU PRO MSE GLY LEU LEU TRP ALA LEU GLU PRO GLU
SEQRES 9 B 446 LYS PRO LEU VAL ARG LEU VAL LYS ARG ASP VAL ARG THR
SEQRES 10 B 446 PRO LEU ALA VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP
SEQRES 11 B 446 PRO ASP PRO GLY ARG LEU LEU CYS GLN THR ARG HIS GLU
SEQRES 12 B 446 ARG TYR PHE LEU PRO PRO GLY VAL ARG ARG GLU PRO VAL
SEQRES 13 B 446 ARG VAL GLY ARG VAL ARG GLY THR LEU PHE LEU PRO PRO
SEQRES 14 B 446 GLU PRO GLY PRO PHE PRO GLY ILE VAL ASP MSE PHE GLY
SEQRES 15 B 446 THR GLY GLY GLY LEU LEU GLU TYR ARG ALA SER LEU LEU
SEQRES 16 B 446 ALA GLY LYS GLY PHE ALA VAL MSE ALA LEU ALA TYR TYR
SEQRES 17 B 446 ASN TYR GLU ASP LEU PRO LYS THR MSE GLU THR LEU HIS
SEQRES 18 B 446 LEU GLU TYR PHE GLU GLU ALA MSE ASN TYR LEU LEU SER
SEQRES 19 B 446 HIS PRO GLU VAL LYS GLY PRO GLY VAL GLY LEU LEU GLY
SEQRES 20 B 446 ILE SER LYS GLY GLY GLU LEU CYS LEU SER MSE ALA SER
SEQRES 21 B 446 PHE LEU LYS GLY ILE THR ALA ALA VAL VAL ILE ASN GLY
SEQRES 22 B 446 SER VAL ALA ASN VAL GLY GLY THR LEU ARG TYR LYS GLY
SEQRES 23 B 446 GLU THR LEU PRO PRO VAL GLY VAL ASN ARG ASN ARG ILE
SEQRES 24 B 446 LYS VAL THR LYS ASP GLY TYR ALA ASP ILE VAL ASP VAL
SEQRES 25 B 446 LEU ASN SER PRO LEU GLU GLY PRO ASP GLN LYS SER PHE
SEQRES 26 B 446 ILE PRO VAL GLU ARG ALA GLU SER THR PHE LEU PHE LEU
SEQRES 27 B 446 VAL GLY GLN ASP ASP HIS ASN TRP LYS SER GLU PHE TYR
SEQRES 28 B 446 ALA ASN GLU ALA CYS LYS ARG LEU GLN ALA HIS GLY ARG
SEQRES 29 B 446 ARG LYS PRO GLN ILE ILE CYS TYR PRO GLU THR GLY HIS
SEQRES 30 B 446 TYR ILE GLU PRO PRO TYR PHE PRO LEU CYS ARG ALA SER
SEQRES 31 B 446 LEU HIS ALA LEU VAL GLY SER PRO ILE ILE TRP GLY GLY
SEQRES 32 B 446 GLU PRO ARG ALA HIS ALA MSE ALA GLN VAL ASP ALA TRP
SEQRES 33 B 446 LYS GLN LEU GLN THR PHE PHE HIS LYS HIS LEU GLY GLY
SEQRES 34 B 446 HIS GLU GLY THR ILE PRO SER LYS VAL LEU GLU HIS HIS
SEQRES 35 B 446 HIS HIS HIS HIS
MODRES 3HLK MSE A 63 MET SELENOMETHIONINE
MODRES 3HLK MSE A 140 MET SELENOMETHIONINE
MODRES 3HLK MSE A 225 MET SELENOMETHIONINE
MODRES 3HLK MSE A 248 MET SELENOMETHIONINE
MODRES 3HLK MSE A 262 MET SELENOMETHIONINE
MODRES 3HLK MSE A 274 MET SELENOMETHIONINE
MODRES 3HLK MSE A 303 MET SELENOMETHIONINE
MODRES 3HLK MSE A 455 MET SELENOMETHIONINE
MODRES 3HLK MSE B 63 MET SELENOMETHIONINE
MODRES 3HLK MSE B 140 MET SELENOMETHIONINE
MODRES 3HLK MSE B 225 MET SELENOMETHIONINE
MODRES 3HLK MSE B 248 MET SELENOMETHIONINE
MODRES 3HLK MSE B 262 MET SELENOMETHIONINE
MODRES 3HLK MSE B 274 MET SELENOMETHIONINE
MODRES 3HLK MSE B 303 MET SELENOMETHIONINE
MODRES 3HLK MSE B 455 MET SELENOMETHIONINE
HET MSE A 63 8
HET MSE A 140 8
HET MSE A 225 8
HET MSE A 248 8
HET MSE A 262 8
HET MSE A 274 8
HET MSE A 303 8
HET MSE A 455 8
HET MSE B 63 8
HET MSE B 140 8
HET MSE B 225 8
HET MSE B 248 8
HET MSE B 262 8
HET MSE B 274 8
HET MSE B 303 8
HET MSE B 455 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 HOH *441(H2 O)
HELIX 1 1 MSE A 140 ALA A 145 1 6
HELIX 2 2 GLU A 234 GLY A 242 1 9
HELIX 3 3 LEU A 267 SER A 279 1 13
HELIX 4 4 SER A 294 LEU A 307 1 14
HELIX 5 5 ASN A 340 ILE A 344 5 5
HELIX 6 6 GLU A 363 PHE A 370 5 8
HELIX 7 7 PRO A 372 ALA A 376 5 5
HELIX 8 8 LYS A 392 HIS A 407 1 16
HELIX 9 9 GLU A 449 LEU A 472 1 24
HELIX 10 10 MSE B 140 ALA B 145 1 6
HELIX 11 11 GLU B 234 GLY B 242 1 9
HELIX 12 12 LEU B 267 HIS B 280 1 14
HELIX 13 13 SER B 294 LEU B 307 1 14
HELIX 14 14 ASN B 340 ILE B 344 5 5
HELIX 15 15 GLU B 363 PHE B 370 5 8
HELIX 16 16 PRO B 372 ALA B 376 5 5
HELIX 17 17 LYS B 392 ALA B 406 1 15
HELIX 18 18 GLU B 449 LEU B 472 1 24
SHEET 1 A 3 THR A 66 GLU A 70 0
SHEET 2 A 3 ARG A 82 ARG A 86 -1 O ARG A 82 N GLU A 70
SHEET 3 A 3 LEU A 122 ASP A 123 -1 O LEU A 122 N VAL A 85
SHEET 1 B 6 CYS A 75 CYS A 76 0
SHEET 2 B 6 LEU A 181 TYR A 190 1 O TYR A 190 N CYS A 75
SHEET 3 B 6 LEU A 164 ASP A 172 -1 N VAL A 170 O LEU A 182
SHEET 4 B 6 PRO A 93 ARG A 101 -1 N THR A 95 O LEU A 171
SHEET 5 B 6 LEU A 107 ARG A 115 -1 O PHE A 108 N LEU A 100
SHEET 6 B 6 GLY A 131 GLY A 132 -1 O GLY A 131 N ARG A 113
SHEET 1 C 6 CYS A 75 CYS A 76 0
SHEET 2 C 6 LEU A 181 TYR A 190 1 O TYR A 190 N CYS A 75
SHEET 3 C 6 LEU A 164 ASP A 172 -1 N VAL A 170 O LEU A 182
SHEET 4 C 6 PRO A 93 ARG A 101 -1 N THR A 95 O LEU A 171
SHEET 5 C 6 LEU A 107 ARG A 115 -1 O PHE A 108 N LEU A 100
SHEET 6 C 6 GLU A 147 PRO A 148 -1 O GLU A 147 N GLN A 109
SHEET 1 D 8 ARG A 197 VAL A 203 0
SHEET 2 D 8 VAL A 206 LEU A 212 -1 O GLY A 208 N VAL A 201
SHEET 3 D 8 ALA A 246 LEU A 250 -1 O ALA A 249 N THR A 209
SHEET 4 D 8 GLY A 221 MSE A 225 1 N ASP A 224 O MSE A 248
SHEET 5 D 8 VAL A 288 ILE A 293 1 O LEU A 291 N VAL A 223
SHEET 6 D 8 ILE A 310 ILE A 316 1 O ILE A 316 N GLY A 292
SHEET 7 D 8 THR A 379 GLY A 385 1 O LEU A 383 N VAL A 315
SHEET 8 D 8 GLN A 413 TYR A 417 1 O ILE A 415 N PHE A 382
SHEET 1 E 3 THR A 264 HIS A 266 0
SHEET 2 E 3 THR A 326 TYR A 329 1 O THR A 326 N LEU A 265
SHEET 3 E 3 GLU A 332 LEU A 334 -1 O GLU A 332 N TYR A 329
SHEET 1 F 2 LYS A 345 VAL A 346 0
SHEET 2 F 2 ALA A 352 ASP A 353 -1 O ASP A 353 N LYS A 345
SHEET 1 G 3 THR B 66 GLU B 70 0
SHEET 2 G 3 ARG B 82 ARG B 86 -1 O ARG B 82 N GLU B 70
SHEET 3 G 3 LEU B 122 ASP B 123 -1 O LEU B 122 N VAL B 85
SHEET 1 H 7 CYS B 75 CYS B 76 0
SHEET 2 H 7 LEU B 181 TYR B 190 1 O TYR B 190 N CYS B 75
SHEET 3 H 7 LEU B 164 ASP B 172 -1 N VAL B 166 O HIS B 187
SHEET 4 H 7 PRO B 93 ARG B 101 -1 N THR B 95 O LEU B 171
SHEET 5 H 7 LEU B 107 ARG B 115 -1 O PHE B 108 N LEU B 100
SHEET 6 H 7 ALA B 129 GLY B 132 -1 O LEU B 130 N ARG B 113
SHEET 7 H 7 ALA B 135 GLY B 136 -1 O GLY B 136 N ALA B 129
SHEET 1 I 6 CYS B 75 CYS B 76 0
SHEET 2 I 6 LEU B 181 TYR B 190 1 O TYR B 190 N CYS B 75
SHEET 3 I 6 LEU B 164 ASP B 172 -1 N VAL B 166 O HIS B 187
SHEET 4 I 6 PRO B 93 ARG B 101 -1 N THR B 95 O LEU B 171
SHEET 5 I 6 LEU B 107 ARG B 115 -1 O PHE B 108 N LEU B 100
SHEET 6 I 6 GLU B 147 PRO B 148 -1 O GLU B 147 N GLN B 109
SHEET 1 J 8 ARG B 197 VAL B 203 0
SHEET 2 J 8 VAL B 206 LEU B 212 -1 O LEU B 212 N ARG B 197
SHEET 3 J 8 ALA B 246 LEU B 250 -1 O VAL B 247 N PHE B 211
SHEET 4 J 8 GLY B 221 MSE B 225 1 N ASP B 224 O LEU B 250
SHEET 5 J 8 VAL B 288 ILE B 293 1 O LEU B 291 N VAL B 223
SHEET 6 J 8 ILE B 310 ILE B 316 1 O ILE B 316 N GLY B 292
SHEET 7 J 8 THR B 379 GLY B 385 1 O LEU B 381 N VAL B 315
SHEET 8 J 8 GLN B 413 TYR B 417 1 O TYR B 417 N VAL B 384
SHEET 1 K 3 THR B 264 HIS B 266 0
SHEET 2 K 3 THR B 326 TYR B 329 1 O THR B 326 N LEU B 265
SHEET 3 K 3 GLU B 332 LEU B 334 -1 O GLU B 332 N TYR B 329
SHEET 1 L 2 LYS B 345 VAL B 346 0
SHEET 2 L 2 ALA B 352 ASP B 353 -1 O ASP B 353 N LYS B 345
SHEET 1 M 2 ALA B 434 SER B 435 0
SHEET 2 M 2 ILE B 444 ILE B 445 -1 O ILE B 444 N SER B 435
LINK C ARG A 62 N MSE A 63 1555 1555 1.33
LINK C MSE A 63 N ALA A 64 1555 1555 1.33
LINK C PRO A 139 N MSE A 140 1555 1555 1.34
LINK C MSE A 140 N GLY A 141 1555 1555 1.33
LINK C ASP A 224 N MSE A 225 1555 1555 1.33
LINK C MSE A 225 N PHE A 226 1555 1555 1.33
LINK C VAL A 247 N MSE A 248 1555 1555 1.33
LINK C MSE A 248 N ALA A 249 1555 1555 1.33
LINK C THR A 261 N MSE A 262 1555 1555 1.33
LINK C MSE A 262 N GLU A 263 1555 1555 1.34
LINK C ALA A 273 N MSE A 274 1555 1555 1.33
LINK C MSE A 274 N ASN A 275 1555 1555 1.33
LINK C SER A 302 N MSE A 303 1555 1555 1.34
LINK C MSE A 303 N ALA A 304 1555 1555 1.33
LINK C ALA A 454 N MSE A 455 1555 1555 1.33
LINK C MSE A 455 N ALA A 456 1555 1555 1.34
LINK C ARG B 62 N MSE B 63 1555 1555 1.33
LINK C MSE B 63 N ALA B 64 1555 1555 1.33
LINK C PRO B 139 N MSE B 140 1555 1555 1.34
LINK C MSE B 140 N GLY B 141 1555 1555 1.32
LINK C ASP B 224 N MSE B 225 1555 1555 1.33
LINK C MSE B 225 N PHE B 226 1555 1555 1.32
LINK C VAL B 247 N MSE B 248 1555 1555 1.33
LINK C MSE B 248 N ALA B 249 1555 1555 1.33
LINK C THR B 261 N MSE B 262 1555 1555 1.33
LINK C MSE B 262 N GLU B 263 1555 1555 1.33
LINK C ALA B 273 N MSE B 274 1555 1555 1.32
LINK C MSE B 274 N ASN B 275 1555 1555 1.33
LINK C SER B 302 N MSE B 303 1555 1555 1.33
LINK C MSE B 303 N ALA B 304 1555 1555 1.33
LINK C ALA B 454 N MSE B 455 1555 1555 1.34
LINK C MSE B 455 N ALA B 456 1555 1555 1.33
CISPEP 1 GLU A 70 PRO A 71 0 -3.17
CISPEP 2 GLU A 215 PRO A 216 0 2.89
CISPEP 3 GLY A 217 PRO A 218 0 0.88
CISPEP 4 GLY A 285 PRO A 286 0 9.22
CISPEP 5 THR A 347 LYS A 348 0 -12.17
CISPEP 6 GLU B 70 PRO B 71 0 -6.27
CISPEP 7 GLU B 215 PRO B 216 0 8.79
CISPEP 8 GLY B 217 PRO B 218 0 -3.67
CISPEP 9 GLY B 285 PRO B 286 0 0.40
CISPEP 10 THR B 347 LYS B 348 0 -11.98
CRYST1 124.557 124.557 131.950 90.00 90.00 120.00 P 31 2 1 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 0.008028 0.004635 0.000000 0.00000
SCALE2 0.000000 0.009270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007579 0.00000
TER 3184 LEU A 472
TER 6390 LEU B 472
MASTER 419 0 16 18 59 0 0 6 6829 2 160 70
END |