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HEADER HYDROLASE 27-SEP-19 6UH8
TITLE CRYSTAL STRUCTURE OF DAD2 N242I MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DECREASED APICAL DOMINANCE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAD2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE 3 ORGANISM_COMMON: PETUNIA;
SOURCE 4 ORGANISM_TAXID: 4102;
SOURCE 5 GENE: DAD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2
KEYWDS STRIGOLACTONE RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SHARMA,C.HAMIAUX,K.C.SNOWDEN
REVDAT 1 26-FEB-20 6UH8 0
JRNL AUTH H.W.LEE,P.SHARMA,B.J.JANSSEN,R.S.M.DRUMMOND,Z.LUO,C.HAMIAUX,
JRNL AUTH 2 T.COLLIER,J.R.ALLISON,R.D.NEWCOMB,K.C.SNOWDEN
JRNL TITL FLEXIBILITY OF THE PETUNIA STRIGOLACTONE RECEPTOR DAD2
JRNL TITL 2 PROMOTES ITS INTERACTION WITH SIGNALING PARTNERS
JRNL REF J.BIOL.CHEM. 2020
JRNL REFN ESSN 1083-351X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
REMARK 1 AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
REMARK 1 TITL DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE
REMARK 1 TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE.
REMARK 1 REF CURR. BIOL. V. 22 2032 2012
REMARK 1 REFN ISSN 1879-0445
REMARK 1 PMID 22959345
REMARK 1 DOI 10.1016/J.CUB.2012.08.007
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 128380
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 9970
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 709
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.48000
REMARK 3 B22 (A**2) : 1.48000
REMARK 3 B33 (A**2) : -4.81000
REMARK 3 B12 (A**2) : 0.74000
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): 0.053
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.854
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4459 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4144 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6085 ; 1.740 ; 1.629
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9544 ; 1.569 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 560 ; 5.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 247 ;26.711 ;20.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 696 ;11.974 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;21.060 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 555 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5090 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1045 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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): 8603 ; 3.782 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 313 ;41.638 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8623 ;25.257 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 265 B 2 265 8537 0.100 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 265
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 37.605 3.173 -4.278
REMARK 3 T TENSOR
REMARK 3 T11: 0.0030 T22: 0.0007
REMARK 3 T33: 0.0873 T12: 0.0004
REMARK 3 T13: -0.0000 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0341
REMARK 3 L33: 0.0017 L12: 0.0047
REMARK 3 L13: -0.0010 L23: -0.0076
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0000 S13: 0.0007
REMARK 3 S21: 0.0019 S22: -0.0003 S23: 0.0077
REMARK 3 S31: -0.0003 S32: 0.0001 S33: -0.0007
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 265
REMARK 3 RESIDUE RANGE : B 301 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): 53.193 35.660 -10.737
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0010
REMARK 3 T33: 0.0820 T12: -0.0000
REMARK 3 T13: 0.0003 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.0545 L22: 0.0147
REMARK 3 L33: 0.0129 L12: -0.0065
REMARK 3 L13: 0.0096 L23: 0.0072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0000 S12: 0.0072 S13: 0.0048
REMARK 3 S21: 0.0000 S22: -0.0014 S23: 0.0011
REMARK 3 S31: 0.0001 S32: 0.0006 S33: 0.0014
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6UH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1000244603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953736
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.31
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138411
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 45.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.10
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 18.90
REMARK 200 R MERGE FOR SHELL (I) : 2.18800
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 2.7.17
REMARK 200 STARTING MODEL: 4DNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5 1.58-1.72 M MGSO4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 66.50933
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 33.25467
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 49.88200
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 16.62733
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 83.13667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 HIS A 266
REMARK 465 ARG A 267
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 HIS B 266
REMARK 465 ARG B 267
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 HOH B 515 O HOH B 599 2.05
REMARK 500 OE1 GLN A 258 O HOH A 401 2.13
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 GLY A 2 N GLY A 2 CA 0.100
REMARK 500 ARG A 108 CD ARG A 108 NE -0.145
REMARK 500 GLY B 2 N GLY B 2 CA 0.143
REMARK 500 GLU B 173 CD GLU B 173 OE2 0.077
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 A 36 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -4.4 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 SER A 96 -119.70 43.40
REMARK 500 ARG A 124 121.72 -172.03
REMARK 500 ASN A 150 92.32 -160.82
REMARK 500 ARG A 216 87.73 -157.07
REMARK 500 ALA A 252 53.05 -140.50
REMARK 500 SER B 96 -120.39 44.74
REMARK 500 ARG B 124 121.16 -174.70
REMARK 500 ASN B 150 98.49 -167.26
REMARK 500 ALA B 252 57.06 -144.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG B 216 -14.98
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 598 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B 642 DISTANCE = 6.01 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 MG B 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 10 OD1
REMARK 620 2 HOH B 421 O 94.5
REMARK 620 3 HOH B 473 O 78.7 93.3
REMARK 620 4 HOH B 550 O 87.0 175.9 90.7
REMARK 620 5 HOH B 571 O 94.3 85.7 172.9 90.4
REMARK 620 6 HOH B 629 O 174.1 89.9 97.1 88.8 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 72 OD2
REMARK 620 2 HOH A 419 O 89.3
REMARK 620 3 HOH A 431 O 89.8 84.2
REMARK 620 4 HOH A 569 O 174.1 96.0 93.4
REMARK 620 5 HOH B 420 O 89.1 175.0 91.1 85.8
REMARK 620 6 HOH B 429 O 88.8 89.6 173.7 88.6 95.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 408 O
REMARK 620 2 HOH A 413 O 84.9
REMARK 620 3 HOH A 588 O 87.1 93.3
REMARK 620 4 HOH B 613 O 89.0 173.8 85.6
REMARK 620 5 HOH B 415 O 93.4 86.4 179.4 94.7
REMARK 620 6 HOH B 408 O 171.3 101.6 98.3 84.5 81.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 472 O
REMARK 620 2 HOH B 639 O 90.9
REMARK 620 3 HOH B 477 O 93.6 175.5
REMARK 620 4 HOH B 615 O 94.2 95.9 83.5
REMARK 620 5 HOH B 507 O 89.1 90.3 90.1 173.0
REMARK 620 6 HOH B 633 O 177.3 86.4 89.1 85.8 91.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 305 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 587 O
REMARK 620 2 HOH B 642 O 101.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 515 O
REMARK 620 2 HOH B 422 O 60.6
REMARK 620 3 HOH B 599 O 44.8 53.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 307 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 450 O
REMARK 620 2 HOH B 619 O 87.6
REMARK 620 3 HOH B 623 O 165.7 78.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 311
DBREF 6UH8 A -1 267 UNP L7MTK5 L7MTK5_PETHY 1 269
DBREF 6UH8 B -1 267 UNP L7MTK5 L7MTK5_PETHY 1 269
SEQADV 6UH8 GLN A 89 UNP L7MTK5 CYS 91 ENGINEERED MUTATION
SEQADV 6UH8 ILE A 242 UNP L7MTK5 ASN 244 ENGINEERED MUTATION
SEQADV 6UH8 GLN B 89 UNP L7MTK5 CYS 91 ENGINEERED MUTATION
SEQADV 6UH8 ILE B 242 UNP L7MTK5 ASN 244 ENGINEERED MUTATION
SEQRES 1 A 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 A 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 A 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 A 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 A 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 A 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 A 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES 8 A 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 A 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 A 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 A 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 A 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 A 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 A 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 A 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 A 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 A 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 A 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ILE ILE GLU GLY
SEQRES 20 A 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 A 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES 1 B 269 GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES 2 B 269 ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES 3 B 269 HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES 4 B 269 LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES 5 B 269 ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES 6 B 269 ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES 7 B 269 ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES 8 B 269 CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES 9 B 269 ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES 10 B 269 LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES 11 B 269 GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES 12 B 269 LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES 13 B 269 VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES 14 B 269 PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 B 269 MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES 16 B 269 PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES 17 B 269 VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES 18 B 269 VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES 19 B 269 GLY GLY LYS ASN THR VAL HIS TRP LEU ILE ILE GLU GLY
SEQRES 20 B 269 HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES 21 B 269 GLU LEU ARG ARG ALA LEU SER HIS ARG
HET MES A 301 12
HET MG A 302 1
HET GOL A 303 6
HET MES B 301 12
HET MG B 302 1
HET MG B 303 1
HET MG B 304 1
HET MG B 305 1
HET MG B 306 1
HET MG B 307 1
HET SO4 B 308 5
HET SO4 B 309 5
HET SO4 B 310 5
HET GOL B 311 6
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MES 2(C6 H13 N O4 S)
FORMUL 4 MG 7(MG 2+)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 13 SO4 3(O4 S 2-)
FORMUL 17 HOH *440(H2 O)
HELIX 1 AA1 GLY A 2 LEU A 9 1 8
HELIX 2 AA2 ASP A 30 ASN A 35 5 6
HELIX 3 AA3 ILE A 37 LEU A 42 5 6
HELIX 4 AA4 ASN A 59 PHE A 63 5 5
HELIX 5 AA5 LEU A 71 LEU A 85 1 15
HELIX 6 AA6 SER A 96 ARG A 109 1 14
HELIX 7 AA7 GLU A 136 ASN A 150 1 15
HELIX 8 AA8 ASN A 150 GLY A 164 1 15
HELIX 9 AA9 VAL A 167 MET A 181 1 15
HELIX 10 AB1 ARG A 182 ASN A 195 1 14
HELIX 11 AB2 MET A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 ALA A 252 1 6
HELIX 14 AB5 ALA A 252 SER A 265 1 14
HELIX 15 AB6 GLN B 3 LEU B 9 1 7
HELIX 16 AB7 ASP B 30 ASN B 35 5 6
HELIX 17 AB8 ILE B 37 PHE B 41 5 5
HELIX 18 AB9 ASN B 59 PHE B 63 5 5
HELIX 19 AC1 LEU B 71 LEU B 85 1 15
HELIX 20 AC2 SER B 96 ARG B 109 1 14
HELIX 21 AC3 GLU B 136 ASN B 150 1 15
HELIX 22 AC4 ASN B 150 GLY B 164 1 15
HELIX 23 AC5 VAL B 167 MET B 181 1 15
HELIX 24 AC6 ARG B 182 ASN B 195 1 14
HELIX 25 AC7 MET B 198 VAL B 205 5 8
HELIX 26 AC8 PRO B 221 LEU B 232 1 12
HELIX 27 AC9 LEU B 247 ALA B 252 1 6
HELIX 28 AD1 ALA B 252 SER B 265 1 14
SHEET 1 AA1 7 ARG A 12 VAL A 14 0
SHEET 2 AA1 7 TYR A 45 TYR A 50 -1 O VAL A 47 N VAL A 14
SHEET 3 AA1 7 ARG A 19 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N ALA A 24
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 AA1 7 CYS A 209 ARG A 216 1 O PHE A 212 N LEU A 118
SHEET 7 AA1 7 ASN A 236 GLU A 244 1 O HIS A 239 N ILE A 211
SHEET 1 AA2 7 ARG B 12 VAL B 14 0
SHEET 2 AA2 7 TYR B 45 TYR B 50 -1 O VAL B 47 N VAL B 14
SHEET 3 AA2 7 ARG B 19 ALA B 24 1 N LEU B 21 O VAL B 48
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N ALA B 24
SHEET 5 AA2 7 PHE B 113 ILE B 119 1 O ILE B 117 N TYR B 92
SHEET 6 AA2 7 CYS B 209 THR B 214 1 O PHE B 212 N LEU B 118
SHEET 7 AA2 7 ASN B 236 LEU B 241 1 O HIS B 239 N ILE B 211
LINK OD1 ASN B 10 MG MG B 304 1555 1555 2.06
LINK OD2 ASP B 72 MG MG B 303 1555 1555 2.08
LINK MG MG A 302 O HOH A 408 1555 1555 2.32
LINK MG MG A 302 O HOH A 413 1555 1555 1.92
LINK MG MG A 302 O HOH A 588 1555 1555 1.89
LINK MG MG A 302 O HOH B 613 1555 1555 1.97
LINK MG MG A 302 O HOH B 415 1555 1555 2.08
LINK MG MG A 302 O HOH B 408 1555 1555 2.26
LINK MG MG B 302 O HOH B 472 1555 1555 2.11
LINK MG MG B 302 O HOH B 639 1555 1555 2.00
LINK MG MG B 302 O HOH B 477 1555 1555 2.01
LINK MG MG B 302 O HOH B 615 1555 1555 2.06
LINK MG MG B 302 O HOH B 507 1555 1555 2.10
LINK MG MG B 302 O HOH B 633 1555 1555 2.17
LINK MG MG B 303 O HOH A 419 1555 1555 2.23
LINK MG MG B 303 O HOH A 431 1555 1555 2.11
LINK MG MG B 303 O HOH A 569 1555 1555 2.07
LINK MG MG B 303 O HOH B 420 1555 1555 2.22
LINK MG MG B 303 O HOH B 429 1555 1555 2.05
LINK MG MG B 304 O HOH B 421 1555 1555 2.10
LINK MG MG B 304 O HOH B 473 1555 1555 2.21
LINK MG MG B 304 O HOH B 550 1555 1555 2.17
LINK MG MG B 304 O HOH B 571 1555 1555 2.00
LINK MG MG B 304 O HOH B 629 1555 1555 2.15
LINK MG MG B 305 O HOH B 587 1555 1555 2.11
LINK MG MG B 305 O HOH B 642 1555 1555 2.35
LINK MG MG B 306 O HOH B 515 1555 1555 2.91
LINK MG MG B 306 O HOH B 422 1555 1555 2.75
LINK MG MG B 306 O HOH B 599 1555 1555 2.04
LINK MG MG B 307 O HOH B 450 1555 1555 2.25
LINK MG MG B 307 O HOH B 619 1555 1555 2.34
LINK MG MG B 307 O HOH B 623 1555 1555 1.99
SITE 1 AC1 11 SER A 96 PHE A 125 PHE A 135 PHE A 158
SITE 2 AC1 11 VAL A 193 PHE A 194 SER A 219 HIS A 246
SITE 3 AC1 11 HOH A 433 HOH A 445 HOH A 531
SITE 1 AC2 6 HOH A 408 HOH A 413 HOH A 588 HOH B 408
SITE 2 AC2 6 HOH B 415 HOH B 613
SITE 1 AC3 6 TYR A 131 HIS A 132 SER A 223 VAL A 224
SITE 2 AC3 6 TYR A 227 HOH A 493
SITE 1 AC4 10 SER B 96 PHE B 125 PHE B 135 PHE B 158
SITE 2 AC4 10 PHE B 194 SER B 219 HIS B 246 HOH B 406
SITE 3 AC4 10 HOH B 460 HOH B 509
SITE 1 AC5 6 HOH B 472 HOH B 477 HOH B 507 HOH B 615
SITE 2 AC5 6 HOH B 633 HOH B 639
SITE 1 AC6 6 HOH A 419 HOH A 431 HOH A 569 ASP B 72
SITE 2 AC6 6 HOH B 420 HOH B 429
SITE 1 AC7 6 ASN B 10 HOH B 421 HOH B 473 HOH B 550
SITE 2 AC7 6 HOH B 571 HOH B 629
SITE 1 AC8 2 HOH B 587 HOH B 642
SITE 1 AC9 3 HOH B 422 HOH B 515 HOH B 599
SITE 1 AD1 4 HIS B 231 HOH B 450 HOH B 619 HOH B 623
SITE 1 AD2 7 PRO B 221 ALA B 222 SER B 223 HOH B 477
SITE 2 AD2 7 HOH B 507 HOH B 516 HOH B 521
SITE 1 AD3 4 HOH A 417 ARG B 108 ARG B 109 HOH B 537
SITE 1 AD4 6 ARG B 36 ALA B 252 PRO B 253 THR B 254
SITE 2 AD4 6 HOH B 404 HOH B 481
SITE 1 AD5 5 GLU B 18 TYR B 131 HIS B 132 SER B 223
SITE 2 AD5 5 VAL B 224
CRYST1 133.736 133.736 99.764 90.00 90.00 120.00 P 65 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 0.007477 0.004317 0.000000 0.00000
SCALE2 0.000000 0.008634 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010024 0.00000
TER 2176 SER A 265
TER 4296 SER B 265
MASTER 564 0 14 28 14 0 26 6 4640 2 94 42
END |