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HEADER HYDROLASE 13-AUG-18 6AGQ
TITLE ACETYL XYLAN ESTERASE FROM PAENIBACILLUS SP. R4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAENIBACILLUS SP. R4;
SOURCE 3 ORGANISM_TAXID: 1079050;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PAENIBACILLUS SP., ACETYL ESTERASE, ACETYL XYLAN ESTERASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PARK,C.W.LEE,J.H.LEE
REVDAT 1 10-OCT-18 6AGQ 0
JRNL AUTH S.PARK,C.W.LEE,J.H.LEE
JRNL TITL ACETYL XYLAN ESTERASE FROM PAENIBACILLUS SP. R4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 115533
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6247
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) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8000
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 439
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 767
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
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): 0.237
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.481
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15510 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 13836 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21096 ; 1.806 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32106 ; 1.090 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1890 ; 7.058 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 750 ;34.505 ;23.360
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2400 ;15.252 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 102 ;15.962 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2172 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17502 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3336 ; 0.002 ; 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): 7578 ; 2.897 ; 3.365
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7577 ; 2.896 ; 3.364
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9462 ; 3.969 ; 5.036
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9463 ; 3.969 ; 5.037
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7932 ; 3.673 ; 3.804
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7933 ; 3.673 ; 3.804
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11635 ; 5.587 ; 5.541
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 17548 ; 7.128 ;39.737
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 17416 ; 7.094 ;39.592
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 : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6AGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300008721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121844
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.2000
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) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE, POTASSIUM PHOSPHATE DIBASIC PH 5.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 76.89850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.82950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 76.89850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 70.82950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -278.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 PRO A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 ASP A 5
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ASN B 3
REMARK 465 VAL B 4
REMARK 465 ASP B 5
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 ASN C 3
REMARK 465 VAL C 4
REMARK 465 ASP C 5
REMARK 465 MET D 1
REMARK 465 PRO D 2
REMARK 465 ASN D 3
REMARK 465 VAL D 4
REMARK 465 ASP D 5
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 ASN E 3
REMARK 465 VAL E 4
REMARK 465 ASP E 5
REMARK 465 MET F 1
REMARK 465 PRO F 2
REMARK 465 ASN F 3
REMARK 465 VAL F 4
REMARK 465 ASP F 5
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 C 514 O HOH C 623 2.08
REMARK 500 O HOH F 541 O HOH F 578 2.19
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 B 235 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 248 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP E 160 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP E 160 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP F 160 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG F 171 NE - CZ - NH1 ANGL. DEV. = 3.7 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 -5.50 88.10
REMARK 500 GLN A 123 -148.06 -89.93
REMARK 500 SER A 185 -119.16 63.05
REMARK 500 PHE A 208 67.64 28.90
REMARK 500 ASP A 237 68.29 -163.72
REMARK 500 LYS B 53 -20.41 71.45
REMARK 500 SER B 96 -5.07 87.51
REMARK 500 GLN B 123 -157.74 -86.15
REMARK 500 SER B 185 -117.26 65.55
REMARK 500 PHE B 208 63.68 27.85
REMARK 500 ASP B 237 66.28 -163.90
REMARK 500 ASP C 49 35.77 72.27
REMARK 500 LYS C 53 -24.72 81.51
REMARK 500 SER C 96 -5.06 94.19
REMARK 500 ARG C 99 -9.61 -51.74
REMARK 500 SER C 185 -122.75 67.60
REMARK 500 PHE C 208 68.22 13.79
REMARK 500 ASP C 237 65.97 -163.69
REMARK 500 SER D 96 -2.90 87.30
REMARK 500 SER D 185 -115.92 55.30
REMARK 500 PHE D 208 66.26 16.05
REMARK 500 LEU D 211 43.02 70.00
REMARK 500 ASP D 237 68.39 -153.45
REMARK 500 LYS E 53 -27.70 77.82
REMARK 500 SER E 96 -6.62 88.12
REMARK 500 ARG E 99 -5.78 -58.66
REMARK 500 GLN E 123 -153.70 -91.47
REMARK 500 SER E 185 -117.16 61.02
REMARK 500 PHE E 208 63.91 28.09
REMARK 500 LEU E 211 31.02 72.02
REMARK 500 ASP E 237 63.23 -163.09
REMARK 500 ASN F 45 111.10 -163.59
REMARK 500 ASP F 49 62.94 33.49
REMARK 500 SER F 96 -0.88 83.39
REMARK 500 ARG F 99 -9.55 -59.03
REMARK 500 GLN F 123 -154.46 -98.03
REMARK 500 SER F 185 -119.75 69.34
REMARK 500 PHE F 208 68.28 22.84
REMARK 500 HIS F 213 75.80 44.43
REMARK 500 ASP F 237 73.08 -161.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 401
DBREF 6AGQ A 1 321 PDB 6AGQ 6AGQ 1 321
DBREF 6AGQ B 1 321 PDB 6AGQ 6AGQ 1 321
DBREF 6AGQ C 1 321 PDB 6AGQ 6AGQ 1 321
DBREF 6AGQ D 1 321 PDB 6AGQ 6AGQ 1 321
DBREF 6AGQ E 1 321 PDB 6AGQ 6AGQ 1 321
DBREF 6AGQ F 1 321 PDB 6AGQ 6AGQ 1 321
SEQRES 1 A 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 A 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 A 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 A 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 A 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 A 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 A 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 A 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 A 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 A 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 A 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 A 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 A 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 A 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 A 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 A 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 A 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 A 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 A 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 A 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 A 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 A 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 A 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 A 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 A 321 MET MET ARG PHE ILE GLU ALA TYR LEU
SEQRES 1 B 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 B 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 B 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 B 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 B 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 B 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 B 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 B 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 B 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 B 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 B 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 B 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 B 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 B 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 B 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 B 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 B 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 B 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 B 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 B 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 B 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 B 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 B 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 B 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 B 321 MET MET ARG PHE ILE GLU ALA TYR LEU
SEQRES 1 C 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 C 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 C 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 C 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 C 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 C 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 C 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 C 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 C 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 C 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 C 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 C 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 C 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 C 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 C 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 C 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 C 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 C 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 C 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 C 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 C 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 C 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 C 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 C 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 C 321 MET MET ARG PHE ILE GLU ALA TYR LEU
SEQRES 1 D 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 D 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 D 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 D 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 D 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 D 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 D 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 D 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 D 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 D 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 D 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 D 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 D 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 D 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 D 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 D 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 D 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 D 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 D 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 D 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 D 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 D 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 D 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 D 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 D 321 MET MET ARG PHE ILE GLU ALA TYR LEU
SEQRES 1 E 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 E 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 E 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 E 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 E 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 E 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 E 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 E 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 E 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 E 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 E 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 E 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 E 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 E 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 E 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 E 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 E 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 E 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 E 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 E 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 E 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 E 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 E 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 E 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 E 321 MET MET ARG PHE ILE GLU ALA TYR LEU
SEQRES 1 F 321 MET PRO ASN VAL ASP MET PRO LEU SER GLN LEU GLN ASP
SEQRES 2 F 321 TYR LYS PRO GLU LEU THR ASN GLU THR ASP PHE ASP LEU
SEQRES 3 F 321 PHE TRP ASP ASN ALA LYS ALA LEU SER ASN GLN LYS PRO
SEQRES 4 F 321 LEU HIS ALA GLN VAL ASN LEU VAL GLN ASP TYR PRO LEU
SEQRES 5 F 321 LYS SER ILE SER ILE TYR ASP VAL VAL TYR ASP GLY ALA
SEQRES 6 F 321 ASP GLY THR PRO ILE HIS GLY TRP TYR VAL THR PRO LYS
SEQRES 7 F 321 GLY GLU HIS GLN PRO GLY SER LEU PRO VAL LEU VAL LYS
SEQRES 8 F 321 TYR HIS GLY TYR SER GLY ASN ARG GLY TYR PRO ASN GLU
SEQRES 9 F 321 LEU LEU GLN TRP ALA SER MET GLY MET ALA ALA LEU ALA
SEQRES 10 F 321 ILE ASP VAL ARG GLY GLN GLY GLY VAL THR PRO ASP ARG
SEQRES 11 F 321 ALA GLU TYR PRO GLN GLY GLY ILE PRO GLY TRP MET THR
SEQRES 12 F 321 LEU GLY ILE LEU ASP PRO ALA SER TYR TYR TYR LYS GLN
SEQRES 13 F 321 VAL TYR LEU ASP CYS ILE ARG ALA LEU ASP PHE VAL CYS
SEQRES 14 F 321 SER ARG GLU GLU VAL ASP ALA SER ARG ILE ALA VAL TYR
SEQRES 15 F 321 GLY GLY SER GLN GLY GLY GLY LEU ALA LEU ALA ALA ALA
SEQRES 16 F 321 GLY LEU ASP SER ARG PRO LYS LEU ALA LEU PRO VAL PHE
SEQRES 17 F 321 PRO PHE LEU CYS HIS PHE ARG ARG SER VAL GLU ILE HIS
SEQRES 18 F 321 ALA SER GLY PRO TYR VAL GLU ILE LYS ASN TRP PHE ARG
SEQRES 19 F 321 ARG TYR ASP PRO GLU HIS ARG GLN GLU GLU GLN VAL TYR
SEQRES 20 F 321 ARG THR LEU SER TYR PHE ASP GLY MET ASN MET ALA SER
SEQRES 21 F 321 ARG ILE LYS ALA ARG THR LEU MET ALA ILE THR LEU GLN
SEQRES 22 F 321 ASP ILE THR CYS PRO PRO SER THR CYS PHE ALA ALA TYR
SEQRES 23 F 321 ASN HIS LEU ALA GLY PRO LYS GLU VAL ARG LEU TYR HIS
SEQRES 24 F 321 ASP TYR GLY HIS GLU GLY LEU PRO PHE HIS GLU GLU ALA
SEQRES 25 F 321 MET MET ARG PHE ILE GLU ALA TYR LEU
HET ZN A 401 1
HET ZN B 401 1
HET ZN C 401 1
HET ZN D 401 1
HET ZN E 401 1
HET ZN F 401 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 6(ZN 2+)
FORMUL 13 HOH *767(H2 O)
HELIX 1 AA1 PRO A 7 GLN A 12 1 6
HELIX 2 AA2 ASP A 23 GLN A 37 1 15
HELIX 3 AA3 TYR A 101 GLU A 104 5 4
HELIX 4 AA4 LEU A 105 MET A 111 1 7
HELIX 5 AA5 ASP A 148 SER A 151 5 4
HELIX 6 AA6 TYR A 152 ARG A 171 1 20
HELIX 7 AA7 SER A 185 ASP A 198 1 14
HELIX 8 AA8 HIS A 213 ILE A 220 1 8
HELIX 9 AA9 PRO A 225 ASP A 237 1 13
HELIX 10 AB1 GLN A 242 TYR A 252 1 11
HELIX 11 AB2 ASP A 254 SER A 260 1 7
HELIX 12 AB3 PRO A 278 ASN A 287 1 10
HELIX 13 AB4 PHE A 308 LEU A 321 1 14
HELIX 14 AB5 PRO B 7 ASP B 13 1 7
HELIX 15 AB6 ASP B 23 GLN B 37 1 15
HELIX 16 AB7 TYR B 101 GLU B 104 5 4
HELIX 17 AB8 LEU B 105 MET B 111 1 7
HELIX 18 AB9 ASP B 148 SER B 151 5 4
HELIX 19 AC1 TYR B 152 SER B 170 1 19
HELIX 20 AC2 SER B 185 ASP B 198 1 14
HELIX 21 AC3 HIS B 213 ILE B 220 1 8
HELIX 22 AC4 SER B 223 PRO B 225 5 3
HELIX 23 AC5 TYR B 226 ASP B 237 1 12
HELIX 24 AC6 GLN B 242 TYR B 252 1 11
HELIX 25 AC7 ASP B 254 SER B 260 1 7
HELIX 26 AC8 PRO B 278 ASN B 287 1 10
HELIX 27 AC9 PHE B 308 LEU B 321 1 14
HELIX 28 AD1 PRO C 7 ASP C 13 1 7
HELIX 29 AD2 ASP C 23 GLN C 37 1 15
HELIX 30 AD3 TYR C 101 GLU C 104 5 4
HELIX 31 AD4 LEU C 105 MET C 111 1 7
HELIX 32 AD5 TYR C 152 SER C 170 1 19
HELIX 33 AD6 SER C 185 ASP C 198 1 14
HELIX 34 AD7 HIS C 213 ILE C 220 1 8
HELIX 35 AD8 SER C 223 PRO C 225 5 3
HELIX 36 AD9 TYR C 226 ASP C 237 1 12
HELIX 37 AE1 GLN C 242 TYR C 252 1 11
HELIX 38 AE2 ASP C 254 SER C 260 1 7
HELIX 39 AE3 PRO C 278 ASN C 287 1 10
HELIX 40 AE4 LEU C 306 LEU C 321 1 16
HELIX 41 AE5 PRO D 7 ASP D 13 1 7
HELIX 42 AE6 ASP D 23 LYS D 38 1 16
HELIX 43 AE7 TYR D 101 GLU D 104 5 4
HELIX 44 AE8 LEU D 105 MET D 111 1 7
HELIX 45 AE9 TYR D 152 SER D 170 1 19
HELIX 46 AF1 SER D 185 ASP D 198 1 14
HELIX 47 AF2 HIS D 213 ILE D 220 1 8
HELIX 48 AF3 SER D 223 PRO D 225 5 3
HELIX 49 AF4 TYR D 226 ASP D 237 1 12
HELIX 50 AF5 GLN D 242 TYR D 252 1 11
HELIX 51 AF6 ASP D 254 SER D 260 1 7
HELIX 52 AF7 PRO D 278 ASN D 287 1 10
HELIX 53 AF8 LEU D 306 LEU D 321 1 16
HELIX 54 AF9 PRO E 7 GLN E 12 1 6
HELIX 55 AG1 ASP E 23 GLN E 37 1 15
HELIX 56 AG2 TYR E 101 GLU E 104 5 4
HELIX 57 AG3 LEU E 105 MET E 111 1 7
HELIX 58 AG4 ASP E 148 SER E 151 5 4
HELIX 59 AG5 TYR E 152 SER E 170 1 19
HELIX 60 AG6 SER E 185 ASP E 198 1 14
HELIX 61 AG7 HIS E 213 ILE E 220 1 8
HELIX 62 AG8 PRO E 225 ASP E 237 1 13
HELIX 63 AG9 GLN E 242 TYR E 252 1 11
HELIX 64 AH1 ASP E 254 SER E 260 1 7
HELIX 65 AH2 PRO E 278 ASN E 287 1 10
HELIX 66 AH3 PHE E 308 LEU E 321 1 14
HELIX 67 AH4 PRO F 7 TYR F 14 1 8
HELIX 68 AH5 ASP F 23 GLN F 37 1 15
HELIX 69 AH6 TYR F 101 GLU F 104 5 4
HELIX 70 AH7 LEU F 105 MET F 111 1 7
HELIX 71 AH8 ASP F 148 SER F 151 5 4
HELIX 72 AH9 TYR F 152 SER F 170 1 19
HELIX 73 AI1 SER F 185 ASP F 198 1 14
HELIX 74 AI2 HIS F 213 ILE F 220 1 8
HELIX 75 AI3 SER F 223 PRO F 225 5 3
HELIX 76 AI4 TYR F 226 ASP F 237 1 12
HELIX 77 AI5 GLN F 242 TYR F 252 1 11
HELIX 78 AI6 ASP F 254 SER F 260 1 7
HELIX 79 AI7 PRO F 278 ASN F 287 1 10
HELIX 80 AI8 PHE F 308 LEU F 321 1 14
SHEET 1 AA1 9 GLN A 43 LEU A 46 0
SHEET 2 AA1 9 ILE A 55 ASP A 63 -1 O VAL A 61 N GLN A 43
SHEET 3 AA1 9 PRO A 69 PRO A 77 -1 O ILE A 70 N TYR A 62
SHEET 4 AA1 9 ALA A 114 ILE A 118 -1 O ALA A 115 N VAL A 75
SHEET 5 AA1 9 LEU A 86 TYR A 92 1 N LYS A 91 O LEU A 116
SHEET 6 AA1 9 VAL A 174 GLY A 184 1 O ASP A 175 N LEU A 86
SHEET 7 AA1 9 LEU A 203 VAL A 207 1 O LEU A 205 N VAL A 181
SHEET 8 AA1 9 ARG A 265 THR A 271 1 O LEU A 267 N ALA A 204
SHEET 9 AA1 9 LYS A 293 TYR A 298 1 O ARG A 296 N ILE A 270
SHEET 1 AA2 9 GLN B 43 VAL B 47 0
SHEET 2 AA2 9 ILE B 55 ASP B 63 -1 O ILE B 57 N VAL B 47
SHEET 3 AA2 9 PRO B 69 PRO B 77 -1 O ILE B 70 N TYR B 62
SHEET 4 AA2 9 ALA B 114 ILE B 118 -1 O ALA B 115 N VAL B 75
SHEET 5 AA2 9 LEU B 86 TYR B 92 1 N PRO B 87 O ALA B 114
SHEET 6 AA2 9 VAL B 174 GLY B 184 1 O ASP B 175 N LEU B 86
SHEET 7 AA2 9 LEU B 203 VAL B 207 1 O LEU B 205 N VAL B 181
SHEET 8 AA2 9 ARG B 265 THR B 271 1 O LEU B 267 N ALA B 204
SHEET 9 AA2 9 LYS B 293 TYR B 298 1 O ARG B 296 N ILE B 270
SHEET 1 AA3 9 GLN C 43 LEU C 46 0
SHEET 2 AA3 9 ILE C 55 ASP C 63 -1 O VAL C 61 N GLN C 43
SHEET 3 AA3 9 PRO C 69 PRO C 77 -1 O TYR C 74 N TYR C 58
SHEET 4 AA3 9 ALA C 114 ILE C 118 -1 O ALA C 115 N VAL C 75
SHEET 5 AA3 9 LEU C 86 TYR C 92 1 N PRO C 87 O ALA C 114
SHEET 6 AA3 9 VAL C 174 GLY C 184 1 O ASP C 175 N LEU C 86
SHEET 7 AA3 9 LEU C 203 VAL C 207 1 O VAL C 207 N GLY C 183
SHEET 8 AA3 9 ARG C 265 THR C 271 1 O ARG C 265 N ALA C 204
SHEET 9 AA3 9 LYS C 293 TYR C 298 1 O ARG C 296 N ILE C 270
SHEET 1 AA4 9 GLN D 43 LEU D 46 0
SHEET 2 AA4 9 ILE D 55 ASP D 63 -1 O VAL D 61 N GLN D 43
SHEET 3 AA4 9 PRO D 69 PRO D 77 -1 O TYR D 74 N TYR D 58
SHEET 4 AA4 9 ALA D 114 ILE D 118 -1 O ALA D 115 N VAL D 75
SHEET 5 AA4 9 LEU D 86 TYR D 92 1 N LYS D 91 O LEU D 116
SHEET 6 AA4 9 VAL D 174 GLY D 184 1 O ARG D 178 N VAL D 88
SHEET 7 AA4 9 LEU D 203 VAL D 207 1 O VAL D 207 N GLY D 183
SHEET 8 AA4 9 ARG D 265 THR D 271 1 O LEU D 267 N ALA D 204
SHEET 9 AA4 9 LYS D 293 TYR D 298 1 O TYR D 298 N ILE D 270
SHEET 1 AA5 9 GLN E 43 LEU E 46 0
SHEET 2 AA5 9 ILE E 55 ASP E 63 -1 O ASP E 59 N ASN E 45
SHEET 3 AA5 9 PRO E 69 PRO E 77 -1 O ILE E 70 N TYR E 62
SHEET 4 AA5 9 ALA E 114 ILE E 118 -1 O ALA E 115 N VAL E 75
SHEET 5 AA5 9 LEU E 86 TYR E 92 1 N LYS E 91 O LEU E 116
SHEET 6 AA5 9 VAL E 174 GLY E 184 1 O ALA E 180 N VAL E 90
SHEET 7 AA5 9 LEU E 203 VAL E 207 1 O LEU E 205 N VAL E 181
SHEET 8 AA5 9 ARG E 265 THR E 271 1 O LEU E 267 N ALA E 204
SHEET 9 AA5 9 LYS E 293 TYR E 298 1 O ARG E 296 N ILE E 270
SHEET 1 AA6 8 ILE F 55 ASP F 63 0
SHEET 2 AA6 8 PRO F 69 PRO F 77 -1 O THR F 76 N SER F 56
SHEET 3 AA6 8 ALA F 114 ILE F 118 -1 O ALA F 115 N VAL F 75
SHEET 4 AA6 8 LEU F 86 LYS F 91 1 N LYS F 91 O LEU F 116
SHEET 5 AA6 8 VAL F 174 GLY F 184 1 O ALA F 180 N VAL F 90
SHEET 6 AA6 8 LEU F 203 VAL F 207 1 O LEU F 205 N VAL F 181
SHEET 7 AA6 8 ARG F 265 THR F 271 1 O ARG F 265 N ALA F 204
SHEET 8 AA6 8 LYS F 293 TYR F 298 1 O TYR F 298 N ILE F 270
SITE 1 AC1 1 TYR A 247
SITE 1 AC2 1 TYR B 247
SITE 1 AC3 1 TYR C 247
SITE 1 AC4 1 TYR D 247
SITE 1 AC5 2 TYR F 247 ASP F 254
CRYST1 153.797 141.659 105.369 90.00 104.49 90.00 C 1 2 1 24
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 0.006502 0.000000 0.001681 0.00000
SCALE2 0.000000 0.007059 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009802 0.00000
TER 2511 LEU A 321
TER 5022 LEU B 321
TER 7533 LEU C 321
TER 10044 LEU D 321
TER 12555 LEU E 321
TER 15066 LEU F 321
MASTER 390 0 6 80 53 0 5 615833 6 0 150
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