| 5fdf-pdb | HEADER HYDROLASE 16-DEC-15 5FDF
TITLE CRYSTAL STRUCTURE OF THE MONOCLINIC FORM OF THERMOTOGA MARITIMA ACETYL
TITLE 2 ESTERASE TM0077 (APO STRUCTURE) AT 1.76 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN-C DEACETYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ACETYLXYLAN ESTERASE, ACETYL ESTERASE;
COMPND 5 EC: 3.1.1.41,3.1.1.72;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: AXEA, TM_0077;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMH1
KEYWDS HYDROLASE, CARBOHYDRATE METABOLISM, CEPHALOSPORIN DEACETYLASE,
KEYWDS 2 ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MANOJ,M.K.SINGH
REVDAT 1 27-APR-16 5FDF 0
JRNL AUTH M.K.SINGH,N.MANOJ
JRNL TITL AN EXTENDED LOOP IN CE7 CARBOHYDRATE ESTERASE FAMILY IS
JRNL TITL 2 DISPENSABLE FOR OLIGOMERIZATION BUT REQUIRED FOR ACTIVITY
JRNL TITL 3 AND THERMOSTABILITY.
JRNL REF J.STRUCT.BIOL. 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 27085421
JRNL DOI 10.1016/J.JSB.2016.04.008
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 184681
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9696
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 1487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.576
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15778 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14511 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21467 ; 1.855 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 33346 ; 1.058 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1930 ; 6.461 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 762 ;30.470 ;22.953
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2346 ;11.795 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 107 ;16.368 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2216 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18084 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3927 ; 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): 7697 ; 1.843 ; 1.979
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7695 ; 1.837 ; 1.978
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9616 ; 2.559 ; 2.957
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): 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 : BABINET MODEL WITH 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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5FDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000213802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 194397
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 39.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.98000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1VLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M AMMONIUM SULFATE, 0.05 M BIS
REMARK 280 -TRIS PH 6.5 AND 30% (V/V) PENTAERYTHRITOL ETHOXYLATE (15/4 EO/
REMARK 280 OH), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 58.10000
REMARK 290 SMTRY3 2 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: 18240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 PHE A 3
REMARK 465 GLU A 134
REMARK 465 LYS A 324
REMARK 465 GLY A 325
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PHE B 3
REMARK 465 LYS B 324
REMARK 465 GLY B 325
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PHE C 3
REMARK 465 LYS C 324
REMARK 465 GLY C 325
REMARK 465 MET D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PHE D 3
REMARK 465 GLU D 134
REMARK 465 LYS D 324
REMARK 465 GLY D 325
REMARK 465 MET E -11
REMARK 465 GLY E -10
REMARK 465 SER E -9
REMARK 465 ASP E -8
REMARK 465 LYS E -7
REMARK 465 ILE E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 PHE E 3
REMARK 465 LYS E 324
REMARK 465 GLY E 325
REMARK 465 MET F -11
REMARK 465 GLY F -10
REMARK 465 SER F -9
REMARK 465 ASP F -8
REMARK 465 LYS F -7
REMARK 465 ILE F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 PHE F 3
REMARK 465 LYS F 324
REMARK 465 GLY F 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 9 CG CD OE1 OE2
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 26 CG CD OE1 OE2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 LYS A 82 CG CD CE NZ
REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 179 CG CD OE1 NE2
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 470 LYS A 203 CG CD CE NZ
REMARK 470 LYS A 205 CG CD CE NZ
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 248 NE CZ NH1 NH2
REMARK 470 LYS A 263 CD CE NZ
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 LYS B 320 CG CD CE NZ
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 LYS C 22 CG CD CE NZ
REMARK 470 GLU C 34 CG CD OE1 OE2
REMARK 470 GLU C 48 CG CD OE1 OE2
REMARK 470 ARG C 65 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 77 CG CD CE NZ
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 GLU C 81 CG CD OE1 OE2
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 LYS C 202 CG CD CE NZ
REMARK 470 LYS C 203 CG CD CE NZ
REMARK 470 LYS C 205 CG CD CE NZ
REMARK 470 LYS C 263 CG CD CE NZ
REMARK 470 LYS C 320 CG CD CE NZ
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 ARG D 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 LYS D 22 CG CD CE NZ
REMARK 470 GLU D 48 CG CD OE1 OE2
REMARK 470 GLU D 79 CG CD OE1 OE2
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 LYS D 82 CG CD CE NZ
REMARK 470 LYS D 202 CG CD CE NZ
REMARK 470 LYS D 205 CG CD CE NZ
REMARK 470 GLU D 244 CG CD OE1 OE2
REMARK 470 LYS D 263 CG CD CE NZ
REMARK 470 LYS D 320 CG CD CE NZ
REMARK 470 GLU D 323 CG CD OE1 OE2
REMARK 470 GLU E 9 CG CD OE1 OE2
REMARK 470 LYS E 22 CG CD CE NZ
REMARK 470 GLU E 45 CG CD OE1 OE2
REMARK 470 GLU E 48 CG CD OE1 OE2
REMARK 470 GLU E 244 CG CD OE1 OE2
REMARK 470 LYS E 263 CG CD CE NZ
REMARK 470 LYS E 320 CG CD CE NZ
REMARK 470 GLU E 323 CG CD OE1 OE2
REMARK 470 LYS F 13 CG CD CE NZ
REMARK 470 LYS F 22 CG CD CE NZ
REMARK 470 GLU F 30 CG CD OE1 OE2
REMARK 470 LYS F 37 CG CD CE NZ
REMARK 470 GLU F 48 CG CD OE1 OE2
REMARK 470 GLU F 79 CG CD OE1 OE2
REMARK 470 GLU F 80 CG CD OE1 OE2
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 LYS F 82 CG CD CE NZ
REMARK 470 ARG F 153 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 202 CG CD CE NZ
REMARK 470 LYS F 203 CG CD CE NZ
REMARK 470 LYS F 205 CG CD CE NZ
REMARK 470 GLU F 244 CG CD OE1 OE2
REMARK 470 LYS F 320 CG CD CE NZ
REMARK 470 GLU F 323 CG CD OE1 OE2
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 550 O HOH C 701 1.81
REMARK 500 OE1 GLU E 55 O HOH E 401 2.13
REMARK 500 O HOH B 719 O HOH B 749 2.17
REMARK 500 O HOH B 610 O HOH B 727 2.17
REMARK 500 O HOH B 686 O HOH B 722 2.17
REMARK 500 OH TYR C 64 OE2 GLU C 134 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 169 CG GLU A 169 CD 0.099
REMARK 500 GLU B 55 CD GLU B 55 OE1 0.081
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 15 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP A 241 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 MET B 47 CG - SD - CE ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP B 241 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 MET C 47 CB - CG - SD ANGL. DEV. = -21.4 DEGREES
REMARK 500 ARG C 68 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 118 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP C 151 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ASP C 151 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP C 163 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG C 218 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP C 241 CB - CG - OD1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP C 241 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP D 241 CB - CG - OD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 ASP D 241 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG D 248 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG D 296 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP E 116 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP E 116 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP E 163 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP E 241 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG E 248 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG E 261 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG F 18 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP F 241 CB - CG - OD1 ANGL. DEV. = 8.4 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 ASP A 5 -159.50 -103.46
REMARK 500 GLN A 120 -119.56 -95.06
REMARK 500 PRO A 139 129.79 -37.67
REMARK 500 SER A 188 -115.25 57.78
REMARK 500 VAL A 211 48.80 39.86
REMARK 500 LEU A 214 34.37 70.13
REMARK 500 ASN A 302 -146.42 -91.92
REMARK 500 ASP B 5 -165.00 -108.03
REMARK 500 ASP B 41 64.84 32.14
REMARK 500 GLN B 120 -116.56 -93.57
REMARK 500 PRO B 139 129.88 -38.46
REMARK 500 SER B 188 -119.63 63.29
REMARK 500 VAL B 211 52.09 38.48
REMARK 500 ASN B 302 -143.64 -84.47
REMARK 500 ASN B 302 -140.43 -88.27
REMARK 500 ASP C 5 -168.52 -101.34
REMARK 500 ARG C 118 122.63 -37.38
REMARK 500 GLN C 120 -120.50 -91.57
REMARK 500 SER C 188 -117.99 59.77
REMARK 500 VAL C 211 54.65 37.15
REMARK 500 ASN C 302 -148.13 -83.65
REMARK 500 ASN C 302 -146.65 -85.31
REMARK 500 GLN D 120 -121.27 -96.97
REMARK 500 PRO D 139 133.98 -38.45
REMARK 500 SER D 188 -120.34 59.08
REMARK 500 VAL D 211 54.18 35.67
REMARK 500 ASN D 302 -140.22 -89.33
REMARK 500 ASN D 302 -137.25 -81.84
REMARK 500 ASP E 5 -163.13 -105.00
REMARK 500 GLN E 120 -116.18 -97.02
REMARK 500 SER E 188 -121.21 66.74
REMARK 500 VAL E 211 56.67 34.32
REMARK 500 ASN E 302 -143.97 -91.16
REMARK 500 ASN E 302 -144.53 -87.67
REMARK 500 ASP F 5 -167.61 -105.51
REMARK 500 GLU F 81 -72.85 -74.10
REMARK 500 GLN F 120 -119.08 -100.14
REMARK 500 SER F 188 -121.02 60.42
REMARK 500 VAL F 211 53.56 36.10
REMARK 500 ASN F 302 -144.63 -95.13
REMARK 500 ASN F 302 -143.25 -86.34
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 613 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH B 753 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C 754 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH C 755 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH E 682 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH F 654 DISTANCE = 7.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VLQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED IN DIFFERENT SPACE GROUPS
REMARK 900 RELATED ID: 3M82 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED IN DIFFERENT SPACE GROUPS
DBREF 5FDF A 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5FDF B 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5FDF C 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5FDF D 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5FDF E 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5FDF F 1 325 UNP Q9WXT2 CAH_THEMA 1 325
SEQADV 5FDF MET A -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY A -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER A -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP A -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS A -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE A -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS A 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF MET B -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY B -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER B -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP B -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS B -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE B -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS B 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF MET C -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY C -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER C -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP C -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS C -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE C -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS C 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF MET D -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY D -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER D -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP D -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS D -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE D -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS D 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF MET E -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY E -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER E -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP E -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS E -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE E -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS E 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF MET F -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5FDF GLY F -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF SER F -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ASP F -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF LYS F -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF ILE F -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5FDF HIS F 0 UNP Q9WXT2 EXPRESSION TAG
SEQRES 1 A 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 A 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 A 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 A 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 A 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 A 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 A 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 A 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 A 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 A 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 A 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 A 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 A 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 A 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 A 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 A 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 A 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 A 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 A 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 A 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 A 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 A 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 A 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 A 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 A 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 B 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 B 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 B 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 B 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 B 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 B 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 B 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 B 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 B 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 B 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 B 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 B 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 B 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 B 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 B 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 B 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 B 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 B 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 B 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 B 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 B 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 B 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 B 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 B 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 B 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 C 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 C 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 C 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 C 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 C 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 C 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 C 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 C 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 C 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 C 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 C 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 C 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 C 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 C 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 C 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 C 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 C 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 C 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 C 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 C 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 C 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 C 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 C 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 C 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 C 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 C 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 D 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 D 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 D 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 D 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 D 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 D 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 D 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 D 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 D 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 D 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 D 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 D 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 D 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 D 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 D 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 D 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 D 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 D 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 D 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 D 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 D 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 D 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 D 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 D 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 D 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 D 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 E 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 E 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 E 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 E 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 E 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 E 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 E 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 E 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 E 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 E 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 E 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 E 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 E 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 E 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 E 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 E 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 E 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 E 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 E 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 E 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 E 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 E 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 E 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 E 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 E 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 E 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 F 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 F 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 F 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 F 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 F 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 F 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 F 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 F 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 F 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 F 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 F 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 F 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 F 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 F 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 F 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 F 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 F 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 F 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 F 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 F 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 F 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 F 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 F 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 F 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 F 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 F 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
HET CL B 401 1
HET ACT C 401 4
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 7 CL CL 1-
FORMUL 8 ACT C2 H3 O2 1-
FORMUL 9 HOH *1487(H2 O)
HELIX 1 AA1 PRO A 7 LYS A 12 1 6
HELIX 2 AA2 ASP A 23 LYS A 37 1 15
HELIX 3 AA3 TYR A 64 GLY A 66 5 3
HELIX 4 AA4 PHE A 98 TRP A 102 5 5
HELIX 5 AA5 LEU A 103 MET A 108 1 6
HELIX 6 AA6 TYR A 155 SER A 173 1 19
HELIX 7 AA7 SER A 188 SER A 201 1 14
HELIX 8 AA8 HIS A 216 VAL A 224 1 9
HELIX 9 AA9 PRO A 228 HIS A 239 1 12
HELIX 10 AB1 LYS A 242 TYR A 252 1 11
HELIX 11 AB2 ASP A 254 ALA A 260 1 7
HELIX 12 AB3 PRO A 278 TYR A 289 1 12
HELIX 13 AB4 GLY A 306 GLU A 323 1 18
HELIX 14 AB5 PRO B 7 LYS B 12 1 6
HELIX 15 AB6 ASP B 23 LYS B 37 1 15
HELIX 16 AB7 TYR B 64 GLY B 66 5 3
HELIX 17 AB8 PHE B 98 TRP B 102 5 5
HELIX 18 AB9 LEU B 103 MET B 108 1 6
HELIX 19 AC1 ASP B 151 THR B 154 5 4
HELIX 20 AC2 TYR B 155 PHE B 174 1 20
HELIX 21 AC3 SER B 188 SER B 201 1 14
HELIX 22 AC4 HIS B 216 VAL B 224 1 9
HELIX 23 AC5 PRO B 228 HIS B 239 1 12
HELIX 24 AC6 LYS B 242 TYR B 252 1 11
HELIX 25 AC7 ASP B 254 ALA B 260 1 7
HELIX 26 AC8 PRO B 278 TYR B 289 1 12
HELIX 27 AC9 GLY B 306 GLU B 323 1 18
HELIX 28 AD1 PRO C 7 LYS C 12 1 6
HELIX 29 AD2 ASP C 23 LYS C 37 1 15
HELIX 30 AD3 TYR C 64 GLY C 66 5 3
HELIX 31 AD4 PHE C 98 TRP C 102 5 5
HELIX 32 AD5 LEU C 103 MET C 108 1 6
HELIX 33 AD6 ASP C 151 THR C 154 5 4
HELIX 34 AD7 TYR C 155 SER C 173 1 19
HELIX 35 AD8 SER C 188 SER C 201 1 14
HELIX 36 AD9 HIS C 216 VAL C 224 1 9
HELIX 37 AE1 PRO C 228 HIS C 239 1 12
HELIX 38 AE2 LYS C 242 TYR C 252 1 11
HELIX 39 AE3 ASP C 254 ALA C 260 1 7
HELIX 40 AE4 PRO C 278 TYR C 289 1 12
HELIX 41 AE5 GLY C 306 GLU C 323 1 18
HELIX 42 AE6 PRO D 7 LYS D 12 1 6
HELIX 43 AE7 ASP D 23 LYS D 37 1 15
HELIX 44 AE8 TYR D 64 GLY D 66 5 3
HELIX 45 AE9 PHE D 98 TRP D 102 5 5
HELIX 46 AF1 LEU D 103 MET D 108 1 6
HELIX 47 AF2 TYR D 155 SER D 173 1 19
HELIX 48 AF3 SER D 188 SER D 201 1 14
HELIX 49 AF4 HIS D 216 VAL D 224 1 9
HELIX 50 AF5 PRO D 228 HIS D 239 1 12
HELIX 51 AF6 LYS D 242 TYR D 252 1 11
HELIX 52 AF7 ASP D 254 ALA D 260 1 7
HELIX 53 AF8 PRO D 278 TYR D 289 1 12
HELIX 54 AF9 GLY D 306 GLU D 323 1 18
HELIX 55 AG1 PRO E 7 LYS E 13 1 7
HELIX 56 AG2 ASP E 23 LYS E 37 1 15
HELIX 57 AG3 TYR E 64 GLY E 66 5 3
HELIX 58 AG4 PHE E 98 TRP E 102 5 5
HELIX 59 AG5 LEU E 103 MET E 108 1 6
HELIX 60 AG6 TYR E 155 SER E 173 1 19
HELIX 61 AG7 SER E 188 SER E 201 1 14
HELIX 62 AG8 HIS E 216 VAL E 224 1 9
HELIX 63 AG9 PRO E 228 HIS E 239 1 12
HELIX 64 AH1 LYS E 242 TYR E 252 1 11
HELIX 65 AH2 ASP E 254 ALA E 260 1 7
HELIX 66 AH3 PRO E 278 TYR E 289 1 12
HELIX 67 AH4 GLY E 306 GLU E 323 1 18
HELIX 68 AH5 PRO F 7 LYS F 13 1 7
HELIX 69 AH6 ASP F 23 LYS F 37 1 15
HELIX 70 AH7 TYR F 64 GLY F 66 5 3
HELIX 71 AH8 PHE F 98 TRP F 102 5 5
HELIX 72 AH9 LEU F 103 MET F 108 1 6
HELIX 73 AI1 TYR F 155 SER F 173 1 19
HELIX 74 AI2 SER F 188 SER F 201 1 14
HELIX 75 AI3 HIS F 216 VAL F 224 1 9
HELIX 76 AI4 TYR F 229 HIS F 239 1 11
HELIX 77 AI5 LYS F 242 TYR F 252 1 11
HELIX 78 AI6 ASP F 254 ALA F 260 1 7
HELIX 79 AI7 PRO F 278 TYR F 289 1 12
HELIX 80 AI8 GLY F 306 GLU F 323 1 18
SHEET 1 AA1 9 VAL A 43 ARG A 46 0
SHEET 2 AA1 9 VAL A 54 SER A 62 -1 O ASP A 58 N GLU A 45
SHEET 3 AA1 9 ARG A 68 PRO A 76 -1 O ILE A 69 N PHE A 61
SHEET 4 AA1 9 ILE A 111 MET A 115 -1 O VAL A 114 N TRP A 72
SHEET 5 AA1 9 LEU A 83 TYR A 89 1 N GLN A 88 O PHE A 113
SHEET 6 AA1 9 VAL A 177 GLY A 187 1 O VAL A 183 N VAL A 87
SHEET 7 AA1 9 ALA A 206 ASP A 210 1 O LEU A 208 N ILE A 184
SHEET 8 AA1 9 ALA A 266 GLY A 271 1 O LEU A 267 N LEU A 207
SHEET 9 AA1 9 LYS A 293 TYR A 298 1 O GLU A 294 N PHE A 268
SHEET 1 AA2 9 VAL B 43 ARG B 46 0
SHEET 2 AA2 9 VAL B 54 SER B 62 -1 O THR B 60 N VAL B 43
SHEET 3 AA2 9 ARG B 68 PRO B 76 -1 O VAL B 75 N GLU B 55
SHEET 4 AA2 9 ILE B 111 MET B 115 -1 O VAL B 114 N TRP B 72
SHEET 5 AA2 9 LEU B 83 GLN B 88 1 N PRO B 84 O ILE B 111
SHEET 6 AA2 9 VAL B 177 GLY B 187 1 O VAL B 183 N CYS B 85
SHEET 7 AA2 9 ALA B 206 ASP B 210 1 O LEU B 208 N ILE B 184
SHEET 8 AA2 9 ALA B 266 GLY B 271 1 O LEU B 267 N CYS B 209
SHEET 9 AA2 9 LYS B 293 TYR B 298 1 O GLU B 294 N PHE B 268
SHEET 1 AA3 9 VAL C 43 ARG C 46 0
SHEET 2 AA3 9 VAL C 54 SER C 62 -1 O ASP C 58 N GLU C 45
SHEET 3 AA3 9 ARG C 68 PRO C 76 -1 O ILE C 69 N PHE C 61
SHEET 4 AA3 9 ILE C 111 MET C 115 -1 O VAL C 114 N TRP C 72
SHEET 5 AA3 9 LEU C 83 GLN C 88 1 N GLN C 88 O PHE C 113
SHEET 6 AA3 9 VAL C 177 GLY C 187 1 O ASP C 178 N LEU C 83
SHEET 7 AA3 9 ALA C 206 ASP C 210 1 O LEU C 208 N ILE C 184
SHEET 8 AA3 9 ALA C 266 GLY C 271 1 O LEU C 267 N CYS C 209
SHEET 9 AA3 9 LYS C 293 TYR C 298 1 O GLU C 294 N PHE C 268
SHEET 1 AA4 9 VAL D 43 ARG D 46 0
SHEET 2 AA4 9 VAL D 54 SER D 62 -1 O ASP D 58 N GLU D 45
SHEET 3 AA4 9 ARG D 68 PRO D 76 -1 O ILE D 69 N PHE D 61
SHEET 4 AA4 9 ILE D 111 MET D 115 -1 O VAL D 114 N TRP D 72
SHEET 5 AA4 9 LEU D 83 GLN D 88 1 N PRO D 84 O ILE D 111
SHEET 6 AA4 9 VAL D 177 GLY D 187 1 O VAL D 183 N CYS D 85
SHEET 7 AA4 9 ALA D 206 ASP D 210 1 O ALA D 206 N ILE D 184
SHEET 8 AA4 9 ALA D 266 GLY D 271 1 O LEU D 267 N CYS D 209
SHEET 9 AA4 9 LYS D 293 TYR D 298 1 O GLU D 294 N PHE D 268
SHEET 1 AA5 9 VAL E 43 ARG E 46 0
SHEET 2 AA5 9 VAL E 54 SER E 62 -1 O THR E 60 N VAL E 43
SHEET 3 AA5 9 ARG E 68 PRO E 76 -1 O VAL E 75 N GLU E 55
SHEET 4 AA5 9 ILE E 111 MET E 115 -1 O VAL E 114 N TRP E 72
SHEET 5 AA5 9 LEU E 83 GLN E 88 1 N GLN E 88 O PHE E 113
SHEET 6 AA5 9 VAL E 177 GLY E 187 1 O VAL E 183 N CYS E 85
SHEET 7 AA5 9 ALA E 206 ASP E 210 1 O ASP E 210 N GLY E 186
SHEET 8 AA5 9 ALA E 266 GLY E 271 1 O LEU E 267 N CYS E 209
SHEET 9 AA5 9 LYS E 293 TYR E 298 1 O GLU E 294 N PHE E 268
SHEET 1 AA6 9 VAL F 43 ARG F 46 0
SHEET 2 AA6 9 VAL F 54 SER F 62 -1 O ASP F 58 N GLU F 45
SHEET 3 AA6 9 ARG F 68 PRO F 76 -1 O VAL F 75 N GLU F 55
SHEET 4 AA6 9 ILE F 111 MET F 115 -1 O VAL F 114 N TRP F 72
SHEET 5 AA6 9 LEU F 83 GLN F 88 1 N GLN F 88 O PHE F 113
SHEET 6 AA6 9 VAL F 177 GLY F 187 1 O VAL F 183 N VAL F 87
SHEET 7 AA6 9 ALA F 206 ASP F 210 1 O LEU F 208 N ILE F 184
SHEET 8 AA6 9 ALA F 266 GLY F 271 1 O LEU F 267 N LEU F 207
SHEET 9 AA6 9 LYS F 293 TYR F 298 1 O ARG F 296 N PHE F 268
CISPEP 1 HIS A 227 PRO A 228 0 9.79
CISPEP 2 HIS B 227 PRO B 228 0 8.32
CISPEP 3 HIS C 227 PRO C 228 0 10.04
CISPEP 4 HIS D 227 PRO D 228 0 11.87
CISPEP 5 HIS E 227 PRO E 228 0 7.53
CISPEP 6 HIS F 227 PRO F 228 0 8.67
SITE 1 AC1 2 HIS B 100 HOH B 519
SITE 1 AC2 8 GLN C 140 PRO C 142 GLY C 143 ARG C 147
SITE 2 AC2 8 GLN F 140 PRO F 142 GLY F 143 ARG F 147
CRYST1 89.760 116.200 103.290 90.00 109.97 90.00 P 1 21 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 0.011141 0.000000 0.004048 0.00000
SCALE2 0.000000 0.008606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010301 0.00000
TER 2517 GLU A 323
TER 5090 GLU B 323
TER 7632 GLU C 323
TER 10174 GLU D 323
TER 12751 GLU E 323
TER 15294 GLU F 323
MASTER 601 0 2 80 54 0 3 616703 6 4 156
END
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