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HEADER NAD-BINDING PROTEIN 30-NOV-06 2O2Z
TITLE CRYSTAL STRUCTURE OF A PROTEIN MEMBER OF THE UPF0052 FAMILY (BH3568)
TITLE 2 FROM BACILLUS HALODURANS AT 2.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;
SOURCE 3 ORGANISM_TAXID: 86665;
SOURCE 4 GENE: NP_244435.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI-2, NAD-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 3 23-MAR-11 2O2Z 1 HEADER TITLE KEYWDS
REVDAT 2 24-FEB-09 2O2Z 1 VERSN
REVDAT 1 19-DEC-06 2O2Z 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN (NP_244435.1) FROM
JRNL TITL 2 BACILLUS HALODURANS AT 2.60 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 54312
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2764
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 205
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9095
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 216
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : 0.66000
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): 0.425
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.706
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9442 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6217 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12822 ; 1.500 ; 2.018
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15382 ; 0.920 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1226 ; 5.492 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;35.560 ;24.936
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1618 ;15.916 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.814 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1559 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10234 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1610 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1874 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6251 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4557 ; 0.175 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5055 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 340 ; 0.170 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.081 ; 0.200
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): 10 ; 0.342 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.174 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.098 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6313 ; 1.566 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2543 ; 0.238 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9827 ; 2.600 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3518 ; 4.899 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2995 ; 6.797 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 118 2
REMARK 3 1 B 4 B 118 2
REMARK 3 1 C 4 C 118 2
REMARK 3 1 D 4 D 118 2
REMARK 3 2 A 119 A 119 6
REMARK 3 2 B 119 B 119 6
REMARK 3 2 C 119 C 119 6
REMARK 3 2 D 119 D 119 6
REMARK 3 3 A 120 A 310 2
REMARK 3 3 B 120 B 310 2
REMARK 3 3 C 120 C 310 2
REMARK 3 3 D 120 D 310 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1766 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1766 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 1766 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 1766 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1869 ; 0.340 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1869 ; 0.300 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1869 ; 0.280 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1869 ; 0.290 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 6 ; 0.130 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 6 ; 0.330 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 6 ; 0.380 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 6 ; 0.620 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 1766 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 1766 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 1766 ; 0.090 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 1766 ; 0.100 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1869 ; 0.880 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1869 ; 0.780 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1869 ; 0.700 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1869 ; 0.730 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 6 ; 0.970 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 6 ; 1.420 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 6 ; 1.240 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 6 ; 1.290 ;10.000
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ONE NAD IS ASSOCIATED WITH EACH MONOMER. NAD
REMARK 3 IS ASSIGNED BASED ON ELECTRON DENSITY. THE ASSIGNMENT IS
REMARK 3 TENTATIVE DUE TO POOR DENSITY AND LIMITED RESOLUTION, ONLY
REMARK 3 PYROPHOSPHATE AND RIBOSE DENSITY ARE DEFINITIVE. 3. A MET-
REMARK 3 INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPOR DURING
REMARK 3 PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE
REMARK 3 RESIDUES WAS REDUCED TO 0.7 TO ACCOUNT FOR THE REDUCED SCATTERING
REMARK 3 DUE TO PARTIAL S-MET INCORPORATION.
REMARK 4
REMARK 4 2O2Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB040621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54381
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.437
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40.0% POLYETHYLENE GLYCOL 400, 0.2M
REMARK 280 LITHIUM SULFATE, 0.1M TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.71500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.84000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.84000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.71500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.82000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1,2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT
REMARK 300 OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION
REMARK 300 STATE.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN A 83
REMARK 465 ASP A 296
REMARK 465 ASP A 297
REMARK 465 GLY A 313
REMARK 465 LYS A 314
REMARK 465 PRO A 315
REMARK 465 ARG A 316
REMARK 465 THR A 317
REMARK 465 SER A 318
REMARK 465 SER A 319
REMARK 465 SER A 320
REMARK 465 ILE A 321
REMARK 465 GLN A 322
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 ASN B 83
REMARK 465 GLN B 295
REMARK 465 GLY B 313
REMARK 465 LYS B 314
REMARK 465 PRO B 315
REMARK 465 ARG B 316
REMARK 465 THR B 317
REMARK 465 SER B 318
REMARK 465 SER B 319
REMARK 465 SER B 320
REMARK 465 ILE B 321
REMARK 465 GLN B 322
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 LYS C 2
REMARK 465 ASN C 83
REMARK 465 GLY C 313
REMARK 465 LYS C 314
REMARK 465 PRO C 315
REMARK 465 ARG C 316
REMARK 465 THR C 317
REMARK 465 SER C 318
REMARK 465 SER C 319
REMARK 465 SER C 320
REMARK 465 ILE C 321
REMARK 465 GLN C 322
REMARK 465 GLY D 0
REMARK 465 ASN D 83
REMARK 465 ASP D 296
REMARK 465 GLY D 313
REMARK 465 LYS D 314
REMARK 465 PRO D 315
REMARK 465 ARG D 316
REMARK 465 THR D 317
REMARK 465 SER D 318
REMARK 465 SER D 319
REMARK 465 SER D 320
REMARK 465 ILE D 321
REMARK 465 GLN D 322
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 MSE A 1 CG SE CE
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 ARG A 107 NH1 NH2
REMARK 470 ARG A 119 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS A 121 CE NZ
REMARK 470 ARG A 169 CZ NH1 NH2
REMARK 470 ARG A 176 NH1 NH2
REMARK 470 LYS A 177 CE NZ
REMARK 470 GLN A 207 CD OE1 NE2
REMARK 470 LYS A 280 CD CE NZ
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 GLN A 295 CG CD OE1 NE2
REMARK 470 LYS A 305 CE NZ
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLU B 80 CG CD OE1 OE2
REMARK 470 LYS B 114 CD CE NZ
REMARK 470 ARG B 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 121 CE NZ
REMARK 470 LYS B 166 CE NZ
REMARK 470 ARG B 169 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 170 CD OE1 OE2
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 LYS B 280 CD CE NZ
REMARK 470 GLU B 312 CG CD OE1 OE2
REMARK 470 LYS C 47 CG CD CE NZ
REMARK 470 GLU C 80 CG CD OE1 OE2
REMARK 470 ARG C 107 CZ NH1 NH2
REMARK 470 ARG C 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 166 CE NZ
REMARK 470 ARG C 169 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 173 CD OE1 OE2
REMARK 470 LYS C 177 CE NZ
REMARK 470 ILE C 256 CD1
REMARK 470 HIS C 277 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 312 CG CD OE1 OE2
REMARK 470 LYS D 3 CG CD CE NZ
REMARK 470 LYS D 47 CG CD CE NZ
REMARK 470 ASN D 81 CG OD1
REMARK 470 ARG D 107 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 121 CE NZ
REMARK 470 ARG D 128 NE CZ NH1 NH2
REMARK 470 LYS D 166 CE NZ
REMARK 470 ARG D 169 CD NE CZ NH1 NH2
REMARK 470 GLU D 170 CD OE1 OE2
REMARK 470 GLN D 207 CD OE1 NE2
REMARK 470 GLU D 254 CG CD OE1 OE2
REMARK 470 LYS D 261 NZ
REMARK 470 LYS D 266 CD CE NZ
REMARK 470 HIS D 277 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 295 CG CD OE1 NE2
REMARK 470 ASP D 297 CG OD1 OD2
REMARK 470 GLU D 312 CG CD OE1 OE2
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 38 16.41 -141.32
REMARK 500 SER A 191 -48.66 -133.77
REMARK 500 GLU A 224 -59.75 -125.46
REMARK 500 SER B 191 -50.92 -129.78
REMARK 500 GLU B 224 -58.49 -124.40
REMARK 500 ASP C 38 12.63 -140.30
REMARK 500 SER C 191 -46.54 -134.48
REMARK 500 GLU C 224 -58.08 -127.49
REMARK 500 GLN C 295 -91.59 -94.55
REMARK 500 ASP C 296 61.90 -109.12
REMARK 500 ASP D 38 14.50 -141.82
REMARK 500 SER D 191 -47.84 -132.82
REMARK 500 GLU D 224 -58.21 -126.19
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 SO4 B 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 372969 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE
REMARK 999 TARGET SEQUENCE. DNA SEQUENCING INDICATES THAT RESIDUE 7
REMARK 999 IS ISOLEUCINE (NOT VALINE) IN THE CLONED CONSTRUCT.
REMARK 999 THE SEQUENCING RESULTS ARE CONSISTENT WITH THE ELECTRON
REMARK 999 DENSITY AND MASS SPECTROMETRY RESULTS FOR THE EXPRESSED
REMARK 999 PROTEIN.
DBREF 2O2Z A 1 322 UNP Q9K706 Y3568_BACHD 1 322
DBREF 2O2Z B 1 322 UNP Q9K706 Y3568_BACHD 1 322
DBREF 2O2Z C 1 322 UNP Q9K706 Y3568_BACHD 1 322
DBREF 2O2Z D 1 322 UNP Q9K706 Y3568_BACHD 1 322
SEQADV 2O2Z GLY A 0 UNP Q9K706 LEADER SEQUENCE
SEQADV 2O2Z MSE A 1 UNP Q9K706 MET 1 MODIFIED RESIDUE
SEQADV 2O2Z ILE A 7 UNP Q9K706 VAL 7 SEE REMARK 999
SEQADV 2O2Z MSE A 98 UNP Q9K706 MET 98 MODIFIED RESIDUE
SEQADV 2O2Z MSE A 112 UNP Q9K706 MET 112 MODIFIED RESIDUE
SEQADV 2O2Z MSE A 136 UNP Q9K706 MET 136 MODIFIED RESIDUE
SEQADV 2O2Z MSE A 219 UNP Q9K706 MET 219 MODIFIED RESIDUE
SEQADV 2O2Z MSE A 238 UNP Q9K706 MET 238 MODIFIED RESIDUE
SEQADV 2O2Z GLY B 0 UNP Q9K706 LEADER SEQUENCE
SEQADV 2O2Z MSE B 1 UNP Q9K706 MET 1 MODIFIED RESIDUE
SEQADV 2O2Z ILE B 7 UNP Q9K706 VAL 7 SEE REMARK 999
SEQADV 2O2Z MSE B 98 UNP Q9K706 MET 98 MODIFIED RESIDUE
SEQADV 2O2Z MSE B 112 UNP Q9K706 MET 112 MODIFIED RESIDUE
SEQADV 2O2Z MSE B 136 UNP Q9K706 MET 136 MODIFIED RESIDUE
SEQADV 2O2Z MSE B 219 UNP Q9K706 MET 219 MODIFIED RESIDUE
SEQADV 2O2Z MSE B 238 UNP Q9K706 MET 238 MODIFIED RESIDUE
SEQADV 2O2Z GLY C 0 UNP Q9K706 LEADER SEQUENCE
SEQADV 2O2Z MSE C 1 UNP Q9K706 MET 1 MODIFIED RESIDUE
SEQADV 2O2Z ILE C 7 UNP Q9K706 VAL 7 SEE REMARK 999
SEQADV 2O2Z MSE C 98 UNP Q9K706 MET 98 MODIFIED RESIDUE
SEQADV 2O2Z MSE C 112 UNP Q9K706 MET 112 MODIFIED RESIDUE
SEQADV 2O2Z MSE C 136 UNP Q9K706 MET 136 MODIFIED RESIDUE
SEQADV 2O2Z MSE C 219 UNP Q9K706 MET 219 MODIFIED RESIDUE
SEQADV 2O2Z MSE C 238 UNP Q9K706 MET 238 MODIFIED RESIDUE
SEQADV 2O2Z GLY D 0 UNP Q9K706 LEADER SEQUENCE
SEQADV 2O2Z MSE D 1 UNP Q9K706 MET 1 MODIFIED RESIDUE
SEQADV 2O2Z ILE D 7 UNP Q9K706 VAL 7 SEE REMARK 999
SEQADV 2O2Z MSE D 98 UNP Q9K706 MET 98 MODIFIED RESIDUE
SEQADV 2O2Z MSE D 112 UNP Q9K706 MET 112 MODIFIED RESIDUE
SEQADV 2O2Z MSE D 136 UNP Q9K706 MET 136 MODIFIED RESIDUE
SEQADV 2O2Z MSE D 219 UNP Q9K706 MET 219 MODIFIED RESIDUE
SEQADV 2O2Z MSE D 238 UNP Q9K706 MET 238 MODIFIED RESIDUE
SEQRES 1 A 323 GLY MSE LYS LYS LYS ASN VAL ILE VAL PHE GLY GLY GLY
SEQRES 2 A 323 THR GLY LEU SER VAL LEU LEU ARG GLY LEU LYS THR PHE
SEQRES 3 A 323 PRO VAL SER ILE THR ALA ILE VAL THR VAL ALA ASP ASP
SEQRES 4 A 323 GLY GLY SER SER GLY ARG LEU ARG LYS GLU LEU ASP ILE
SEQRES 5 A 323 PRO PRO PRO GLY ASP VAL ARG ASN VAL LEU VAL ALA LEU
SEQRES 6 A 323 SER GLU VAL GLU PRO LEU LEU GLU GLN LEU PHE GLN HIS
SEQRES 7 A 323 ARG PHE GLU ASN GLY ASN GLY LEU SER GLY HIS SER LEU
SEQRES 8 A 323 GLY ASN LEU LEU LEU ALA GLY MSE THR SER ILE THR GLY
SEQRES 9 A 323 ASP PHE ALA ARG GLY ILE SER GLU MSE SER LYS VAL LEU
SEQRES 10 A 323 ASN VAL ARG GLY LYS VAL LEU PRO ALA SER ASN ARG SER
SEQRES 11 A 323 ILE ILE LEU HIS GLY GLU MSE GLU ASP GLY THR ILE VAL
SEQRES 12 A 323 THR GLY GLU SER SER ILE PRO LYS ALA GLY LYS LYS ILE
SEQRES 13 A 323 LYS ARG VAL PHE LEU THR PRO LYS ASP THR LYS PRO LEU
SEQRES 14 A 323 ARG GLU GLY LEU GLU ALA ILE ARG LYS ALA ASP VAL ILE
SEQRES 15 A 323 VAL ILE GLY PRO GLY SER LEU TYR THR SER VAL LEU PRO
SEQRES 16 A 323 ASN LEU LEU VAL PRO GLY ILE CYS GLU ALA ILE LYS GLN
SEQRES 17 A 323 SER THR ALA ARG LYS VAL TYR ILE CYS ASN VAL MSE THR
SEQRES 18 A 323 GLN ASN GLY GLU THR ASP GLY TYR THR ALA SER ASP HIS
SEQRES 19 A 323 LEU GLN ALA ILE MSE ASP HIS CYS GLY VAL GLY ILE VAL
SEQRES 20 A 323 ASP ASP ILE LEU VAL HIS GLY GLU PRO ILE SER ASP THR
SEQRES 21 A 323 VAL LYS ALA LYS TYR ALA LYS GLU LYS ALA GLU PRO VAL
SEQRES 22 A 323 ILE VAL ASP GLU HIS LYS LEU LYS ALA LEU GLY VAL GLY
SEQRES 23 A 323 THR ILE SER ASP TYR PHE VAL LEU GLU GLN ASP ASP VAL
SEQRES 24 A 323 LEU ARG HIS ASN ALA SER LYS VAL SER GLU ALA ILE LEU
SEQRES 25 A 323 GLU GLY LYS PRO ARG THR SER SER SER ILE GLN
SEQRES 1 B 323 GLY MSE LYS LYS LYS ASN VAL ILE VAL PHE GLY GLY GLY
SEQRES 2 B 323 THR GLY LEU SER VAL LEU LEU ARG GLY LEU LYS THR PHE
SEQRES 3 B 323 PRO VAL SER ILE THR ALA ILE VAL THR VAL ALA ASP ASP
SEQRES 4 B 323 GLY GLY SER SER GLY ARG LEU ARG LYS GLU LEU ASP ILE
SEQRES 5 B 323 PRO PRO PRO GLY ASP VAL ARG ASN VAL LEU VAL ALA LEU
SEQRES 6 B 323 SER GLU VAL GLU PRO LEU LEU GLU GLN LEU PHE GLN HIS
SEQRES 7 B 323 ARG PHE GLU ASN GLY ASN GLY LEU SER GLY HIS SER LEU
SEQRES 8 B 323 GLY ASN LEU LEU LEU ALA GLY MSE THR SER ILE THR GLY
SEQRES 9 B 323 ASP PHE ALA ARG GLY ILE SER GLU MSE SER LYS VAL LEU
SEQRES 10 B 323 ASN VAL ARG GLY LYS VAL LEU PRO ALA SER ASN ARG SER
SEQRES 11 B 323 ILE ILE LEU HIS GLY GLU MSE GLU ASP GLY THR ILE VAL
SEQRES 12 B 323 THR GLY GLU SER SER ILE PRO LYS ALA GLY LYS LYS ILE
SEQRES 13 B 323 LYS ARG VAL PHE LEU THR PRO LYS ASP THR LYS PRO LEU
SEQRES 14 B 323 ARG GLU GLY LEU GLU ALA ILE ARG LYS ALA ASP VAL ILE
SEQRES 15 B 323 VAL ILE GLY PRO GLY SER LEU TYR THR SER VAL LEU PRO
SEQRES 16 B 323 ASN LEU LEU VAL PRO GLY ILE CYS GLU ALA ILE LYS GLN
SEQRES 17 B 323 SER THR ALA ARG LYS VAL TYR ILE CYS ASN VAL MSE THR
SEQRES 18 B 323 GLN ASN GLY GLU THR ASP GLY TYR THR ALA SER ASP HIS
SEQRES 19 B 323 LEU GLN ALA ILE MSE ASP HIS CYS GLY VAL GLY ILE VAL
SEQRES 20 B 323 ASP ASP ILE LEU VAL HIS GLY GLU PRO ILE SER ASP THR
SEQRES 21 B 323 VAL LYS ALA LYS TYR ALA LYS GLU LYS ALA GLU PRO VAL
SEQRES 22 B 323 ILE VAL ASP GLU HIS LYS LEU LYS ALA LEU GLY VAL GLY
SEQRES 23 B 323 THR ILE SER ASP TYR PHE VAL LEU GLU GLN ASP ASP VAL
SEQRES 24 B 323 LEU ARG HIS ASN ALA SER LYS VAL SER GLU ALA ILE LEU
SEQRES 25 B 323 GLU GLY LYS PRO ARG THR SER SER SER ILE GLN
SEQRES 1 C 323 GLY MSE LYS LYS LYS ASN VAL ILE VAL PHE GLY GLY GLY
SEQRES 2 C 323 THR GLY LEU SER VAL LEU LEU ARG GLY LEU LYS THR PHE
SEQRES 3 C 323 PRO VAL SER ILE THR ALA ILE VAL THR VAL ALA ASP ASP
SEQRES 4 C 323 GLY GLY SER SER GLY ARG LEU ARG LYS GLU LEU ASP ILE
SEQRES 5 C 323 PRO PRO PRO GLY ASP VAL ARG ASN VAL LEU VAL ALA LEU
SEQRES 6 C 323 SER GLU VAL GLU PRO LEU LEU GLU GLN LEU PHE GLN HIS
SEQRES 7 C 323 ARG PHE GLU ASN GLY ASN GLY LEU SER GLY HIS SER LEU
SEQRES 8 C 323 GLY ASN LEU LEU LEU ALA GLY MSE THR SER ILE THR GLY
SEQRES 9 C 323 ASP PHE ALA ARG GLY ILE SER GLU MSE SER LYS VAL LEU
SEQRES 10 C 323 ASN VAL ARG GLY LYS VAL LEU PRO ALA SER ASN ARG SER
SEQRES 11 C 323 ILE ILE LEU HIS GLY GLU MSE GLU ASP GLY THR ILE VAL
SEQRES 12 C 323 THR GLY GLU SER SER ILE PRO LYS ALA GLY LYS LYS ILE
SEQRES 13 C 323 LYS ARG VAL PHE LEU THR PRO LYS ASP THR LYS PRO LEU
SEQRES 14 C 323 ARG GLU GLY LEU GLU ALA ILE ARG LYS ALA ASP VAL ILE
SEQRES 15 C 323 VAL ILE GLY PRO GLY SER LEU TYR THR SER VAL LEU PRO
SEQRES 16 C 323 ASN LEU LEU VAL PRO GLY ILE CYS GLU ALA ILE LYS GLN
SEQRES 17 C 323 SER THR ALA ARG LYS VAL TYR ILE CYS ASN VAL MSE THR
SEQRES 18 C 323 GLN ASN GLY GLU THR ASP GLY TYR THR ALA SER ASP HIS
SEQRES 19 C 323 LEU GLN ALA ILE MSE ASP HIS CYS GLY VAL GLY ILE VAL
SEQRES 20 C 323 ASP ASP ILE LEU VAL HIS GLY GLU PRO ILE SER ASP THR
SEQRES 21 C 323 VAL LYS ALA LYS TYR ALA LYS GLU LYS ALA GLU PRO VAL
SEQRES 22 C 323 ILE VAL ASP GLU HIS LYS LEU LYS ALA LEU GLY VAL GLY
SEQRES 23 C 323 THR ILE SER ASP TYR PHE VAL LEU GLU GLN ASP ASP VAL
SEQRES 24 C 323 LEU ARG HIS ASN ALA SER LYS VAL SER GLU ALA ILE LEU
SEQRES 25 C 323 GLU GLY LYS PRO ARG THR SER SER SER ILE GLN
SEQRES 1 D 323 GLY MSE LYS LYS LYS ASN VAL ILE VAL PHE GLY GLY GLY
SEQRES 2 D 323 THR GLY LEU SER VAL LEU LEU ARG GLY LEU LYS THR PHE
SEQRES 3 D 323 PRO VAL SER ILE THR ALA ILE VAL THR VAL ALA ASP ASP
SEQRES 4 D 323 GLY GLY SER SER GLY ARG LEU ARG LYS GLU LEU ASP ILE
SEQRES 5 D 323 PRO PRO PRO GLY ASP VAL ARG ASN VAL LEU VAL ALA LEU
SEQRES 6 D 323 SER GLU VAL GLU PRO LEU LEU GLU GLN LEU PHE GLN HIS
SEQRES 7 D 323 ARG PHE GLU ASN GLY ASN GLY LEU SER GLY HIS SER LEU
SEQRES 8 D 323 GLY ASN LEU LEU LEU ALA GLY MSE THR SER ILE THR GLY
SEQRES 9 D 323 ASP PHE ALA ARG GLY ILE SER GLU MSE SER LYS VAL LEU
SEQRES 10 D 323 ASN VAL ARG GLY LYS VAL LEU PRO ALA SER ASN ARG SER
SEQRES 11 D 323 ILE ILE LEU HIS GLY GLU MSE GLU ASP GLY THR ILE VAL
SEQRES 12 D 323 THR GLY GLU SER SER ILE PRO LYS ALA GLY LYS LYS ILE
SEQRES 13 D 323 LYS ARG VAL PHE LEU THR PRO LYS ASP THR LYS PRO LEU
SEQRES 14 D 323 ARG GLU GLY LEU GLU ALA ILE ARG LYS ALA ASP VAL ILE
SEQRES 15 D 323 VAL ILE GLY PRO GLY SER LEU TYR THR SER VAL LEU PRO
SEQRES 16 D 323 ASN LEU LEU VAL PRO GLY ILE CYS GLU ALA ILE LYS GLN
SEQRES 17 D 323 SER THR ALA ARG LYS VAL TYR ILE CYS ASN VAL MSE THR
SEQRES 18 D 323 GLN ASN GLY GLU THR ASP GLY TYR THR ALA SER ASP HIS
SEQRES 19 D 323 LEU GLN ALA ILE MSE ASP HIS CYS GLY VAL GLY ILE VAL
SEQRES 20 D 323 ASP ASP ILE LEU VAL HIS GLY GLU PRO ILE SER ASP THR
SEQRES 21 D 323 VAL LYS ALA LYS TYR ALA LYS GLU LYS ALA GLU PRO VAL
SEQRES 22 D 323 ILE VAL ASP GLU HIS LYS LEU LYS ALA LEU GLY VAL GLY
SEQRES 23 D 323 THR ILE SER ASP TYR PHE VAL LEU GLU GLN ASP ASP VAL
SEQRES 24 D 323 LEU ARG HIS ASN ALA SER LYS VAL SER GLU ALA ILE LEU
SEQRES 25 D 323 GLU GLY LYS PRO ARG THR SER SER SER ILE GLN
MODRES 2O2Z MSE A 1 MET SELENOMETHIONINE
MODRES 2O2Z MSE A 98 MET SELENOMETHIONINE
MODRES 2O2Z MSE A 112 MET SELENOMETHIONINE
MODRES 2O2Z MSE A 136 MET SELENOMETHIONINE
MODRES 2O2Z MSE A 219 MET SELENOMETHIONINE
MODRES 2O2Z MSE A 238 MET SELENOMETHIONINE
MODRES 2O2Z MSE B 98 MET SELENOMETHIONINE
MODRES 2O2Z MSE B 112 MET SELENOMETHIONINE
MODRES 2O2Z MSE B 136 MET SELENOMETHIONINE
MODRES 2O2Z MSE B 219 MET SELENOMETHIONINE
MODRES 2O2Z MSE B 238 MET SELENOMETHIONINE
MODRES 2O2Z MSE C 98 MET SELENOMETHIONINE
MODRES 2O2Z MSE C 112 MET SELENOMETHIONINE
MODRES 2O2Z MSE C 136 MET SELENOMETHIONINE
MODRES 2O2Z MSE C 219 MET SELENOMETHIONINE
MODRES 2O2Z MSE C 238 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 1 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 98 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 112 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 136 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 219 MET SELENOMETHIONINE
MODRES 2O2Z MSE D 238 MET SELENOMETHIONINE
HET MSE A 1 5
HET MSE A 98 8
HET MSE A 112 8
HET MSE A 136 8
HET MSE A 219 8
HET MSE A 238 8
HET MSE B 98 8
HET MSE B 112 8
HET MSE B 136 8
HET MSE B 219 8
HET MSE B 238 8
HET MSE C 98 8
HET MSE C 112 8
HET MSE C 136 8
HET MSE C 219 8
HET MSE C 238 8
HET MSE D 1 8
HET MSE D 98 8
HET MSE D 112 8
HET MSE D 136 8
HET MSE D 219 8
HET MSE D 238 8
HET SO4 B 323 5
HET SO4 A 323 5
HET SO4 D 323 5
HET SO4 C 323 5
HET SO4 A 324 5
HET SO4 C 324 5
HET SO4 D 324 5
HET SO4 B 324 5
HET NAD A 400 44
HET NAD B 400 44
HET NAD C 400 44
HET NAD D 400 44
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 13 NAD 4(C21 H27 N7 O14 P2)
FORMUL 17 HOH *280(H2 O)
HELIX 1 1 GLY A 12 LYS A 23 1 12
HELIX 2 2 GLY A 39 ASP A 50 1 12
HELIX 3 3 PRO A 54 SER A 65 1 12
HELIX 4 4 GLU A 68 HIS A 77 1 10
HELIX 5 5 SER A 89 GLY A 103 1 15
HELIX 6 6 ASP A 104 LEU A 116 1 13
HELIX 7 7 SER A 147 GLY A 152 5 6
HELIX 8 8 LEU A 168 ALA A 178 1 11
HELIX 9 9 SER A 191 LEU A 197 1 7
HELIX 10 10 GLY A 200 SER A 208 1 9
HELIX 11 11 THR A 229 GLY A 242 1 14
HELIX 12 12 SER A 257 LYS A 266 1 10
HELIX 13 13 ASP A 275 LEU A 282 1 8
HELIX 14 14 ASN A 302 GLU A 312 1 11
HELIX 15 15 GLY B 12 LYS B 23 1 12
HELIX 16 16 GLY B 39 ASP B 50 1 12
HELIX 17 17 PRO B 54 SER B 65 1 12
HELIX 18 18 GLU B 68 HIS B 77 1 10
HELIX 19 19 SER B 89 GLY B 103 1 15
HELIX 20 20 ASP B 104 LEU B 116 1 13
HELIX 21 21 SER B 147 GLY B 152 5 6
HELIX 22 22 LEU B 168 LYS B 177 1 10
HELIX 23 23 SER B 191 LEU B 197 1 7
HELIX 24 24 GLY B 200 SER B 208 1 9
HELIX 25 25 THR B 229 GLY B 242 1 14
HELIX 26 26 SER B 257 LYS B 266 1 10
HELIX 27 27 ASP B 275 LEU B 282 1 8
HELIX 28 28 ASN B 302 LEU B 311 1 10
HELIX 29 29 GLY C 12 LYS C 23 1 12
HELIX 30 30 GLY C 39 ASP C 50 1 12
HELIX 31 31 PRO C 54 SER C 65 1 12
HELIX 32 32 GLU C 68 HIS C 77 1 10
HELIX 33 33 SER C 89 GLY C 103 1 15
HELIX 34 34 ASP C 104 LEU C 116 1 13
HELIX 35 35 SER C 147 GLY C 152 5 6
HELIX 36 36 LEU C 168 ALA C 178 1 11
HELIX 37 37 SER C 191 LEU C 197 1 7
HELIX 38 38 GLY C 200 SER C 208 1 9
HELIX 39 39 THR C 229 GLY C 242 1 14
HELIX 40 40 SER C 257 LYS C 266 1 10
HELIX 41 41 ASP C 275 LEU C 282 1 8
HELIX 42 42 ASN C 302 GLU C 312 1 11
HELIX 43 43 GLY D 12 LYS D 23 1 12
HELIX 44 44 GLY D 39 ASP D 50 1 12
HELIX 45 45 PRO D 54 SER D 65 1 12
HELIX 46 46 GLU D 68 HIS D 77 1 10
HELIX 47 47 SER D 89 GLY D 103 1 15
HELIX 48 48 ASP D 104 LEU D 116 1 13
HELIX 49 49 SER D 147 GLY D 152 5 6
HELIX 50 50 LEU D 168 ALA D 178 1 11
HELIX 51 51 VAL D 192 LEU D 197 1 6
HELIX 52 52 GLY D 200 SER D 208 1 9
HELIX 53 53 THR D 229 GLY D 242 1 14
HELIX 54 54 SER D 257 LYS D 266 1 10
HELIX 55 55 ASP D 275 LEU D 282 1 8
HELIX 56 56 ASN D 302 GLU D 312 1 11
SHEET 1 A 7 LYS A 121 PRO A 124 0
SHEET 2 A 7 VAL A 27 VAL A 33 1 N ALA A 31 O LEU A 123
SHEET 3 A 7 LYS A 4 GLY A 10 1 N VAL A 8 O ILE A 32
SHEET 4 A 7 VAL A 180 ILE A 183 1 O VAL A 182 N ILE A 7
SHEET 5 A 7 ARG A 211 ILE A 215 1 O ILE A 215 N ILE A 183
SHEET 6 A 7 ASP A 248 HIS A 252 1 O LEU A 250 N TYR A 214
SHEET 7 A 7 GLY A 285 ASP A 289 1 O GLY A 285 N ILE A 249
SHEET 1 B 3 ILE A 141 THR A 143 0
SHEET 2 B 3 ILE A 131 MSE A 136 -1 N GLY A 134 O VAL A 142
SHEET 3 B 3 ILE A 155 THR A 161 -1 O THR A 161 N ILE A 131
SHEET 1 C 2 VAL A 292 LEU A 293 0
SHEET 2 C 2 ARG A 300 HIS A 301 -1 O ARG A 300 N LEU A 293
SHEET 1 D 7 LYS B 121 PRO B 124 0
SHEET 2 D 7 VAL B 27 VAL B 33 1 N ALA B 31 O LEU B 123
SHEET 3 D 7 LYS B 4 GLY B 10 1 N VAL B 8 O ILE B 32
SHEET 4 D 7 VAL B 180 ILE B 183 1 O VAL B 182 N ILE B 7
SHEET 5 D 7 ARG B 211 ILE B 215 1 O ARG B 211 N ILE B 181
SHEET 6 D 7 ASP B 248 HIS B 252 1 O LEU B 250 N TYR B 214
SHEET 7 D 7 GLY B 285 ASP B 289 1 O GLY B 285 N ILE B 249
SHEET 1 E 3 ILE B 141 THR B 143 0
SHEET 2 E 3 ILE B 131 MSE B 136 -1 N GLY B 134 O VAL B 142
SHEET 3 E 3 ILE B 155 THR B 161 -1 O ARG B 157 N GLU B 135
SHEET 1 F 2 VAL B 292 LEU B 293 0
SHEET 2 F 2 ARG B 300 HIS B 301 -1 O ARG B 300 N LEU B 293
SHEET 1 G 7 LYS C 121 PRO C 124 0
SHEET 2 G 7 VAL C 27 VAL C 33 1 N ALA C 31 O LEU C 123
SHEET 3 G 7 LYS C 4 GLY C 10 1 N VAL C 6 O SER C 28
SHEET 4 G 7 VAL C 180 ILE C 183 1 O VAL C 182 N ILE C 7
SHEET 5 G 7 ARG C 211 ILE C 215 1 O ARG C 211 N ILE C 181
SHEET 6 G 7 ASP C 248 HIS C 252 1 O LEU C 250 N TYR C 214
SHEET 7 G 7 GLY C 285 ASP C 289 1 O GLY C 285 N ILE C 249
SHEET 1 H 3 ILE C 141 THR C 143 0
SHEET 2 H 3 ILE C 131 MSE C 136 -1 N GLY C 134 O VAL C 142
SHEET 3 H 3 ILE C 155 THR C 161 -1 O LYS C 156 N GLU C 135
SHEET 1 I 2 VAL C 292 GLU C 294 0
SHEET 2 I 2 LEU C 299 HIS C 301 -1 O ARG C 300 N LEU C 293
SHEET 1 J 7 LYS D 121 PRO D 124 0
SHEET 2 J 7 VAL D 27 VAL D 33 1 N ALA D 31 O LEU D 123
SHEET 3 J 7 LYS D 4 GLY D 10 1 N VAL D 8 O ILE D 32
SHEET 4 J 7 VAL D 180 ILE D 183 1 O VAL D 182 N ILE D 7
SHEET 5 J 7 ARG D 211 ILE D 215 1 O ARG D 211 N ILE D 181
SHEET 6 J 7 ASP D 248 HIS D 252 1 O LEU D 250 N TYR D 214
SHEET 7 J 7 GLY D 285 ASP D 289 1 O GLY D 285 N ILE D 249
SHEET 1 K 3 ILE D 141 THR D 143 0
SHEET 2 K 3 ILE D 131 MSE D 136 -1 N GLY D 134 O VAL D 142
SHEET 3 K 3 ILE D 155 THR D 161 -1 O THR D 161 N ILE D 131
SHEET 1 L 2 VAL D 292 GLU D 294 0
SHEET 2 L 2 LEU D 299 HIS D 301 -1 O ARG D 300 N LEU D 293
LINK C GLY A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C GLY A 97 N MSE A 98 1555 1555 1.32
LINK C MSE A 98 N THR A 99 1555 1555 1.34
LINK C GLU A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N SER A 113 1555 1555 1.32
LINK C GLU A 135 N MSE A 136 1555 1555 1.33
LINK C MSE A 136 N GLU A 137 1555 1555 1.33
LINK C VAL A 218 N MSE A 219 1555 1555 1.33
LINK C MSE A 219 N THR A 220 1555 1555 1.33
LINK C ILE A 237 N MSE A 238 1555 1555 1.33
LINK C MSE A 238 N ASP A 239 1555 1555 1.33
LINK C GLY B 97 N MSE B 98 1555 1555 1.33
LINK C MSE B 98 N THR B 99 1555 1555 1.33
LINK C GLU B 111 N MSE B 112 1555 1555 1.34
LINK C MSE B 112 N SER B 113 1555 1555 1.32
LINK C GLU B 135 N MSE B 136 1555 1555 1.32
LINK C MSE B 136 N GLU B 137 1555 1555 1.33
LINK C VAL B 218 N MSE B 219 1555 1555 1.33
LINK C MSE B 219 N THR B 220 1555 1555 1.33
LINK C ILE B 237 N MSE B 238 1555 1555 1.32
LINK C MSE B 238 N ASP B 239 1555 1555 1.32
LINK OE1 GLU B 267 N7A NAD B 400 1555 1555 2.01
LINK C GLY C 97 N MSE C 98 1555 1555 1.33
LINK C MSE C 98 N THR C 99 1555 1555 1.34
LINK C GLU C 111 N MSE C 112 1555 1555 1.33
LINK C MSE C 112 N SER C 113 1555 1555 1.32
LINK C GLU C 135 N MSE C 136 1555 1555 1.32
LINK C MSE C 136 N GLU C 137 1555 1555 1.33
LINK C VAL C 218 N MSE C 219 1555 1555 1.33
LINK C MSE C 219 N THR C 220 1555 1555 1.33
LINK C ILE C 237 N MSE C 238 1555 1555 1.32
LINK C MSE C 238 N ASP C 239 1555 1555 1.33
LINK C MSE D 1 N LYS D 2 1555 1555 1.33
LINK C GLY D 97 N MSE D 98 1555 1555 1.32
LINK C MSE D 98 N THR D 99 1555 1555 1.33
LINK C GLU D 111 N MSE D 112 1555 1555 1.32
LINK C MSE D 112 N SER D 113 1555 1555 1.34
LINK C GLU D 135 N MSE D 136 1555 1555 1.32
LINK C MSE D 136 N GLU D 137 1555 1555 1.34
LINK C VAL D 218 N MSE D 219 1555 1555 1.33
LINK C MSE D 219 N THR D 220 1555 1555 1.33
LINK C ILE D 237 N MSE D 238 1555 1555 1.32
LINK C MSE D 238 N ASP D 239 1555 1555 1.32
CISPEP 1 THR A 161 PRO A 162 0 -4.01
CISPEP 2 GLY A 184 PRO A 185 0 5.23
CISPEP 3 THR B 161 PRO B 162 0 -1.25
CISPEP 4 GLY B 184 PRO B 185 0 6.18
CISPEP 5 THR C 161 PRO C 162 0 -9.79
CISPEP 6 GLY C 184 PRO C 185 0 3.91
CISPEP 7 THR D 161 PRO D 162 0 -2.78
CISPEP 8 GLY D 184 PRO D 185 0 4.47
SITE 1 AC1 5 SER B 41 SER B 42 ARG B 58 ARG B 78
SITE 2 AC1 5 ASN B 92
SITE 1 AC2 6 GLY A 40 SER A 41 SER A 42 ARG A 58
SITE 2 AC2 6 ARG A 78 ASN A 92
SITE 1 AC3 7 SER D 41 SER D 42 ARG D 58 ARG D 78
SITE 2 AC3 7 ASN D 92 HOH D 438 HOH D 469
SITE 1 AC4 6 SER C 41 SER C 42 ARG C 58 ARG C 78
SITE 2 AC4 6 ASN C 92 HOH C 463
SITE 1 AC5 9 GLY A 11 GLY A 12 THR A 13 GLY A 14
SITE 2 AC5 9 GLY A 186 SER A 187 SER A 191 NAD A 400
SITE 3 AC5 9 HOH A 448
SITE 1 AC6 9 GLY C 11 GLY C 12 THR C 13 GLY C 14
SITE 2 AC6 9 GLY C 186 SER C 187 SER C 191 NAD C 400
SITE 3 AC6 9 HOH C 406
SITE 1 AC7 9 GLY D 11 GLY D 12 THR D 13 GLY D 186
SITE 2 AC7 9 SER D 187 SER D 191 NAD D 400 HOH D 403
SITE 3 AC7 9 HOH D 467
SITE 1 AC8 9 GLY B 11 GLY B 12 THR B 13 GLY B 186
SITE 2 AC8 9 SER B 187 SER B 191 NAD B 400 HOH B 406
SITE 3 AC8 9 HOH B 465
SITE 1 AC9 16 THR A 13 GLY A 14 GLY A 186 SER A 187
SITE 2 AC9 16 ASN A 217 VAL A 218 MSE A 219 GLN A 221
SITE 3 AC9 16 LYS A 263 TYR A 264 GLU A 267 VAL A 298
SITE 4 AC9 16 ARG A 300 HIS A 301 SO4 A 324 HOH A 418
SITE 1 BC1 17 THR B 13 GLY B 14 GLY B 186 SER B 187
SITE 2 BC1 17 ASN B 217 VAL B 218 MSE B 219 GLN B 221
SITE 3 BC1 17 LYS B 263 TYR B 264 GLU B 267 VAL B 298
SITE 4 BC1 17 ARG B 300 HIS B 301 SO4 B 324 HOH B 424
SITE 5 BC1 17 HOH B 456
SITE 1 BC2 17 THR C 13 GLY C 14 GLY C 186 SER C 187
SITE 2 BC2 17 ASN C 217 VAL C 218 MSE C 219 GLN C 221
SITE 3 BC2 17 LYS C 263 TYR C 264 GLU C 267 VAL C 298
SITE 4 BC2 17 ARG C 300 HIS C 301 SO4 C 324 HOH C 417
SITE 5 BC2 17 HOH C 438
SITE 1 BC3 17 THR D 13 GLY D 14 GLY D 186 SER D 187
SITE 2 BC3 17 ASN D 217 VAL D 218 MSE D 219 GLN D 221
SITE 3 BC3 17 LYS D 263 TYR D 264 GLU D 267 VAL D 298
SITE 4 BC3 17 ARG D 300 HIS D 301 SO4 D 324 HOH D 431
SITE 5 BC3 17 HOH D 474
CRYST1 51.430 143.640 233.680 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019440 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004280 0.00000
ATOM 1 N GLY A 0 59.503 104.175 73.553 1.00 70.17 N
ATOM 2 CA GLY A 0 60.756 104.864 73.108 1.00 73.43 C
ATOM 3 C GLY A 0 61.867 103.917 72.653 1.00 75.28 C
ATOM 4 O GLY A 0 62.586 104.188 71.668 1.00 75.88 O
HETATM 5 N MSE A 1 62.017 102.818 73.398 1.00 75.74 N
HETATM 6 CA MSE A 1 62.940 101.737 73.070 1.00 74.24 C
HETATM 7 C MSE A 1 62.128 100.616 72.408 1.00 73.14 C
HETATM 8 O MSE A 1 61.002 100.318 72.829 1.00 71.68 O
HETATM 9 CB MSE A 1 63.651 101.219 74.344 1.00 73.98 C
ATOM 10 N LYS A 2 62.684 100.035 71.345 1.00 72.62 N
ATOM 11 CA LYS A 2 62.188 98.764 70.812 1.00 71.25 C
ATOM 12 C LYS A 2 62.838 97.711 71.698 1.00 68.56 C
ATOM 13 O LYS A 2 64.067 97.545 71.696 1.00 65.95 O
ATOM 14 CB LYS A 2 62.581 98.546 69.335 1.00 72.17 C
ATOM 15 CG LYS A 2 61.596 97.683 68.505 1.00 72.65 C
ATOM 16 CD LYS A 2 61.446 96.257 69.051 1.00 76.11 C
ATOM 17 CE LYS A 2 60.538 95.372 68.171 1.00 76.34 C
ATOM 18 NZ LYS A 2 60.374 93.947 68.653 1.00 68.39 N
ATOM 19 N LYS A 3 62.015 97.043 72.496 1.00 65.39 N
ATOM 20 CA LYS A 3 62.480 95.925 73.293 1.00 61.81 C
ATOM 21 C LYS A 3 62.461 94.667 72.415 1.00 59.72 C
ATOM 22 O LYS A 3 61.424 94.340 71.831 1.00 60.03 O
ATOM 23 CB LYS A 3 61.589 95.774 74.517 1.00 60.86 C
ATOM 24 CG LYS A 3 61.652 96.966 75.458 1.00 61.00 C
ATOM 25 CD LYS A 3 60.532 96.901 76.500 1.00 63.76 C
ATOM 26 CE LYS A 3 60.734 97.901 77.644 1.00 60.56 C
ATOM 27 NZ LYS A 3 61.979 97.594 78.393 1.00 57.49 N
ATOM 28 N LYS A 4 63.603 93.976 72.310 1.00 57.83 N
ATOM 29 CA LYS A 4 63.667 92.730 71.548 1.00 56.44 C
ATOM 30 C LYS A 4 62.823 91.738 72.340 1.00 53.78 C
ATOM 31 O LYS A 4 62.870 91.728 73.567 1.00 52.54 O
ATOM 32 CB LYS A 4 65.093 92.192 71.420 1.00 56.88 C
ATOM 33 CG LYS A 4 65.879 92.642 70.207 1.00 58.40 C
ATOM 34 CD LYS A 4 67.364 92.298 70.413 1.00 60.07 C
ATOM 35 CE LYS A 4 68.249 92.603 69.190 1.00 63.23 C
ATOM 36 NZ LYS A 4 68.667 91.373 68.429 1.00 65.91 N
ATOM 37 N ASN A 5 62.017 90.943 71.646 1.00 51.60 N
ATOM 38 CA ASN A 5 61.229 89.893 72.295 1.00 49.22 C
ATOM 39 C ASN A 5 62.060 88.637 72.484 1.00 46.37 C
ATOM 40 O ASN A 5 62.531 88.066 71.507 1.00 45.53 O
ATOM 41 CB ASN A 5 60.012 89.513 71.466 1.00 49.50 C
ATOM 42 CG ASN A 5 58.911 90.539 71.531 1.00 49.91 C
ATOM 43 OD1 ASN A 5 58.792 91.301 72.486 1.00 50.53 O
ATOM 44 ND2 ASN A 5 58.092 90.563 70.496 1.00 48.39 N
ATOM 45 N VAL A 6 62.215 88.216 73.738 1.00 43.17 N
ATOM 46 CA VAL A 6 63.009 87.047 74.088 1.00 41.44 C
ATOM 47 C VAL A 6 62.157 86.007 74.805 1.00 42.45 C
ATOM 48 O VAL A 6 61.452 86.317 75.755 1.00 39.79 O
ATOM 49 CB VAL A 6 64.181 87.429 74.992 1.00 40.82 C
ATOM 50 CG1 VAL A 6 64.987 86.197 75.370 1.00 32.05 C
ATOM 51 CG2 VAL A 6 65.050 88.460 74.296 1.00 38.47 C
ATOM 52 N ILE A 7 62.220 84.778 74.319 1.00 45.86 N
ATOM 53 CA ILE A 7 61.542 83.676 74.952 1.00 46.25 C
ATOM 54 C ILE A 7 62.600 82.725 75.505 1.00 43.13 C
ATOM 55 O ILE A 7 63.572 82.420 74.836 1.00 39.17 O
ATOM 56 CB ILE A 7 60.584 82.970 73.974 1.00 46.23 C
ATOM 57 CG1 ILE A 7 59.876 81.821 74.676 1.00 50.82 C
ATOM 58 CG2 ILE A 7 61.324 82.430 72.792 1.00 44.28 C
ATOM 59 CD1 ILE A 7 58.426 81.729 74.314 1.00 56.35 C
ATOM 60 N VAL A 8 62.424 82.303 76.750 1.00 38.24 N
ATOM 61 CA VAL A 8 63.362 81.412 77.432 1.00 36.64 C
ATOM 62 C VAL A 8 62.651 80.159 77.939 1.00 36.53 C
ATOM 63 O VAL A 8 61.600 80.240 78.577 1.00 35.68 O