HEADER TRANSFERASE 12-NOV-07 3BCA
TITLE CRYSTAL STRUCTURE OF MOUSE SELENOCYSTEINE SYNTHASE, SODIUM IODIDE SOAK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: O-PHOSPHOSERYL-TRNA(SEC) SELENIUM TRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ELASTASE-RESISTANT FRAGMENT: RESIDUES 19-468;
COMPND 5 SYNONYM: SELENOCYSTEINE SYNTHASE, SEC SYNTHASE, SELENOCYSTEINYL-
COMPND 6 TRNA(SEC) SYNTHASE, SEP-TRNA:SEC-TRNA SYNTHASE, SEPSECS, UGA
COMPND 7 SUPPRESSOR TRNA-ASSOCIATED PROTEIN;
COMPND 8 EC: 2.9.1.-;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SEPSECS, D5ERTD135E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM-13-SECS
KEYWDS DISORDER-ORDER TRANSITION, PHOSPHATE-LOOP, PYRIDOXAL PHOSPHATE,
KEYWDS 2 SELENOCYSTEINE SYNTHASE (SECS, SEPSECS), SOLUBLE LIVER ANTIGEN/LIVER
KEYWDS 3 AND PANCREAS ANTIGEN (SLA/LP), PROTEIN BIOSYNTHESIS, SELENIUM,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.M.GANICHKIN,M.C.WAHL
REVDAT 5 25-OCT-17 3BCA 1 REMARK
REVDAT 4 13-JUL-11 3BCA 1 VERSN
REVDAT 3 24-FEB-09 3BCA 1 VERSN
REVDAT 2 18-MAR-08 3BCA 1 JRNL
REVDAT 1 18-DEC-07 3BCA 0
JRNL AUTH O.M.GANICHKIN,X.M.XU,B.A.CARLSON,H.MIX,D.L.HATFIELD,
JRNL AUTH 2 V.N.GLADYSHEV,M.C.WAHL
JRNL TITL STRUCTURE AND CATALYTIC MECHANISM OF EUKARYOTIC
JRNL TITL 2 SELENOCYSTEINE SYNTHASE.
JRNL REF J.BIOL.CHEM. V. 283 5849 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18093968
JRNL DOI 10.1074/JBC.M709342200
REMARK 2
REMARK 2 RESOLUTION. 2.25 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 26104
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1382
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 264
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 32.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.25000
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): 0.247
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.207
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.454
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3506 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4742 ; 1.229 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 443 ; 5.631 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;34.993 ;23.378
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 627 ;14.689 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.950 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 538 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2607 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1719 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2439 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 250 ; 0.168 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.101 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 111 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 34 ; 0.179 ; 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): 2207 ; 0.423 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3534 ; 0.782 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1378 ; 1.411 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1208 ; 2.358 ; 4.500
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 106
REMARK 3 ORIGIN FOR THE GROUP (A): 43.3300 61.2750 -0.1400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0072 T22: -0.1166
REMARK 3 T33: -0.1198 T12: -0.0189
REMARK 3 T13: 0.0133 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.4119 L22: 1.2835
REMARK 3 L33: 2.0809 L12: 0.3942
REMARK 3 L13: 0.4458 L23: 0.8102
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: -0.0559 S13: 0.0504
REMARK 3 S21: -0.0142 S22: -0.0301 S23: -0.2120
REMARK 3 S31: -0.0319 S32: 0.2292 S33: -0.0211
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 107 A 345
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8400 37.1050 15.5230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: -0.1236
REMARK 3 T33: -0.1724 T12: -0.0052
REMARK 3 T13: -0.0364 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.4731 L22: 0.9111
REMARK 3 L33: 0.7716 L12: 0.0393
REMARK 3 L13: -0.1884 L23: -0.3377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: -0.0561 S13: -0.0619
REMARK 3 S21: 0.0692 S22: -0.0108 S23: -0.0738
REMARK 3 S31: 0.0893 S32: 0.0481 S33: -0.0177
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 346 A 466
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0400 45.1710 25.9010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0201 T22: -0.0727
REMARK 3 T33: -0.1913 T12: -0.0105
REMARK 3 T13: 0.0166 T23: 0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 1.8336 L22: 1.3218
REMARK 3 L33: 1.5093 L12: -0.2982
REMARK 3 L13: -0.7850 L23: -0.1174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0518 S12: 0.1395 S13: -0.0992
REMARK 3 S21: 0.0117 S22: 0.0296 S23: 0.1853
REMARK 3 S31: -0.0882 S32: -0.2970 S33: -0.0814
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED IN PHASING.
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 3BCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045344.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : OSMIC
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52394
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11 % (V/V) ETHYLENE GLYCOL, SOAKED IN
REMARK 280 0.5 M NAI, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.61100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.18550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.76000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.61100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.18550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.76000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.61100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.18550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.76000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.61100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.18550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.76000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18960 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 59.22200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 138.37100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 59.22200
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 138.37100
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 598 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 19
REMARK 465 GLN A 20
REMARK 465 GLY A 21
REMARK 465 CYS A 22
REMARK 465 ARG A 97
REMARK 465 SER A 98
REMARK 465 GLY A 99
REMARK 465 ASP A 100
REMARK 465 ILE A 101
REMARK 465 SER A 102
REMARK 465 ALA A 103
REMARK 465 VAL A 104
REMARK 465 ARG A 467
REMARK 465 ALA A 468
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 OE2 GLU A 43 I IOD A 537 1.74
REMARK 500 O HOH A 703 O HOH A 711 2.11
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 VAL A 131 79.81 -104.72
REMARK 500 THR A 224 -99.90 -92.95
REMARK 500 SER A 415 59.15 30.59
REMARK 500 MET A 423 -22.00 102.07
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 IOD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 533
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 536
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 537
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 538
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 539
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 540
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 541
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 543
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 546
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 547
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 549
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 560
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 561
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 562
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BC8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE SELENOCYSTEINE SYNTHASE
REMARK 900 RELATED ID: 3BCB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE SELENOCYSTEINE SYNTHASE, SODIUM
REMARK 900 PHOSPHATE SOAK
DBREF 3BCA A 19 468 UNP Q6P6M7 SPCS_MOUSE 19 468
SEQRES 1 A 450 ARG GLN GLY CYS GLU ALA ARG ARG ALA HIS GLU HIS LEU
SEQRES 2 A 450 ILE ARG LEU LEU LEU GLU GLN GLY LYS CYS PRO GLU ASP
SEQRES 3 A 450 GLY TRP ASP GLU SER THR LEU GLU LEU PHE LEU HIS GLU
SEQRES 4 A 450 LEU ALA VAL MET ASP SER ASN ASN PHE LEU GLY ASN CYS
SEQRES 5 A 450 GLY VAL GLY GLU ARG GLU GLY ARG VAL ALA SER ALA LEU
SEQRES 6 A 450 VAL ALA ARG ARG HIS TYR ARG PHE ILE HIS GLY ILE GLY
SEQRES 7 A 450 ARG SER GLY ASP ILE SER ALA VAL GLN PRO LYS ALA ALA
SEQRES 8 A 450 GLY SER SER LEU LEU ASN LYS ILE THR ASN SER LEU VAL
SEQRES 9 A 450 LEU ASN VAL ILE LYS LEU ALA GLY VAL HIS SER VAL ALA
SEQRES 10 A 450 SER CYS PHE VAL VAL PRO MET ALA THR GLY MET SER LEU
SEQRES 11 A 450 THR LEU CYS PHE LEU THR LEU ARG HIS LYS ARG PRO LYS
SEQRES 12 A 450 ALA LYS TYR ILE ILE TRP PRO ARG ILE ASP GLN LYS SER
SEQRES 13 A 450 CYS PHE LYS SER MET VAL THR ALA GLY PHE GLU PRO VAL
SEQRES 14 A 450 VAL ILE GLU ASN VAL LEU GLU GLY ASP GLU LEU ARG THR
SEQRES 15 A 450 ASP LEU LYS ALA VAL GLU ALA LYS ILE GLN GLU LEU GLY
SEQRES 16 A 450 PRO GLU HIS ILE LEU CYS LEU HIS SER THR THR ALA CYS
SEQRES 17 A 450 PHE ALA PRO ARG VAL PRO ASP ARG LEU GLU GLU LEU ALA
SEQRES 18 A 450 VAL ILE CYS ALA ASN TYR ASP ILE PRO HIS VAL VAL ASN
SEQRES 19 A 450 ASN ALA TYR GLY LEU GLN SER SER LYS CYS MET HIS LEU
SEQRES 20 A 450 ILE GLN GLN GLY ALA ARG VAL GLY ARG ILE ASP ALA PHE
SEQRES 21 A 450 VAL GLN SER LEU ASP LLP ASN PHE MET VAL PRO VAL GLY
SEQRES 22 A 450 GLY ALA ILE ILE ALA GLY PHE ASN GLU PRO PHE ILE GLN
SEQRES 23 A 450 ASP ILE SER LYS MET TYR PRO GLY ARG ALA SER ALA SER
SEQRES 24 A 450 PRO SER LEU ASP VAL LEU ILE THR LEU LEU SER LEU GLY
SEQRES 25 A 450 CYS SER GLY TYR ARG LYS LEU LEU LYS GLU ARG LYS GLU
SEQRES 26 A 450 MET PHE VAL TYR LEU SER THR GLN LEU LYS LYS LEU ALA
SEQRES 27 A 450 GLU ALA HIS ASN GLU ARG LEU LEU GLN THR PRO HIS ASN
SEQRES 28 A 450 PRO ILE SER LEU ALA MET THR LEU LYS THR ILE ASP GLY
SEQRES 29 A 450 HIS HIS ASP LYS ALA VAL THR GLN LEU GLY SER MET LEU
SEQRES 30 A 450 PHE THR ARG GLN VAL SER GLY ALA ARG ALA VAL PRO LEU
SEQRES 31 A 450 GLY ASN VAL GLN THR VAL SER GLY HIS THR PHE ARG GLY
SEQRES 32 A 450 PHE MET SER HIS ALA ASP ASN TYR PRO CYS ALA TYR LEU
SEQRES 33 A 450 ASN ALA ALA ALA ALA ILE GLY MET LYS MET GLN ASP VAL
SEQRES 34 A 450 ASP LEU PHE ILE LYS ARG LEU ASP LYS CYS LEU ASN ILE
SEQRES 35 A 450 VAL ARG LYS GLU GLN THR ARG ALA
MODRES 3BCA LLP A 284 LYS
HET LLP A 284 24
HET IOD A 501 1
HET IOD A 502 1
HET IOD A 503 1
HET IOD A 504 1
HET IOD A 505 1
HET IOD A 506 1
HET IOD A 507 1
HET IOD A 508 2
HET IOD A 509 1
HET IOD A 510 2
HET IOD A 511 1
HET IOD A 512 1
HET IOD A 513 1
HET IOD A 514 1
HET IOD A 515 1
HET IOD A 516 1
HET IOD A 517 1
HET IOD A 518 1
HET IOD A 519 2
HET IOD A 520 1
HET IOD A 521 1
HET IOD A 522 1
HET IOD A 523 2
HET IOD A 524 1
HET IOD A 525 1
HET IOD A 526 1
HET IOD A 527 2
HET IOD A 528 2
HET IOD A 529 1
HET IOD A 530 1
HET IOD A 531 1
HET IOD A 532 1
HET IOD A 533 1
HET IOD A 534 1
HET IOD A 535 2
HET IOD A 536 1
HET IOD A 537 1
HET IOD A 538 1
HET IOD A 539 1
HET IOD A 540 1
HET IOD A 541 1
HET IOD A 542 2
HET IOD A 543 1
HET IOD A 544 1
HET IOD A 545 1
HET IOD A 546 1
HET IOD A 547 1
HET IOD A 548 1
HET IOD A 549 2
HET IOD A 550 1
HET IOD A 551 1
HET IOD A 552 2
HET IOD A 553 1
HET IOD A 554 1
HET IOD A 555 2
HET IOD A 556 1
HET IOD A 557 1
HET IOD A 558 1
HET IOD A 559 2
HET IOD A 560 1
HET IOD A 561 1
HET IOD A 562 1
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM IOD IODIDE ION
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP C14 H22 N3 O7 P
FORMUL 2 IOD 62(I 1-)
FORMUL 64 HOH *264(H2 O)
HELIX 1 1 GLU A 23 GLY A 39 1 17
HELIX 2 2 ASP A 47 VAL A 60 1 14
HELIX 3 3 MET A 61 PHE A 66 5 6
HELIX 4 4 SER A 81 HIS A 88 1 8
HELIX 5 5 ALA A 108 GLY A 130 1 23
HELIX 6 6 ALA A 143 ARG A 159 1 17
HELIX 7 7 GLN A 172 ALA A 182 1 11
HELIX 8 8 ASP A 201 GLY A 213 1 13
HELIX 9 9 ARG A 234 ASP A 246 1 13
HELIX 10 10 SER A 259 GLY A 273 1 15
HELIX 11 11 LEU A 282 MET A 287 1 6
HELIX 12 12 ASN A 299 TYR A 310 1 12
HELIX 13 13 ALA A 316 HIS A 359 1 44
HELIX 14 14 LYS A 386 ARG A 398 1 13
HELIX 15 15 LYS A 443 GLN A 465 1 23
SHEET 1 A 7 SER A 136 VAL A 140 0
SHEET 2 A 7 ALA A 293 GLY A 297 -1 O ALA A 293 N VAL A 140
SHEET 3 A 7 ALA A 277 SER A 281 -1 N GLN A 280 O ILE A 294
SHEET 4 A 7 HIS A 249 ASN A 252 1 N VAL A 251 O ALA A 277
SHEET 5 A 7 ILE A 217 THR A 223 1 N LEU A 220 O VAL A 250
SHEET 6 A 7 TYR A 164 PRO A 168 1 N TYR A 164 O LEU A 218
SHEET 7 A 7 GLU A 185 ILE A 189 1 O VAL A 187 N ILE A 165
SHEET 1 B 2 VAL A 192 GLU A 194 0
SHEET 2 B 2 GLU A 197 ARG A 199 -1 O ARG A 199 N VAL A 192
SHEET 1 C 3 SER A 372 THR A 376 0
SHEET 2 C 3 TYR A 433 ALA A 437 -1 O LEU A 434 N MET A 375
SHEET 3 C 3 ARG A 404 VAL A 406 -1 N ARG A 404 O ASN A 435
SHEET 1 D 2 VAL A 411 VAL A 414 0
SHEET 2 D 2 HIS A 417 ARG A 420 -1 O PHE A 419 N GLN A 412
LINK C ASP A 283 N LLP A 284 1555 1555 1.33
LINK C LLP A 284 N ASN A 285 1555 1555 1.33
CISPEP 1 GLN A 105 PRO A 106 0 6.83
CISPEP 2 ALA A 228 PRO A 229 0 6.81
SITE 1 AC1 2 ARG A 75 HOH A 797
SITE 1 AC2 2 LYS A 173 HOH A 624
SITE 1 AC3 1 GLY A 312
SITE 1 AC4 1 LYS A 158
SITE 1 AC5 2 GLY A 68 GLN A 399
SITE 1 AC6 3 LEU A 202 ARG A 234 THR A 379
SITE 1 AC7 1 ALA A 80
SITE 1 AC8 1 ASN A 428
SITE 1 AC9 1 LYS A 177
SITE 1 BC1 1 LYS A 177
SITE 1 BC2 2 GLY A 213 GLU A 215
SITE 1 BC3 1 HOH A 688
SITE 1 BC4 3 SER A 259 ARG A 341 LYS A 342
SITE 1 BC5 1 ARG A 271
SITE 1 BC6 1 LYS A 456
SITE 1 BC7 3 CYS A 41 ASN A 124 CYS A 331
SITE 1 BC8 1 LYS A 127
SITE 1 BC9 2 LYS A 339 HOH A 731
SITE 1 CC1 2 THR A 350 GLN A 351
SITE 1 CC2 1 CYS A 431
SITE 1 CC3 2 THR A 389 PRO A 407
SITE 1 CC4 1 HOH A 657
SITE 1 CC5 1 ASP A 455
SITE 1 CC6 4 SER A 393 THR A 397 ARG A 398 HOH A 666
SITE 1 CC7 2 ASN A 119 HOH A 654
SITE 1 CC8 2 MET A 444 GLN A 445
SITE 1 CC9 2 HOH A 580 HOH A 620
SITE 1 DC1 3 GLU A 43 SER A 332 ARG A 335
SITE 1 DC2 1 ARG A 453
SITE 1 DC3 1 VAL A 79
SITE 1 DC4 2 GLY A 96 SER A 112
SITE 1 DC5 1 SER A 112
SITE 1 DC6 1 HOH A 640
SITE 1 DC7 2 LYS A 163 HIS A 216
SITE 1 DC8 2 LYS A 261 CYS A 262
SITE 1 DC9 2 GLU A 48 SER A 49
SITE 1 EC1 1 GLU A 29
SITE 1 EC2 2 SER A 133 GLN A 267
SITE 1 EC3 2 SER A 260 HOH A 683
SITE 1 EC4 1 LYS A 208
SITE 1 EC5 2 LYS A 116 ILE A 117
SITE 1 EC6 1 LYS A 386
SITE 1 EC7 1 SER A 393
SITE 1 EC8 1 CYS A 137
SITE 1 EC9 1 GLN A 304
CRYST1 59.222 138.371 141.520 90.00 90.00 90.00 I 2 2 2 8
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 0.016886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007066 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
