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HEADER HYDROLASE 09-JUL-07 2QJW
TITLE CRYSTAL STRUCTURE OF A PUTATIVE HYDROLASE OF THE ALPHA/BETA
TITLE 2 SUPERFAMILY (XCC1541) FROM XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS AT
TITLE 3 1.35 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN XCC1541;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS;
SOURCE 3 ORGANISM_TAXID: 340;
SOURCE 4 STRAIN: NCPPB 528, LMG 568;
SOURCE 5 ATCC: 33913;
SOURCE 6 GENE: NP_636912.1, XCC1541;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PUTATIVE HYDROLASE OF THE ALPHA/BETA SUPERFAMILY, STRUCTURAL
KEYWDS 2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 3 28-JUL-10 2QJW 1 HEADER TITLE KEYWDS
REVDAT 2 24-FEB-09 2QJW 1 VERSN
REVDAT 1 24-JUL-07 2QJW 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF UNCHARACTERIZED PROTEIN XCC1541
JRNL TITL 2 (NP_636912.1) FROM XANTHOMONAS CAMPESTRIS AT 1.35 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 140130
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7030
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9712
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 534
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5138
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 767
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.26000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.060
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.211
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5564 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3709 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7605 ; 1.767 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9049 ; 1.124 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 748 ; 4.251 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 209 ;26.402 ;22.440
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 859 ;11.019 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;16.900 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 881 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6378 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1116 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1266 ; 0.221 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4240 ; 0.193 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2805 ; 0.175 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 2926 ; 0.092 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 967 ; 0.183 ; 0.500
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): 25 ; 0.115 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 124 ; 0.283 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 78 ; 0.224 ; 0.500
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): 3716 ; 1.906 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1460 ; 0.926 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5817 ; 2.615 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2039 ; 3.989 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1788 ; 5.570 ;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 : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 175 5
REMARK 3 1 B 3 B 175 5
REMARK 3 1 C 3 C 175 5
REMARK 3 1 D 3 D 175 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 908 ; 0.270 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 908 ; 0.290 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 908 ; 0.220 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 908 ; 0.210 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 911 ; 0.460 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 911 ; 0.490 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 911 ; 0.450 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 911 ; 0.370 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 908 ; 1.840 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 908 ; 1.350 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 908 ; 1.650 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 908 ; 1.850 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 911 ; 2.410 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 911 ; 1.920 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 911 ; 2.180 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 911 ; 2.310 ;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 : 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:
REMARK 3 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE
REMARK 3 SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION.
REMARK 3 3. CHLORIDE IONS, TARTRATE ION AND THE FRAGMENTS OF
REMARK 3 POLYETHYLENE GLYCOL 400 MOLECULE WITH DIFFERENT MOLECULAR WEIGHT
REMARK 3 WERE MODELED IN THIS STRUCTURE.
REMARK 3 4. RESIDUES 71 TO 75 IN SUBUNIT D ARE DISORDERED AND NOT MODELED
REMARK 3 IN THE STRUCTURE.
REMARK 3 5. UNEXPLAINED ELECTRON DENSITY NEAR RESIDUES A147 AND D147 ARE
REMARK 3 NOT MODELED. THEY ARE SUGGESTED AS NITROBENZENE (NBZ).
REMARK 4
REMARK 4 2QJW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB043690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837, 0.97920
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140150
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 29.775
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.264M DI-AMMONIUM TARTRATE,
REMARK 280 15.8% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 30.32000
REMARK 290 SMTRY3 2 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 FOUR CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A
REMARK 300 SIGNIFICANT OLIGOMERIZATION 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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 GLY C 0
REMARK 465 MSE C 1
REMARK 465 SER C 2
REMARK 465 GLY D 0
REMARK 465 LYS D 72
REMARK 465 GLY D 73
REMARK 465 PRO D 74
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 LEU A 19 CG CD1 CD2
REMARK 470 GLU A 26 CD OE1 OE2
REMARK 470 ARG A 30 NE CZ NH1 NH2
REMARK 470 ARG A 47 CD NE CZ NH1 NH2
REMARK 470 ARG A 56 CD NE CZ NH1 NH2
REMARK 470 LYS A 72 CE NZ
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 51 CG CD OE1 NE2
REMARK 470 GLU B 64 CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 GLN B 162 CG CD OE1 NE2
REMARK 470 ARG B 166 NE CZ NH1 NH2
REMARK 470 ARG C 3 CD NE CZ NH1 NH2
REMARK 470 GLU C 26 CG CD OE1 OE2
REMARK 470 ARG C 47 CD NE CZ NH1 NH2
REMARK 470 LYS C 72 CE NZ
REMARK 470 LYS C 107 NZ
REMARK 470 GLU C 130 OE1 OE2
REMARK 470 ARG C 156 CD NE CZ NH1 NH2
REMARK 470 GLN C 162 CD OE1 NE2
REMARK 470 ARG C 166 NE CZ NH1 NH2
REMARK 470 GLN C 173 CD OE1 NE2
REMARK 470 ARG D 47 CD NE CZ NH1 NH2
REMARK 470 GLN D 51 CG CD OE1 NE2
REMARK 470 ARG D 56 CZ NH1 NH2
REMARK 470 GLU D 71 CG CD OE1 OE2
REMARK 470 ARG D 97 NE CZ NH1 NH2
REMARK 470 GLU D 130 CD OE1 OE2
REMARK 470 ARG D 166 NE CZ NH1 NH2
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 MSE B 108 CG MSE B 108 SE -0.222
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 ASP A 54 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG C 144 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 144 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 147 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 14 -149.71 -102.96
REMARK 500 SER A 81 -119.39 52.63
REMARK 500 VAL A 103 59.95 37.46
REMARK 500 MSE A 108 56.20 -144.10
REMARK 500 GLU B 13 -7.23 67.08
REMARK 500 SER B 81 -123.85 56.79
REMARK 500 VAL B 103 64.37 33.98
REMARK 500 MSE B 108 48.09 -148.75
REMARK 500 GLU C 13 -8.39 67.85
REMARK 500 SER C 81 -115.75 54.56
REMARK 500 VAL C 103 60.39 34.70
REMARK 500 GLU D 13 -10.78 68.99
REMARK 500 SER D 81 -116.73 54.69
REMARK 500 VAL D 103 63.08 33.03
REMARK 500 MSE D 108 46.50 -146.42
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 CL B 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA B 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G C 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 176
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 372467 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 2QJW A 1 175 UNP Q8PAE4 Q8PAE4_XANCP 1 175
DBREF 2QJW B 1 175 UNP Q8PAE4 Q8PAE4_XANCP 1 175
DBREF 2QJW C 1 175 UNP Q8PAE4 Q8PAE4_XANCP 1 175
DBREF 2QJW D 1 175 UNP Q8PAE4 Q8PAE4_XANCP 1 175
SEQADV 2QJW GLY A 0 UNP Q8PAE4 LEADER SEQUENCE
SEQADV 2QJW MSE A 1 UNP Q8PAE4 MET 1 MODIFIED RESIDUE
SEQADV 2QJW MSE A 102 UNP Q8PAE4 MET 102 MODIFIED RESIDUE
SEQADV 2QJW MSE A 108 UNP Q8PAE4 MET 108 MODIFIED RESIDUE
SEQADV 2QJW GLY B 0 UNP Q8PAE4 LEADER SEQUENCE
SEQADV 2QJW MSE B 1 UNP Q8PAE4 MET 1 MODIFIED RESIDUE
SEQADV 2QJW MSE B 102 UNP Q8PAE4 MET 102 MODIFIED RESIDUE
SEQADV 2QJW MSE B 108 UNP Q8PAE4 MET 108 MODIFIED RESIDUE
SEQADV 2QJW GLY C 0 UNP Q8PAE4 LEADER SEQUENCE
SEQADV 2QJW MSE C 1 UNP Q8PAE4 MET 1 MODIFIED RESIDUE
SEQADV 2QJW MSE C 102 UNP Q8PAE4 MET 102 MODIFIED RESIDUE
SEQADV 2QJW MSE C 108 UNP Q8PAE4 MET 108 MODIFIED RESIDUE
SEQADV 2QJW GLY D 0 UNP Q8PAE4 LEADER SEQUENCE
SEQADV 2QJW MSE D 1 UNP Q8PAE4 MET 1 MODIFIED RESIDUE
SEQADV 2QJW MSE D 102 UNP Q8PAE4 MET 102 MODIFIED RESIDUE
SEQADV 2QJW MSE D 108 UNP Q8PAE4 MET 108 MODIFIED RESIDUE
SEQRES 1 A 176 GLY MSE SER ARG GLY HIS CYS ILE LEU ALA HIS GLY PHE
SEQRES 2 A 176 GLU SER GLY PRO ASP ALA LEU LYS VAL THR ALA LEU ALA
SEQRES 3 A 176 GLU VAL ALA GLU ARG LEU GLY TRP THR HIS GLU ARG PRO
SEQRES 4 A 176 ASP PHE THR ASP LEU ASP ALA ARG ARG ASP LEU GLY GLN
SEQRES 5 A 176 LEU GLY ASP VAL ARG GLY ARG LEU GLN ARG LEU LEU GLU
SEQRES 6 A 176 ILE ALA ARG ALA ALA THR GLU LYS GLY PRO VAL VAL LEU
SEQRES 7 A 176 ALA GLY SER SER LEU GLY SER TYR ILE ALA ALA GLN VAL
SEQRES 8 A 176 SER LEU GLN VAL PRO THR ARG ALA LEU PHE LEU MSE VAL
SEQRES 9 A 176 PRO PRO THR LYS MSE GLY PRO LEU PRO ALA LEU ASP ALA
SEQRES 10 A 176 ALA ALA VAL PRO ILE SER ILE VAL HIS ALA TRP HIS ASP
SEQRES 11 A 176 GLU LEU ILE PRO ALA ALA ASP VAL ILE ALA TRP ALA GLN
SEQRES 12 A 176 ALA ARG SER ALA ARG LEU LEU LEU VAL ASP ASP GLY HIS
SEQRES 13 A 176 ARG LEU GLY ALA HIS VAL GLN ALA ALA SER ARG ALA PHE
SEQRES 14 A 176 ALA GLU LEU LEU GLN SER LEU
SEQRES 1 B 176 GLY MSE SER ARG GLY HIS CYS ILE LEU ALA HIS GLY PHE
SEQRES 2 B 176 GLU SER GLY PRO ASP ALA LEU LYS VAL THR ALA LEU ALA
SEQRES 3 B 176 GLU VAL ALA GLU ARG LEU GLY TRP THR HIS GLU ARG PRO
SEQRES 4 B 176 ASP PHE THR ASP LEU ASP ALA ARG ARG ASP LEU GLY GLN
SEQRES 5 B 176 LEU GLY ASP VAL ARG GLY ARG LEU GLN ARG LEU LEU GLU
SEQRES 6 B 176 ILE ALA ARG ALA ALA THR GLU LYS GLY PRO VAL VAL LEU
SEQRES 7 B 176 ALA GLY SER SER LEU GLY SER TYR ILE ALA ALA GLN VAL
SEQRES 8 B 176 SER LEU GLN VAL PRO THR ARG ALA LEU PHE LEU MSE VAL
SEQRES 9 B 176 PRO PRO THR LYS MSE GLY PRO LEU PRO ALA LEU ASP ALA
SEQRES 10 B 176 ALA ALA VAL PRO ILE SER ILE VAL HIS ALA TRP HIS ASP
SEQRES 11 B 176 GLU LEU ILE PRO ALA ALA ASP VAL ILE ALA TRP ALA GLN
SEQRES 12 B 176 ALA ARG SER ALA ARG LEU LEU LEU VAL ASP ASP GLY HIS
SEQRES 13 B 176 ARG LEU GLY ALA HIS VAL GLN ALA ALA SER ARG ALA PHE
SEQRES 14 B 176 ALA GLU LEU LEU GLN SER LEU
SEQRES 1 C 176 GLY MSE SER ARG GLY HIS CYS ILE LEU ALA HIS GLY PHE
SEQRES 2 C 176 GLU SER GLY PRO ASP ALA LEU LYS VAL THR ALA LEU ALA
SEQRES 3 C 176 GLU VAL ALA GLU ARG LEU GLY TRP THR HIS GLU ARG PRO
SEQRES 4 C 176 ASP PHE THR ASP LEU ASP ALA ARG ARG ASP LEU GLY GLN
SEQRES 5 C 176 LEU GLY ASP VAL ARG GLY ARG LEU GLN ARG LEU LEU GLU
SEQRES 6 C 176 ILE ALA ARG ALA ALA THR GLU LYS GLY PRO VAL VAL LEU
SEQRES 7 C 176 ALA GLY SER SER LEU GLY SER TYR ILE ALA ALA GLN VAL
SEQRES 8 C 176 SER LEU GLN VAL PRO THR ARG ALA LEU PHE LEU MSE VAL
SEQRES 9 C 176 PRO PRO THR LYS MSE GLY PRO LEU PRO ALA LEU ASP ALA
SEQRES 10 C 176 ALA ALA VAL PRO ILE SER ILE VAL HIS ALA TRP HIS ASP
SEQRES 11 C 176 GLU LEU ILE PRO ALA ALA ASP VAL ILE ALA TRP ALA GLN
SEQRES 12 C 176 ALA ARG SER ALA ARG LEU LEU LEU VAL ASP ASP GLY HIS
SEQRES 13 C 176 ARG LEU GLY ALA HIS VAL GLN ALA ALA SER ARG ALA PHE
SEQRES 14 C 176 ALA GLU LEU LEU GLN SER LEU
SEQRES 1 D 176 GLY MSE SER ARG GLY HIS CYS ILE LEU ALA HIS GLY PHE
SEQRES 2 D 176 GLU SER GLY PRO ASP ALA LEU LYS VAL THR ALA LEU ALA
SEQRES 3 D 176 GLU VAL ALA GLU ARG LEU GLY TRP THR HIS GLU ARG PRO
SEQRES 4 D 176 ASP PHE THR ASP LEU ASP ALA ARG ARG ASP LEU GLY GLN
SEQRES 5 D 176 LEU GLY ASP VAL ARG GLY ARG LEU GLN ARG LEU LEU GLU
SEQRES 6 D 176 ILE ALA ARG ALA ALA THR GLU LYS GLY PRO VAL VAL LEU
SEQRES 7 D 176 ALA GLY SER SER LEU GLY SER TYR ILE ALA ALA GLN VAL
SEQRES 8 D 176 SER LEU GLN VAL PRO THR ARG ALA LEU PHE LEU MSE VAL
SEQRES 9 D 176 PRO PRO THR LYS MSE GLY PRO LEU PRO ALA LEU ASP ALA
SEQRES 10 D 176 ALA ALA VAL PRO ILE SER ILE VAL HIS ALA TRP HIS ASP
SEQRES 11 D 176 GLU LEU ILE PRO ALA ALA ASP VAL ILE ALA TRP ALA GLN
SEQRES 12 D 176 ALA ARG SER ALA ARG LEU LEU LEU VAL ASP ASP GLY HIS
SEQRES 13 D 176 ARG LEU GLY ALA HIS VAL GLN ALA ALA SER ARG ALA PHE
SEQRES 14 D 176 ALA GLU LEU LEU GLN SER LEU
MODRES 2QJW MSE A 1 MET SELENOMETHIONINE
MODRES 2QJW MSE A 102 MET SELENOMETHIONINE
MODRES 2QJW MSE A 108 MET SELENOMETHIONINE
MODRES 2QJW MSE B 1 MET SELENOMETHIONINE
MODRES 2QJW MSE B 102 MET SELENOMETHIONINE
MODRES 2QJW MSE B 108 MET SELENOMETHIONINE
MODRES 2QJW MSE C 102 MET SELENOMETHIONINE
MODRES 2QJW MSE C 108 MET SELENOMETHIONINE
MODRES 2QJW MSE D 1 MET SELENOMETHIONINE
MODRES 2QJW MSE D 102 MET SELENOMETHIONINE
MODRES 2QJW MSE D 108 MET SELENOMETHIONINE
HET MSE A 1 16
HET MSE A 102 8
HET MSE A 108 16
HET MSE B 1 16
HET MSE B 102 8
HET MSE B 108 16
HET MSE C 102 8
HET MSE C 108 16
HET MSE D 1 8
HET MSE D 102 8
HET MSE D 108 16
HET CL B 176 1
HET CL B 177 1
HET CL A 176 1
HET CL B 178 1
HET CL A 177 1
HET CL C 176 1
HET CL A 178 1
HET CL C 177 1
HET TLA B 179 10
HET P6G C 178 19
HET PEG C 179 7
HET PEG B 180 7
HET PEG C 180 7
HET PEG D 176 7
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM TLA L(+)-TARTARIC ACID
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 5 CL 8(CL 1-)
FORMUL 13 TLA C4 H6 O6
FORMUL 14 P6G C12 H26 O7
FORMUL 15 PEG 4(C4 H10 O3)
FORMUL 19 HOH *767(H2 O)
HELIX 1 1 ALA A 18 LEU A 31 1 14
HELIX 2 2 PHE A 40 ALA A 45 1 6
HELIX 3 3 ARG A 46 GLY A 50 5 5
HELIX 4 4 ASP A 54 GLU A 71 1 18
HELIX 5 5 SER A 81 LEU A 92 1 12
HELIX 6 6 PRO A 133 SER A 145 1 13
HELIX 7 7 HIS A 160 SER A 174 1 15
HELIX 8 8 ALA B 18 GLY B 32 1 15
HELIX 9 9 PHE B 40 ALA B 45 1 6
HELIX 10 10 ARG B 46 GLY B 50 5 5
HELIX 11 11 ASP B 54 THR B 70 1 17
HELIX 12 12 GLU B 71 GLY B 73 5 3
HELIX 13 13 SER B 81 LEU B 92 1 12
HELIX 14 14 PRO B 133 ARG B 144 1 12
HELIX 15 15 HIS B 160 SER B 174 1 15
HELIX 16 16 ALA C 18 LEU C 31 1 14
HELIX 17 17 PHE C 40 ALA C 45 1 6
HELIX 18 18 ARG C 46 GLY C 50 5 5
HELIX 19 19 ASP C 54 GLU C 71 1 18
HELIX 20 20 SER C 81 SER C 91 1 11
HELIX 21 21 PRO C 133 ARG C 144 1 12
HELIX 22 22 HIS C 160 SER C 174 1 15
HELIX 23 23 ALA D 18 GLY D 32 1 15
HELIX 24 24 PHE D 40 ALA D 45 1 6
HELIX 25 25 ARG D 46 GLY D 50 5 5
HELIX 26 26 ASP D 54 THR D 70 1 17
HELIX 27 27 SER D 81 LEU D 92 1 12
HELIX 28 28 PRO D 133 ARG D 144 1 12
HELIX 29 29 HIS D 160 LEU D 175 1 16
SHEET 1 A12 THR A 34 GLU A 36 0
SHEET 2 A12 HIS A 5 ALA A 9 1 N CYS A 6 O THR A 34
SHEET 3 A12 VAL A 75 SER A 80 1 O ALA A 78 N ALA A 9
SHEET 4 A12 ALA A 98 MSE A 102 1 O PHE A 100 N LEU A 77
SHEET 5 A12 ILE A 121 ALA A 126 1 O SER A 122 N LEU A 101
SHEET 6 A12 ARG A 147 VAL A 151 1 O LEU A 149 N HIS A 125
SHEET 7 A12 ARG B 147 VAL B 151 -1 O LEU B 148 N LEU A 150
SHEET 8 A12 ILE B 121 ALA B 126 1 N HIS B 125 O LEU B 149
SHEET 9 A12 THR B 96 MSE B 102 1 N LEU B 101 O SER B 122
SHEET 10 A12 VAL B 75 SER B 80 1 N VAL B 75 O ARG B 97
SHEET 11 A12 HIS B 5 ALA B 9 1 N ALA B 9 O ALA B 78
SHEET 12 A12 THR B 34 GLU B 36 1 O GLU B 36 N LEU B 8
SHEET 1 B12 THR C 34 GLU C 36 0
SHEET 2 B12 HIS C 5 ALA C 9 1 N LEU C 8 O GLU C 36
SHEET 3 B12 VAL C 75 SER C 80 1 O ALA C 78 N ALA C 9
SHEET 4 B12 ALA C 98 MSE C 102 1 O MSE C 102 N GLY C 79
SHEET 5 B12 ILE C 121 ALA C 126 1 O SER C 122 N LEU C 101
SHEET 6 B12 ARG C 147 VAL C 151 1 O LEU C 149 N HIS C 125
SHEET 7 B12 ARG D 147 VAL D 151 -1 O LEU D 148 N LEU C 150
SHEET 8 B12 ILE D 121 ALA D 126 1 N HIS D 125 O LEU D 149
SHEET 9 B12 ALA D 98 MSE D 102 1 N LEU D 101 O SER D 122
SHEET 10 B12 VAL D 76 SER D 80 1 N GLY D 79 O MSE D 102
SHEET 11 B12 HIS D 5 ALA D 9 1 N ALA D 9 O ALA D 78
SHEET 12 B12 THR D 34 GLU D 36 1 O GLU D 36 N LEU D 8
LINK C GLY A 0 N AMSE A 1 1555 1555 1.33
LINK C GLY A 0 N BMSE A 1 1555 1555 1.34
LINK C AMSE A 1 N SER A 2 1555 1555 1.34
LINK C BMSE A 1 N SER A 2 1555 1555 1.34
LINK C LEU A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N VAL A 103 1555 1555 1.33
LINK C LYS A 107 N AMSE A 108 1555 1555 1.33
LINK C LYS A 107 N BMSE A 108 1555 1555 1.33
LINK C AMSE A 108 N GLY A 109 1555 1555 1.34
LINK C BMSE A 108 N GLY A 109 1555 1555 1.32
LINK C GLY B 0 N AMSE B 1 1555 1555 1.33
LINK C GLY B 0 N BMSE B 1 1555 1555 1.31
LINK C AMSE B 1 N SER B 2 1555 1555 1.32
LINK C BMSE B 1 N SER B 2 1555 1555 1.33
LINK C LEU B 101 N MSE B 102 1555 1555 1.32
LINK C MSE B 102 N VAL B 103 1555 1555 1.35
LINK C LYS B 107 N AMSE B 108 1555 1555 1.33
LINK C LYS B 107 N BMSE B 108 1555 1555 1.34
LINK C BMSE B 108 N GLY B 109 1555 1555 1.33
LINK C AMSE B 108 N GLY B 109 1555 1555 1.34
LINK C LEU C 101 N MSE C 102 1555 1555 1.32
LINK C MSE C 102 N VAL C 103 1555 1555 1.32
LINK C LYS C 107 N BMSE C 108 1555 1555 1.34
LINK C LYS C 107 N AMSE C 108 1555 1555 1.34
LINK C BMSE C 108 N GLY C 109 1555 1555 1.32
LINK C AMSE C 108 N GLY C 109 1555 1555 1.32
LINK C MSE D 1 N BSER D 2 1555 1555 1.32
LINK C MSE D 1 N ASER D 2 1555 1555 1.33
LINK C LEU D 101 N MSE D 102 1555 1555 1.32
LINK C MSE D 102 N VAL D 103 1555 1555 1.30
LINK C LYS D 107 N BMSE D 108 1555 1555 1.33
LINK C LYS D 107 N AMSE D 108 1555 1555 1.34
LINK C BMSE D 108 N GLY D 109 1555 1555 1.32
LINK C AMSE D 108 N GLY D 109 1555 1555 1.33
SITE 1 AC1 3 GLY B 11 SER B 14 ALA B 18
SITE 1 AC2 3 ARG B 3 TRP B 33 GLN B 173
SITE 1 AC3 4 HIS A 35 GLU A 36 ARG A 37 HOH A 367
SITE 1 AC4 2 ARG B 47 GLY B 50
SITE 1 AC5 5 ARG A 147 HOH A 184 VAL B 151 ASP B 152
SITE 2 AC5 5 HIS B 160
SITE 1 AC6 5 ARG C 147 HOH C 185 VAL D 151 ASP D 152
SITE 2 AC6 5 HIS D 160
SITE 1 AC7 6 VAL A 151 ASP A 152 HIS A 160 HOH A 352
SITE 2 AC7 6 ARG B 147 HOH B 192
SITE 1 AC8 4 VAL C 151 ASP C 152 ARG D 147 HOH D 189
SITE 1 AC9 14 GLY B 11 PHE B 12 SER B 14 LYS B 20
SITE 2 AC9 14 SER B 81 HIS B 155 ARG B 156 PEG B 180
SITE 3 AC9 14 HOH B 197 HOH B 207 HOH B 222 ARG C 67
SITE 4 AC9 14 GLN C 93 PRO C 95
SITE 1 BC1 5 ASP C 152 ASP C 153 GLY C 154 HOH C 267
SITE 2 BC1 5 HOH C 318
SITE 1 BC2 7 PRO C 120 ILE C 121 ARG C 147 HOH C 186
SITE 2 BC2 7 HOH C 262 HOH C 287 HOH D 249
SITE 1 BC3 3 SER B 81 TLA B 179 HOH B 268
SITE 1 BC4 5 ARG B 3 HOH B 309 LYS C 107 GLY C 109
SITE 2 BC4 5 HOH C 205
SITE 1 BC5 2 ASP D 39 ASP D 42
CRYST1 71.800 60.640 74.720 90.00 94.57 90.00 P 1 21 1 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 0.013928 0.000000 0.001112 0.00000
SCALE2 0.000000 0.016491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013426 0.00000
TER 1381 LEU A 175
TER 2744 LEU B 175
TER 4061 LEU C 175
TER 5383 LEU D 175
MASTER 466 0 25 29 24 0 23 6 5970 4 215 56
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