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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 17-AUG-06 2I3D
TITLE CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN ATU1826, A
TITLE 2 PUTATIVE ALPHA/BETA HYDROLASE FROM AGROBACTERIUM
TITLE 3 TUMEFACIENS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN ATU1826;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AGR_C_3351P;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: C58;
SOURCE 5 ATCC: 33970;
SOURCE 6 GENE: ATU1826;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS STRUCTURAL GENOMICS, APC5865, HYDROLASE, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,X.XU,H.ZHENG,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 19-SEP-06 2I3D 0
JRNL AUTH J.OSIPIUK,X.XU,H.ZHENG,A.SAVCHENKO,A.EDWARDS,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN ATU1826,
JRNL TITL 2 A PUTATIVE ALPHA/BETA HYDROLASE FROM AGROBACTERIUM
JRNL TITL 3 TUMEFACIENS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.6
REMARK 3 NUMBER OF REFLECTIONS : 53497
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2684
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 15.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : 0.29000
REMARK 3 B12 (A**2) : -0.07000
REMARK 3 B13 (A**2) : 0.07000
REMARK 3 B23 (A**2) : 0.20000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.551
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3730 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5090 ; 1.560 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 494 ; 5.910 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;34.168 ;24.180
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 637 ;13.201 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.646 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2966 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1925 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2546 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 397 ; 0.210 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.091 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 65 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 51 ; 0.253 ; 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): 2328 ; 1.536 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3674 ; 2.145 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 4.064 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1386 ; 4.615 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3910 ; 3.729 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 522 ; 6.210 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3605 ; 3.719 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2I3D COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-2006.
REMARK 100 THE RCSB ID CODE IS RCSB039085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 35.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 15.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE/RESOLVE, HKL2000_PH
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES BUFFER, 0.4 M MAGNESIUM
REMARK 280 CHLORIDE, 30% PEG 2000 MME, PH 6.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.
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 MSE A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 220
REMARK 465 ALA A 221
REMARK 465 LYS A 222
REMARK 465 ARG A 223
REMARK 465 ILE A 224
REMARK 465 ARG A 225
REMARK 465 GLY A 226
REMARK 465 SER A 227
REMARK 465 MSE B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 ARG B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 ALA B 221
REMARK 465 LYS B 222
REMARK 465 ARG B 223
REMARK 465 ILE B 224
REMARK 465 ARG B 225
REMARK 465 GLY B 226
REMARK 465 SER B 227
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
REMARK 500 O HOH 7 O HOH 449 1.81
REMARK 500 OE1 GLU A 162 O HOH 481 2.16
REMARK 500 O HOH 60 O HOH 65 2.16
REMARK 500 O HOH 174 O HOH 215 2.17
REMARK 500 O ALA B 220 O HOH 391 2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 93 O HOH 382 1454 1.98
REMARK 500 O HOH 178 O HOH 382 1454 2.17
REMARK 500 O HOH 123 O HOH 206 1556 2.18
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 505 DISTANCE = 5.72 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC5865 RELATED DB: TARGETDB
DBREF 2I3D A 1 225 UNP Q8UED4 Q8UED4_AGRT5 1 225
DBREF 2I3D B 1 225 UNP Q8UED4 Q8UED4_AGRT5 1 225
SEQADV 2I3D MSE A -21 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY A -20 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER A -19 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER A -18 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -17 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -16 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -15 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -14 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -13 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A -12 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER A -11 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER A -10 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY A -9 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D ARG A -8 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLU A -7 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D ASN A -6 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D LEU A -5 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D TYR A -4 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D PHE A -3 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLN A -2 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY A -1 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS A 0 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D MSE A 1 UNP Q8UED4 MET 1 MODIFIED RESIDUE
SEQADV 2I3D MSE A 41 UNP Q8UED4 MET 41 MODIFIED RESIDUE
SEQADV 2I3D MSE A 115 UNP Q8UED4 MET 115 MODIFIED RESIDUE
SEQADV 2I3D MSE A 119 UNP Q8UED4 MET 119 MODIFIED RESIDUE
SEQADV 2I3D MSE A 128 UNP Q8UED4 MET 128 MODIFIED RESIDUE
SEQADV 2I3D MSE A 200 UNP Q8UED4 MET 200 MODIFIED RESIDUE
SEQADV 2I3D GLY A 226 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER A 227 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D MSE B -21 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY B -20 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER B -19 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER B -18 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -17 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -16 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -15 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -14 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -13 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B -12 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER B -11 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER B -10 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY B -9 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D ARG B -8 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLU B -7 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D ASN B -6 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D LEU B -5 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D TYR B -4 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D PHE B -3 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLN B -2 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D GLY B -1 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D HIS B 0 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D MSE B 1 UNP Q8UED4 MET 1 MODIFIED RESIDUE
SEQADV 2I3D MSE B 41 UNP Q8UED4 MET 41 MODIFIED RESIDUE
SEQADV 2I3D MSE B 115 UNP Q8UED4 MET 115 MODIFIED RESIDUE
SEQADV 2I3D MSE B 119 UNP Q8UED4 MET 119 MODIFIED RESIDUE
SEQADV 2I3D MSE B 128 UNP Q8UED4 MET 128 MODIFIED RESIDUE
SEQADV 2I3D MSE B 200 UNP Q8UED4 MET 200 MODIFIED RESIDUE
SEQADV 2I3D GLY B 226 UNP Q8UED4 CLONING ARTIFACT
SEQADV 2I3D SER B 227 UNP Q8UED4 CLONING ARTIFACT
SEQRES 1 A 249 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 249 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE PRO GLU VAL
SEQRES 3 A 249 ILE PHE ASN GLY PRO ALA GLY ARG LEU GLU GLY ARG TYR
SEQRES 4 A 249 GLN PRO SER LYS GLU LYS SER ALA PRO ILE ALA ILE ILE
SEQRES 5 A 249 LEU HIS PRO HIS PRO GLN PHE GLY GLY THR MSE ASN ASN
SEQRES 6 A 249 GLN ILE VAL TYR GLN LEU PHE TYR LEU PHE GLN LYS ARG
SEQRES 7 A 249 GLY PHE THR THR LEU ARG PHE ASN PHE ARG SER ILE GLY
SEQRES 8 A 249 ARG SER GLN GLY GLU PHE ASP HIS GLY ALA GLY GLU LEU
SEQRES 9 A 249 SER ASP ALA ALA SER ALA LEU ASP TRP VAL GLN SER LEU
SEQRES 10 A 249 HIS PRO ASP SER LYS SER CYS TRP VAL ALA GLY TYR SER
SEQRES 11 A 249 PHE GLY ALA TRP ILE GLY MSE GLN LEU LEU MSE ARG ARG
SEQRES 12 A 249 PRO GLU ILE GLU GLY PHE MSE SER ILE ALA PRO GLN PRO
SEQRES 13 A 249 ASN THR TYR ASP PHE SER PHE LEU ALA PRO CYS PRO SER
SEQRES 14 A 249 SER GLY LEU ILE ILE ASN GLY ASP ALA ASP LYS VAL ALA
SEQRES 15 A 249 PRO GLU LYS ASP VAL ASN GLY LEU VAL GLU LYS LEU LYS
SEQRES 16 A 249 THR GLN LYS GLY ILE LEU ILE THR HIS ARG THR LEU PRO
SEQRES 17 A 249 GLY ALA ASN HIS PHE PHE ASN GLY LYS VAL ASP GLU LEU
SEQRES 18 A 249 MSE GLY GLU CYS GLU ASP TYR LEU ASP ARG ARG LEU ASN
SEQRES 19 A 249 GLY GLU LEU VAL PRO GLU PRO ALA ALA LYS ARG ILE ARG
SEQRES 20 A 249 GLY SER
SEQRES 1 B 249 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 249 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE PRO GLU VAL
SEQRES 3 B 249 ILE PHE ASN GLY PRO ALA GLY ARG LEU GLU GLY ARG TYR
SEQRES 4 B 249 GLN PRO SER LYS GLU LYS SER ALA PRO ILE ALA ILE ILE
SEQRES 5 B 249 LEU HIS PRO HIS PRO GLN PHE GLY GLY THR MSE ASN ASN
SEQRES 6 B 249 GLN ILE VAL TYR GLN LEU PHE TYR LEU PHE GLN LYS ARG
SEQRES 7 B 249 GLY PHE THR THR LEU ARG PHE ASN PHE ARG SER ILE GLY
SEQRES 8 B 249 ARG SER GLN GLY GLU PHE ASP HIS GLY ALA GLY GLU LEU
SEQRES 9 B 249 SER ASP ALA ALA SER ALA LEU ASP TRP VAL GLN SER LEU
SEQRES 10 B 249 HIS PRO ASP SER LYS SER CYS TRP VAL ALA GLY TYR SER
SEQRES 11 B 249 PHE GLY ALA TRP ILE GLY MSE GLN LEU LEU MSE ARG ARG
SEQRES 12 B 249 PRO GLU ILE GLU GLY PHE MSE SER ILE ALA PRO GLN PRO
SEQRES 13 B 249 ASN THR TYR ASP PHE SER PHE LEU ALA PRO CYS PRO SER
SEQRES 14 B 249 SER GLY LEU ILE ILE ASN GLY ASP ALA ASP LYS VAL ALA
SEQRES 15 B 249 PRO GLU LYS ASP VAL ASN GLY LEU VAL GLU LYS LEU LYS
SEQRES 16 B 249 THR GLN LYS GLY ILE LEU ILE THR HIS ARG THR LEU PRO
SEQRES 17 B 249 GLY ALA ASN HIS PHE PHE ASN GLY LYS VAL ASP GLU LEU
SEQRES 18 B 249 MSE GLY GLU CYS GLU ASP TYR LEU ASP ARG ARG LEU ASN
SEQRES 19 B 249 GLY GLU LEU VAL PRO GLU PRO ALA ALA LYS ARG ILE ARG
SEQRES 20 B 249 GLY SER
MODRES 2I3D MSE A 41 MET SELENOMETHIONINE
MODRES 2I3D MSE A 115 MET SELENOMETHIONINE
MODRES 2I3D MSE A 119 MET SELENOMETHIONINE
MODRES 2I3D MSE A 128 MET SELENOMETHIONINE
MODRES 2I3D MSE A 200 MET SELENOMETHIONINE
MODRES 2I3D MSE B 1 MET SELENOMETHIONINE
MODRES 2I3D MSE B 41 MET SELENOMETHIONINE
MODRES 2I3D MSE B 115 MET SELENOMETHIONINE
MODRES 2I3D MSE B 119 MET SELENOMETHIONINE
MODRES 2I3D MSE B 128 MET SELENOMETHIONINE
MODRES 2I3D MSE B 200 MET SELENOMETHIONINE
HET MSE A 41 8
HET MSE A 115 13
HET MSE A 119 8
HET MSE A 128 8
HET MSE A 200 8
HET MSE B 1 8
HET MSE B 41 8
HET MSE B 115 13
HET MSE B 119 8
HET MSE B 128 8
HET MSE B 200 8
HET MG 601 1
HET MG 602 1
HET CL 603 1
HET CL 604 1
HET CL 605 1
HET CL 606 1
HET CL 607 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 11(C5 H11 N1 O2 SE1)
FORMUL 3 MG 2(MG1 2+)
FORMUL 5 CL 5(CL1 1-)
FORMUL 10 HOH *513(H2 O1)
HELIX 1 1 HIS A 34 GLY A 38 5 5
HELIX 2 2 ASN A 43 ARG A 56 1 14
HELIX 3 3 GLY A 78 HIS A 96 1 19
HELIX 4 4 SER A 108 ARG A 121 1 14
HELIX 5 5 PRO A 161 LYS A 173 1 13
HELIX 6 6 LYS A 195 ASN A 212 1 18
HELIX 7 7 HIS B 34 GLY B 38 5 5
HELIX 8 8 ASN B 43 ARG B 56 1 14
HELIX 9 9 GLY B 78 HIS B 96 1 19
HELIX 10 10 SER B 108 ARG B 121 1 14
HELIX 11 11 PRO B 161 THR B 174 1 14
HELIX 12 12 LYS B 195 ASN B 212 1 18
SHEET 1 A 8 GLU A 3 GLY A 8 0
SHEET 2 A 8 GLY A 11 GLN A 18 -1 O GLY A 11 N GLY A 8
SHEET 3 A 8 THR A 59 PHE A 63 -1 O ARG A 62 N ARG A 16
SHEET 4 A 8 ILE A 27 LEU A 31 1 N ALA A 28 O THR A 59
SHEET 5 A 8 CYS A 102 TYR A 107 1 O ALA A 105 N LEU A 31
SHEET 6 A 8 ILE A 124 ILE A 130 1 O ILE A 130 N GLY A 106
SHEET 7 A 8 GLY A 149 GLY A 154 1 O LEU A 150 N SER A 129
SHEET 8 A 8 ILE A 180 LEU A 185 1 O THR A 181 N GLY A 149
SHEET 1 B 8 GLU B 3 GLY B 8 0
SHEET 2 B 8 GLY B 11 GLN B 18 -1 O GLY B 11 N GLY B 8
SHEET 3 B 8 THR B 59 PHE B 63 -1 O ARG B 62 N ARG B 16
SHEET 4 B 8 ILE B 27 LEU B 31 1 N ALA B 28 O THR B 59
SHEET 5 B 8 CYS B 102 TYR B 107 1 O TRP B 103 N ILE B 27
SHEET 6 B 8 ILE B 124 ILE B 130 1 O ILE B 130 N GLY B 106
SHEET 7 B 8 GLY B 149 GLY B 154 1 O LEU B 150 N SER B 129
SHEET 8 B 8 ILE B 180 LEU B 185 1 O LEU B 185 N ASN B 153
CISPEP 1 ALA A 143 PRO A 144 0 -12.30
CISPEP 2 MSE B 1 PRO B 2 0 10.28
CISPEP 3 ALA B 143 PRO B 144 0 2.60
CRYST1 46.549 50.579 54.844 92.25 115.17 99.82 P 1 2
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 0.021483 0.003720 0.010643 0.00000
SCALE2 0.000000 0.020065 0.002534 0.00000
SCALE3 0.000000 0.000000 0.020306 0.00000
END |