HEADER HYDROLASE 18-JAN-05 2BHU
TITLE CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS
TITLE 2 MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS TREHALOSE, ALPHA-AMYLASE, HYDROLASE, PROTEIN-CARBOHYDRATE
KEYWDS 2 COMPLEX, DESICCATION RESISTANCE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.TIMMINS,H.-K.S.LEIROS,G.LEONARD,I.LEIROS,S.MCSWEENEY
REVDAT 2 24-FEB-09 2BHU 1 VERSN
REVDAT 1 31-MAR-05 2BHU 0
JRNL AUTH J.TIMMINS,H.-K.S.LEIROS,G.LEONARD,I.LEIROS,
JRNL AUTH 2 S.MCSWEENEY
JRNL TITL CRYSTAL STRUCTURE OF MALTOOLIGOSYLTREHALOSE
JRNL TITL 2 TREHALOHYDROLASE FROM DEINOCOCCUS RADIODURANS IN
JRNL TITL 3 COMPLEX WITH DISACCHARIDES
JRNL REF J.MOL.BIOL. V. 347 949 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15784255
JRNL DOI 10.1016/J.JMB.2005.02.011
REMARK 2
REMARK 2 RESOLUTION. 1.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 205610
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) : 0.129
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10891
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) : 1.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13628
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 707
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 1130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.00000
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): 0.030
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.032
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.990
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5187 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4551 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7122 ; 1.797 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10547 ; 0.951 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 672 ; 5.974 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 258 ;35.790 ;22.984
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 770 ;11.588 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;17.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 735 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6135 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1171 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1126 ; 0.265 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5146 ; 0.206 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2582 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3006 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 842 ; 0.196 ; 0.200
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): 41 ; 1.075 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 175 ; 0.567 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 104 ; 0.212 ; 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): 4039 ; 1.941 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5127 ; 2.353 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2357 ; 3.116 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1995 ; 3.933 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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. WARNING: THIS ENTRY CONTAINS ATOMS THAT HAVE
REMARK 3 BEEN REFINED WITH AN OCCUPANCY OF 0.00.
REMARK 4
REMARK 4 2BHU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-05.
REMARK 100 THE PDBE ID CODE IS EBI-22406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.005
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 216600
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 2000 MME, 0.1 M
REMARK 280 TRIS-HCL PH8.5, 0.1 M MGCL2
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 29.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.25500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.25500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A INSERTION MUTATION BETWEEN RESIDUES 430 AND 431 IN
REMARK 400 THE UNIPROT ENTRY. RESIDUES THR431 AND LEU432 INSERTED AT
REMARK 400 THIS 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 MET A 1
REMARK 465 THR A 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 THR A 8
REMARK 465 PRO A 9
REMARK 465 THR A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 ALA A 13
REMARK 465 GLY A 473
REMARK 465 GLY A 474
REMARK 465 PHE A 475
REMARK 465 SER A 476
REMARK 465 GLY A 477
REMARK 465 PHE A 478
REMARK 465 SER A 479
REMARK 465 GLY A 480
REMARK 465 GLU A 481
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480 M RES CSSEQI ATOMS
REMARK 480 ARG A 22 NH1 NH2
REMARK 480 ARG A 46 CD NE CZ NH1 NH2
REMARK 480 ASP A 113 OD1 OD2
REMARK 480 ARG A 204 CD NE CZ NH1 NH2
REMARK 480 MET A 243 CE CE
REMARK 480 ILE A 296 CD1
REMARK 480 LEU A 305 CD2
REMARK 480 GLU A 459 CD OE1 OE2
REMARK 480 GLN A 462 NE2
REMARK 480 GLU A 466 CD OE1
REMARK 480 LYS A 469 CD
REMARK 480 LYS A 470 CD CE NZ
REMARK 480 ASP A 482 CG OD1 OD2
REMARK 480 ARG A 509 NH1 NH2
REMARK 480 ARG A 512 CD NE CZ NH1 NH2
REMARK 480 ARG A 519 CZ NH1 NH2 CZ NH1 NH2
REMARK 480 LEU A 520 CD2
REMARK 480 GLU A 570 OE2
REMARK 480 ARG A 579 NE CZ NH1 NH2
REMARK 480 ARG A 580 NH1 NH2
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 CD ARG A 423 - O HOH A 2863 2.16
REMARK 500 O HOH A 2136 - O HOH A 2171 2.00
REMARK 500 O HOH A 2202 - O HOH A 2204 2.14
REMARK 500 O HOH A 2356 - O HOH A 2361 2.04
REMARK 500 O HOH A 2576 - O HOH A 2582 2.00
REMARK 500 O HOH A 2706 - O HOH A 2708 2.04
REMARK 500 O HOH A 2765 - O HOH A 2768 2.17
REMARK 500 O HOH A 2928 - O HOH A 2937 2.14
REMARK 500 O HOH A 3016 - O HOH A 3020 2.10
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 O HOH A 2202 O HOH A 2818 4455 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 22 CA A ARG A 22 CB A -0.153
REMARK 500 ARG A 22 CB A ARG A 22 CG A 0.263
REMARK 500 ARG A 22 CZ A ARG A 22 NH1A 7.481
REMARK 500 ARG A 22 CZ A ARG A 22 NH2A 8.353
REMARK 500 GLU A 193 CD A GLU A 193 OE1A 0.076
REMARK 500 GLU A 193 CD A GLU A 193 OE2A 0.155
REMARK 500 MET A 243 CG A MET A 243 SD A 0.709
REMARK 500 MET A 243 SD A MET A 243 CE A 1.127
REMARK 500 GLN A 462 CD GLN A 462 NE2 0.188
REMARK 500 GLU A 466 CD GLU A 466 OE2 1.201
REMARK 500 GLU A 466 CG GLU A 466 CD -0.095
REMARK 500 LYS A 469 CD LYS A 469 CE 0.242
REMARK 500 LYS A 470 CG LYS A 470 CD -0.214
REMARK 500 ASP A 482 CB ASP A 482 CG 0.606
REMARK 500 GLU A 503 CD A GLU A 503 OE1A 1.524
REMARK 500 GLU A 503 CD A GLU A 503 OE2A 2.554
REMARK 500 GLU A 503 CG A GLU A 503 CD A 0.609
REMARK 500 ARG A 519 NE A ARG A 519 CZ A 0.235
REMARK 500 ARG A 579 CD ARG A 579 NE -0.135
REMARK 500 ARG A 580 CZ ARG A 580 NH1 -0.080
REMARK 500 ARG A 580 CZ ARG A 580 NH2 0.595
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 22 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 22 CB - CG - CD ANGL. DEV. = -24.7 DEGREES
REMARK 500 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -93.8 DEGREES
REMARK 500 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -89.1 DEGREES
REMARK 500 ARG A 22 NH1 - CZ - NH2 ANGL. DEV. = ***** DEGREES
REMARK 500 ARG A 94 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PHE A 182 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 GLU A 193 CG - CD - OE1 ANGL. DEV. = -13.3 DEGREES
REMARK 500 MET A 243 CB - CG - SD ANGL. DEV. = -31.8 DEGREES
REMARK 500 MET A 243 CG - SD - CE ANGL. DEV. = -30.7 DEGREES
REMARK 500 LYS A 469 CD - CE - NZ ANGL. DEV. = -45.1 DEGREES
REMARK 500 ASP A 482 CA - CB - CG ANGL. DEV. = -28.2 DEGREES
REMARK 500 GLU A 503 CG - CD - OE1 ANGL. DEV. = -62.4 DEGREES
REMARK 500 GLU A 503 CG - CD - OE2 ANGL. DEV. = -84.7 DEGREES
REMARK 500 GLU A 503 OE1 - CD - OE2 ANGL. DEV. = -88.7 DEGREES
REMARK 500 ARG A 519 CD - NE - CZ ANGL. DEV. = 22.0 DEGREES
REMARK 500 ARG A 519 NE - CZ - NH1 ANGL. DEV. = -16.0 DEGREES
REMARK 500 ARG A 519 NE - CZ - NH2 ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG A 530 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLU A 570 OE1 - CD - OE2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG A 579 CG - CD - NE ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 580 NE - CZ - NH1 ANGL. DEV. = 28.2 DEGREES
REMARK 500 ARG A 580 NE - CZ - NH2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG A 580 NH1 - CZ - NH2 ANGL. DEV. = -29.0 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 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 GLN A 342 14.43 -144.08
REMARK 500 ASP A 455 50.81 -149.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU A 466 0.09 SIDE CHAIN
REMARK 500 GLU A 570 0.12 SIDE CHAIN
REMARK 500 ARG A 580 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 22 18.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A3064 O
REMARK 620 2 ASP A 540 OD1 93.4
REMARK 620 3 HOH A2300 O 85.3 96.5
REMARK 620 4 HOH A2316 O 171.2 93.2 88.2
REMARK 620 5 HOH A3009 O 93.8 84.6 178.7 92.6
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BHY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS
REMARK 900 MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX
REMARK 900 WITH TREHALOSE
REMARK 900 RELATED ID: 2BHZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEINOCOCCUS RADIODURANS
REMARK 900 MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE IN COMPLEX
REMARK 900 WITH MALTOSE
DBREF 2BHU A 1 430 UNP Q9RX51 Q9RX51 1 430
DBREF 2BHU A 431 432 PDB 2BHU 2BHU 431 432
DBREF 2BHU A 433 602 UNP Q9RX51 Q9RX51 431 600
SEQRES 1 A 602 MET THR GLN THR GLN PRO VAL THR PRO THR PRO PRO ALA
SEQRES 2 A 602 SER PHE GLN THR GLN HIS ASP PRO ARG THR ARG LEU GLY
SEQRES 3 A 602 ALA THR PRO LEU PRO GLY GLY ALA GLY THR ARG PHE ARG
SEQRES 4 A 602 LEU TRP THR SER THR ALA ARG THR VAL ALA VAL ARG VAL
SEQRES 5 A 602 ASN GLY THR GLU HIS VAL MET THR SER LEU GLY GLY GLY
SEQRES 6 A 602 ILE TYR GLU LEU GLU LEU PRO VAL GLY PRO GLY ALA ARG
SEQRES 7 A 602 TYR LEU PHE VAL LEU ASP GLY VAL PRO THR PRO ASP PRO
SEQRES 8 A 602 TYR ALA ARG PHE LEU PRO ASP GLY VAL HIS GLY GLU ALA
SEQRES 9 A 602 GLU VAL VAL ASP PHE GLY THR PHE ASP TRP THR ASP ALA
SEQRES 10 A 602 ASP TRP HIS GLY ILE LYS LEU ALA ASP CYS VAL PHE TYR
SEQRES 11 A 602 GLU VAL HIS VAL GLY THR PHE THR PRO GLU GLY THR TYR
SEQRES 12 A 602 ARG ALA ALA ALA GLU LYS LEU PRO TYR LEU LYS GLU LEU
SEQRES 13 A 602 GLY VAL THR ALA ILE GLN VAL MET PRO LEU ALA ALA PHE
SEQRES 14 A 602 ASP GLY GLN ARG GLY TRP GLY TYR ASP GLY ALA ALA PHE
SEQRES 15 A 602 TYR ALA PRO TYR ALA PRO TYR GLY ARG PRO GLU ASP LEU
SEQRES 16 A 602 MET ALA LEU VAL ASP ALA ALA HIS ARG LEU GLY LEU GLY
SEQRES 17 A 602 VAL PHE LEU ASP VAL VAL TYR ASN HIS PHE GLY PRO SER
SEQRES 18 A 602 GLY ASN TYR LEU SER SER TYR ALA PRO SER TYR PHE THR
SEQRES 19 A 602 ASP ARG PHE SER SER ALA TRP GLY MET GLY LEU ASP TYR
SEQRES 20 A 602 ALA GLU PRO HIS MET ARG ARG TYR VAL THR GLY ASN ALA
SEQRES 21 A 602 ARG MET TRP LEU ARG ASP TYR HIS PHE ASP GLY LEU ARG
SEQRES 22 A 602 LEU ASP ALA THR PRO TYR MET THR ASP ASP SER GLU THR
SEQRES 23 A 602 HIS ILE LEU THR GLU LEU ALA GLN GLU ILE HIS GLU LEU
SEQRES 24 A 602 GLY GLY THR HIS LEU LEU LEU ALA GLU ASP HIS ARG ASN
SEQRES 25 A 602 LEU PRO ASP LEU VAL THR VAL ASN HIS LEU ASP GLY ILE
SEQRES 26 A 602 TRP THR ASP ASP PHE HIS HIS GLU THR ARG VAL THR LEU
SEQRES 27 A 602 THR GLY GLU GLN GLU GLY TYR TYR ALA GLY TYR ARG GLY
SEQRES 28 A 602 GLY ALA GLU ALA LEU ALA TYR THR ILE ARG ARG GLY TRP
SEQRES 29 A 602 ARG TYR GLU GLY GLN PHE TRP ALA VAL LYS GLY GLU GLU
SEQRES 30 A 602 HIS GLU ARG GLY HIS PRO SER ASP ALA LEU GLU ALA PRO
SEQRES 31 A 602 ASN PHE VAL TYR CYS ILE GLN ASN HIS ASP GLN ILE GLY
SEQRES 32 A 602 ASN ARG PRO LEU GLY GLU ARG LEU HIS GLN SER ASP GLY
SEQRES 33 A 602 VAL THR LEU HIS GLU TYR ARG GLY ALA ALA ALA LEU LEU
SEQRES 34 A 602 LEU THR LEU PRO MET THR PRO LEU LEU PHE GLN GLY GLN
SEQRES 35 A 602 GLU TRP ALA ALA SER THR PRO PHE GLN PHE PHE SER ASP
SEQRES 36 A 602 HIS ALA GLY GLU LEU GLY GLN ALA VAL SER GLU GLY ARG
SEQRES 37 A 602 LYS LYS GLU PHE GLY GLY PHE SER GLY PHE SER GLY GLU
SEQRES 38 A 602 ASP VAL PRO ASP PRO GLN ALA GLU GLN THR PHE LEU ASN
SEQRES 39 A 602 SER LYS LEU ASN TRP ALA GLU ARG GLU GLY GLY GLU HIS
SEQRES 40 A 602 ALA ARG THR LEU ARG LEU TYR ARG ASP LEU LEU ARG LEU
SEQRES 41 A 602 ARG ARG GLU ASP PRO VAL LEU HIS ASN ARG GLN ARG GLU
SEQRES 42 A 602 ASN LEU THR THR GLY HIS ASP GLY ASP VAL LEU TRP VAL
SEQRES 43 A 602 ARG THR VAL THR GLY ALA GLY GLU ARG VAL LEU LEU TRP
SEQRES 44 A 602 ASN LEU GLY GLN ASP THR ARG ALA VAL ALA GLU VAL LYS
SEQRES 45 A 602 LEU PRO PHE THR VAL PRO ARG ARG LEU LEU LEU HIS THR
SEQRES 46 A 602 GLU GLY ARG GLU ASP LEU THR LEU GLY ALA GLY GLU ALA
SEQRES 47 A 602 VAL LEU VAL GLY
HET MG A1606 1
HET TRS A1603 16
HET PGE A1604 20
HETNAM MG MAGNESIUM ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN TRS TRIS BUFFER
FORMUL 2 MG MG 2+
FORMUL 3 TRS C4 H12 N O3 1+
FORMUL 4 PGE C6 H14 O4
FORMUL 5 HOH *1130(H2 O1)
HELIX 1 1 ASP A 20 ARG A 24 5 5
HELIX 2 2 PRO A 31 ALA A 34 5 4
HELIX 3 3 LYS A 123 CYS A 127 5 5
HELIX 4 4 HIS A 133 THR A 138 1 6
HELIX 5 5 THR A 142 LYS A 149 1 8
HELIX 6 6 LYS A 149 GLY A 157 1 9
HELIX 7 7 ALA A 187 GLY A 190 5 4
HELIX 8 8 ARG A 191 LEU A 205 1 15
HELIX 9 9 TYR A 224 ALA A 229 1 6
HELIX 10 10 GLU A 249 HIS A 268 1 20
HELIX 11 11 ALA A 276 MET A 280 5 5
HELIX 12 12 HIS A 287 GLU A 298 1 12
HELIX 13 13 PRO A 314 VAL A 319 1 6
HELIX 14 14 ASP A 328 GLY A 340 1 13
HELIX 15 15 GLU A 343 TYR A 349 5 7
HELIX 16 16 GLY A 352 GLY A 363 1 12
HELIX 17 17 GLU A 388 PRO A 390 5 3
HELIX 18 18 ASN A 398 ASN A 404 1 7
HELIX 19 19 ARG A 410 SER A 414 5 5
HELIX 20 20 THR A 418 LEU A 432 1 15
HELIX 21 21 GLY A 441 ALA A 445 5 5
HELIX 22 22 ALA A 457 PHE A 472 1 16
HELIX 23 23 ALA A 488 ASN A 494 1 7
HELIX 24 24 TRP A 499 GLU A 503 5 5
HELIX 25 25 GLY A 504 ASP A 524 1 21
HELIX 26 26 GLN A 531 GLU A 533 5 3
HELIX 27 27 ALA A 569 VAL A 571 5 3
SHEET 1 AA 4 GLY A 26 PRO A 29 0
SHEET 2 AA 4 THR A 36 TRP A 41 -1 O ARG A 37 N THR A 28
SHEET 3 AA 4 ILE A 66 LEU A 71 -1 O TYR A 67 N LEU A 40
SHEET 4 AA 4 THR A 60 GLY A 63 -1 O THR A 60 N GLU A 68
SHEET 1 AB 4 THR A 55 VAL A 58 0
SHEET 2 AB 4 VAL A 48 VAL A 52 -1 O VAL A 50 N HIS A 57
SHEET 3 AB 4 ARG A 78 LEU A 83 -1 O LEU A 80 N ARG A 51
SHEET 4 AB 4 ALA A 104 GLU A 105 -1 O ALA A 104 N TYR A 79
SHEET 1 AC 4 THR A 55 VAL A 58 0
SHEET 2 AC 4 VAL A 48 VAL A 52 -1 O VAL A 50 N HIS A 57
SHEET 3 AC 4 ARG A 78 LEU A 83 -1 O LEU A 80 N ARG A 51
SHEET 4 AC 4 VAL A 86 THR A 88 -1 O VAL A 86 N LEU A 83
SHEET 1 AD 9 PHE A 129 VAL A 132 0
SHEET 2 AD 9 ALA A 160 VAL A 163 1 O ALA A 160 N TYR A 130
SHEET 3 AD 9 GLY A 208 VAL A 213 1 O GLY A 208 N ILE A 161
SHEET 4 AD 9 GLY A 271 LEU A 274 1 O GLY A 271 N LEU A 211
SHEET 5 AD 9 LEU A 304 GLU A 308 1 O LEU A 304 N LEU A 272
SHEET 6 AD 9 GLY A 324 TRP A 326 1 O GLY A 324 N ALA A 307
SHEET 7 AD 9 PHE A 392 CYS A 395 1 N VAL A 393 O ILE A 325
SHEET 8 AD 9 THR A 435 PHE A 439 1 O THR A 435 N TYR A 394
SHEET 9 AD 9 PHE A 129 VAL A 132 1 O PHE A 129 N LEU A 438
SHEET 1 AE 2 ALA A 167 ALA A 168 0
SHEET 2 AE 2 ALA A 181 PRO A 185 -1 N ALA A 181 O ALA A 168
SHEET 1 AF 2 PHE A 233 SER A 238 0
SHEET 2 AF 2 MET A 243 LEU A 245 -1 O GLY A 244 N THR A 234
SHEET 1 AG 2 GLU A 367 TRP A 371 0
SHEET 2 AG 2 HIS A 378 GLY A 381 -1 O HIS A 378 N TRP A 371
SHEET 1 AH 5 LEU A 535 ASP A 540 0
SHEET 2 AH 5 VAL A 543 THR A 550 -1 O VAL A 543 N ASP A 540
SHEET 3 AH 5 GLY A 553 ASN A 560 -1 O GLY A 553 N THR A 550
SHEET 4 AH 5 ALA A 598 GLY A 602 -1 O VAL A 599 N LEU A 558
SHEET 5 AH 5 ARG A 580 HIS A 584 -1 O ARG A 580 N GLY A 602
SHEET 1 AI 2 ARG A 566 ALA A 567 0
SHEET 2 AI 2 THR A 592 LEU A 593 -1 O LEU A 593 N ARG A 566
LINK NE2BGLN A 369 C3 BPGE A1604 1555 1555 2.01
LINK MG MG A1606 OD1 ASP A 540 1555 1565 2.13
LINK MG MG A1606 O HOH A2300 1555 1555 2.08
LINK MG MG A1606 O HOH A2316 1555 1555 2.08
LINK MG MG A1606 O HOH A3009 1555 1565 2.05
LINK MG MG A1606 O HOH A3064 1555 1565 2.08
SITE 1 AC1 6 ASP A 113 ASP A 540 HOH A2300 HOH A2316
SITE 2 AC1 6 HOH A3009 HOH A3064
SITE 1 AC2 11 THR A 337 LEU A 338 GLY A 416 GLU A 421
SITE 2 AC2 11 GLN A 563 HOH A3045 HOH A3119 HOH A3120
SITE 3 AC2 11 HOH A3121 HOH A3123 HOH A3124
SITE 1 AC3 14 PRO A 31 ALA A 34 PRO A 72 GLY A 348
SITE 2 AC3 14 TYR A 349 TYR A 358 ARG A 365 TYR A 366
SITE 3 AC3 14 GLN A 369 HOH A2083 HOH A3127 HOH A3128
SITE 4 AC3 14 HOH A3129 HOH A3130
CRYST1 59.580 66.620 152.510 90.00 90.00 90.00 P 21 21 21 4
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 0.016784 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006557 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
