HEADER TRANSFERASE 16-NOV-07 3BE4
TITLE CRYSTAL STRUCTURE OF CRYPTOSPORIDIUM PARVUM ADENYLATE KINASE CGD5_3360
CAVEAT 3BE4 CHIRALITY ERRORS AT RESIDUE A 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM IOWA II;
SOURCE 3 ORGANISM_TAXID: 353152;
SOURCE 4 STRAIN: IOWA TYPE II;
SOURCE 5 GENE: CDG5_3360;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15-TEV-LIC
KEYWDS ADENYLATE KINASE, MALARIA, CRYPTOSPORIDIUM PARVUM NONPROTEIN KINASE
KEYWDS 2 INHIBITORS, NUCLEOTIDE-BINDING, TRANSFERASE, STRUCTURAL GENOMICS,
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,J.LEW,I.KOZIERADZKI,Y.H.LIN,X.SUN,C.KHUU,Y.ZHAO,
AUTHOR 2 M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,A.BOCHKAREV,R.HUI,
AUTHOR 3 J.D.ARTZ,M.AMANI,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 30-AUG-23 3BE4 1 REMARK SEQADV LINK
REVDAT 4 25-OCT-17 3BE4 1 REMARK
REVDAT 3 13-JUL-11 3BE4 1 VERSN
REVDAT 2 24-FEB-09 3BE4 1 VERSN
REVDAT 1 18-DEC-07 3BE4 0
JRNL AUTH A.K.WERNIMONT,J.LEW,I.KOZIERADZKI,Y.H.LIN,X.SUN,C.KHUU,
JRNL AUTH 2 Y.ZHAO,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,
JRNL AUTH 3 A.BOCHKAREV,R.HUI,J.D.ARTZ,M.AMANI
JRNL TITL CRYSTAL STRUCTURE OF CRYPTOSPORIDIUM PARVUM ADENYLATE KINASE
JRNL TITL 2 CGD5_3360.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 36130
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1814
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2582
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1655
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 259
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.01000
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): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.570
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1805 ; 0.035 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2462 ; 2.939 ; 2.034
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 229 ; 6.950 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;37.836 ;25.270
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 319 ;15.529 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;18.141 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.370 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1318 ; 0.017 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 926 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1254 ; 0.319 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 207 ; 0.213 ; 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): 37 ; 0.268 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.412 ; 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): 1127 ; 1.980 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1766 ; 2.748 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 783 ; 3.965 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 688 ; 5.429 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3BE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36167
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46600
REMARK 200 R SYM FOR SHELL (I) : 0.43800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1AK2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE, 0.1 M BTP PH
REMARK 280 7.0, 10 MM ADENOSINE-5-PENTAPHOSPHATE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 50.58750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.20671
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.14433
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 50.58750
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 29.20671
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 24.14433
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 50.58750
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 29.20671
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 24.14433
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.41341
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 48.28867
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 58.41341
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 48.28867
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 58.41341
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 48.28867
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 THR A 48
REMARK 465 LYS A 49
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 LYS A 27 CG CD CE NZ
REMARK 470 LYS A 45 CG CD CE NZ
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; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 198 NZ
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 N GLY A 1 O ASN A 84 1.52
REMARK 500 O HOH A 321 O HOH A 464 2.04
REMARK 500 O HOH A 385 O HOH A 466 2.05
REMARK 500 OE1 GLU A 171 O HOH A 460 2.17
REMARK 500 O HOH A 302 O HOH A 425 2.19
REMARK 500 OE1 GLU A 171 O HOH A 412 2.19
REMARK 500 O HOH A 306 O HOH A 406 2.19
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 ND2 ASN A 2 O HOH A 448 5555 1.63
REMARK 500 O HOH A 341 O HOH A 452 3555 1.89
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 LYS A 26 CB LYS A 26 CG -0.238
REMARK 500 ARG A 41 CD ARG A 41 NE -0.104
REMARK 500 ARG A 41 CZ ARG A 41 NH1 -0.117
REMARK 500 ARG A 41 CZ ARG A 41 NH2 0.106
REMARK 500 PHE A 77 CE1 PHE A 77 CZ 0.116
REMARK 500 SER A 130 CB SER A 130 OG -0.096
REMARK 500 CYS A 133 CB CYS A 133 SG -0.124
REMARK 500 LYS A 198 CE LYS A 198 NZ -0.656
REMARK 500 GLU A 208 CG GLU A 208 CD 0.093
REMARK 500 GLU A 211 CG GLU A 211 CD 0.112
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 38 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 41 CG - CD - NE ANGL. DEV. = -15.9 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH1 ANGL. DEV. = -17.5 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH2 ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU A 52 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP A 66 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ILE A 141 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 ASP A 168 CB - CG - OD1 ANGL. DEV. = 6.0 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
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 ASN A 2 -116.50 53.22
REMARK 500 ASN A 147 65.64 -161.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 168 -13.62
REMARK 500
REMARK 500 REMARK: NULL
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 A 218 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AP5 A 219 O2G
REMARK 620 2 AP5 A 219 O1D 90.0
REMARK 620 3 HOH A 418 O 170.7 97.5
REMARK 620 4 HOH A 419 O 95.1 87.9 90.7
REMARK 620 5 HOH A 423 O 87.1 88.7 87.6 176.0
REMARK 620 6 HOH A 424 O 84.8 174.1 87.9 89.6 93.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AP5 A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 221
DBREF 3BE4 A 2 217 UNP Q5CRC5 Q5CRC5_CRYPV 4 219
SEQADV 3BE4 GLY A 1 UNP Q5CRC5 EXPRESSION TAG
SEQRES 1 A 217 GLY ASN SER LYS LYS HIS ASN LEU ILE LEU ILE GLY ALA
SEQRES 2 A 217 PRO GLY SER GLY LYS GLY THR GLN CYS GLU PHE ILE LYS
SEQRES 3 A 217 LYS GLU TYR GLY LEU ALA HIS LEU SER THR GLY ASP MET
SEQRES 4 A 217 LEU ARG GLU ALA ILE LYS ASN GLY THR LYS ILE GLY LEU
SEQRES 5 A 217 GLU ALA LYS SER ILE ILE GLU SER GLY ASN PHE VAL GLY
SEQRES 6 A 217 ASP GLU ILE VAL LEU GLY LEU VAL LYS GLU LYS PHE ASP
SEQRES 7 A 217 LEU GLY VAL CYS VAL ASN GLY PHE VAL LEU ASP GLY PHE
SEQRES 8 A 217 PRO ARG THR ILE PRO GLN ALA GLU GLY LEU ALA LYS ILE
SEQRES 9 A 217 LEU SER GLU ILE GLY ASP SER LEU THR SER VAL ILE TYR
SEQRES 10 A 217 PHE GLU ILE ASP ASP SER GLU ILE ILE GLU ARG ILE SER
SEQRES 11 A 217 GLY ARG CYS THR HIS PRO ALA SER GLY ARG ILE TYR HIS
SEQRES 12 A 217 VAL LYS TYR ASN PRO PRO LYS GLN PRO GLY ILE ASP ASP
SEQRES 13 A 217 VAL THR GLY GLU PRO LEU VAL TRP ARG ASP ASP ASP ASN
SEQRES 14 A 217 ALA GLU ALA VAL LYS VAL ARG LEU ASP VAL PHE HIS LYS
SEQRES 15 A 217 GLN THR ALA PRO LEU VAL LYS PHE TYR GLU ASP LEU GLY
SEQRES 16 A 217 ILE LEU LYS ARG VAL ASN ALA LYS LEU PRO PRO LYS GLU
SEQRES 17 A 217 VAL THR GLU GLN ILE LYS LYS ILE LEU
HET MG A 218 1
HET AP5 A 219 57
HET GOL A 220 6
HET GOL A 221 6
HETNAM MG MAGNESIUM ION
HETNAM AP5 BIS(ADENOSINE)-5'-PENTAPHOSPHATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 MG MG 2+
FORMUL 3 AP5 C20 H29 N10 O22 P5
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *259(H2 O)
HELIX 1 1 GLY A 1 LYS A 5 5 5
HELIX 2 2 GLY A 17 GLY A 30 1 14
HELIX 3 3 THR A 36 ASN A 46 1 11
HELIX 4 4 GLY A 51 GLY A 61 1 11
HELIX 5 5 GLY A 65 LEU A 79 1 15
HELIX 6 6 THR A 94 GLY A 109 1 16
HELIX 7 7 ASP A 121 GLY A 131 1 11
HELIX 8 8 ARG A 165 ASP A 168 5 4
HELIX 9 9 ASN A 169 THR A 184 1 16
HELIX 10 10 PRO A 186 ASP A 193 1 8
HELIX 11 11 PRO A 205 LEU A 217 1 13
SHEET 1 A 5 ALA A 32 SER A 35 0
SHEET 2 A 5 PHE A 86 ASP A 89 1 O VAL A 87 N ALA A 32
SHEET 3 A 5 ASN A 7 GLY A 12 1 N LEU A 8 O PHE A 86
SHEET 4 A 5 SER A 114 GLU A 119 1 O PHE A 118 N ILE A 11
SHEET 5 A 5 LEU A 197 ASN A 201 1 O LYS A 198 N TYR A 117
SHEET 1 B 2 ARG A 132 THR A 134 0
SHEET 2 B 2 ILE A 141 HIS A 143 -1 O TYR A 142 N CYS A 133
LINK MG MG A 218 O2G AP5 A 219 1555 1555 2.02
LINK MG MG A 218 O1D AP5 A 219 1555 1555 2.02
LINK MG MG A 218 O HOH A 418 1555 1555 2.12
LINK MG MG A 218 O HOH A 419 1555 1555 2.10
LINK MG MG A 218 O HOH A 423 1555 1555 2.09
LINK MG MG A 218 O HOH A 424 1555 1555 2.11
CISPEP 1 PHE A 91 PRO A 92 0 -12.94
SITE 1 AC1 5 AP5 A 219 HOH A 418 HOH A 419 HOH A 423
SITE 2 AC1 5 HOH A 424
SITE 1 AC2 42 PRO A 14 GLY A 15 SER A 16 GLY A 17
SITE 2 AC2 42 LYS A 18 GLY A 19 THR A 20 THR A 36
SITE 3 AC2 42 GLY A 37 LEU A 40 ARG A 41 ILE A 58
SITE 4 AC2 42 ASN A 62 VAL A 64 VAL A 69 GLY A 90
SITE 5 AC2 42 PHE A 91 ARG A 93 GLN A 97 ARG A 128
SITE 6 AC2 42 ARG A 132 ILE A 141 TYR A 142 HIS A 143
SITE 7 AC2 42 TYR A 146 ARG A 165 ARG A 176 LEU A 204
SITE 8 AC2 42 PRO A 205 PRO A 206 MG A 218 HOH A 227
SITE 9 AC2 42 HOH A 228 HOH A 230 HOH A 232 HOH A 233
SITE 10 AC2 42 HOH A 237 HOH A 254 HOH A 279 HOH A 419
SITE 11 AC2 42 HOH A 423 HOH A 424
SITE 1 AC3 7 GLU A 23 ARG A 140 ILE A 141 TYR A 142
SITE 2 AC3 7 GOL A 221 HOH A 297 HOH A 366
SITE 1 AC4 4 ASN A 147 GOL A 220 HOH A 335 HOH A 447
CRYST1 101.175 101.175 72.433 90.00 90.00 120.00 H 3 9
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 0.009884 0.005706 0.000000 0.00000
SCALE2 0.000000 0.011413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
