HEADER TRANSFERASE/TRANSFERASE INHIBITOR 12-APR-12 4EN4
TITLE CRYSTAL STRUCTURE OF THE TERNARY HUMAN PL KINASE-GINKGOTOXIN-MGATP
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXAL KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PYRIDOXINE KINASE;
COMPND 5 EC: 2.7.1.35;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDXK, C21ORF124, C21ORF97, PKH, PNK, PRED79;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.SAFO,F.N.MUSAYEV,A.K.GANDHI
REVDAT 4 13-MAR-24 4EN4 1 SOURCE
REVDAT 3 13-SEP-23 4EN4 1 REMARK LINK
REVDAT 2 22-AUG-12 4EN4 1 JRNL
REVDAT 1 02-MAY-12 4EN4 0
JRNL AUTH A.K.GANDHI,J.V.DESAI,M.S.GHATGE,M.L.DI SALVO,S.DI BIASE,
JRNL AUTH 2 R.DANSO-DANQUAH,F.N.MUSAYEV,R.CONTESTABILE,V.SCHIRCH,
JRNL AUTH 3 M.K.SAFO
JRNL TITL CRYSTAL STRUCTURES OF HUMAN PYRIDOXAL KINASE IN COMPLEX WITH
JRNL TITL 2 THE NEUROTOXINS, GINKGOTOXIN AND THEOPHYLLINE: INSIGHTS INTO
JRNL TITL 3 PYRIDOXAL KINASE INHIBITION.
JRNL REF PLOS ONE V. 7 40954 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22879864
JRNL DOI 10.1371/JOURNAL.PONE.0040954
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3465978.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 45953
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 SET) : 0.219
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2312
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4283
REMARK 3 BIN R VALUE (WORKING SET) : 0.4250
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 243
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 206
REMARK 3 SOLVENT ATOMS : 268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.81000
REMARK 3 B22 (A**2) : -5.41000
REMARK 3 B33 (A**2) : -8.40000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.57
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.75
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.230
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.720 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.490 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 57.78
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : ATP.PAR
REMARK 3 PARAMETER FILE 5 : MPD.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4EN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.2SSI
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49008
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 28.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.330
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.65
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3FHX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: GINKGOTOXIN, MGATP, 48-50% MPD, PH
REMARK 280 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.37450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.61050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.77700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.37450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.61050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.77700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.37450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.61050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.77700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.37450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.61050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 84.77700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 502 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 MET B 1
REMARK 465 GLU B 2
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 NE ARG B 206 O HOH B 536 2.15
REMARK 500 N GLY B 232 O6 GT1 B 405 2.17
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 GLU A 4 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 GLY B 279 N - CA - C ANGL. DEV. = 16.1 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 TRP A 52 131.88 -173.71
REMARK 500 ASN A 73 32.66 71.26
REMARK 500 LEU A 116 -34.91 -135.48
REMARK 500 ASP A 121 80.17 30.04
REMARK 500 SER A 125 133.88 -171.70
REMARK 500 ASP A 131 8.10 -69.74
REMARK 500 SER A 187 146.23 -172.70
REMARK 500 ASN A 197 42.74 -70.85
REMARK 500 ASP A 227 62.07 -69.81
REMARK 500 ASN A 250 53.73 -116.67
REMARK 500 ASN A 251 71.78 -155.86
REMARK 500 ASP A 302 85.75 -150.31
REMARK 500 GLU B 4 137.61 -170.38
REMARK 500 TRP B 52 143.37 -170.61
REMARK 500 ASN B 75 51.27 -106.93
REMARK 500 LEU B 116 -30.79 -132.49
REMARK 500 ASP B 121 -42.95 70.20
REMARK 500 SER B 196 -11.90 146.63
REMARK 500 HIS B 248 67.26 -119.58
REMARK 500 ALA B 278 63.88 -118.03
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 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 113 OD1
REMARK 620 2 THR A 148 O 63.7
REMARK 620 3 THR A 186 OG1 162.1 103.1
REMARK 620 4 ATP A 404 O3B 112.9 174.1 79.1
REMARK 620 5 ATP A 404 O2G 72.1 124.6 125.4 56.3
REMARK 620 6 HOH A 518 O 67.6 87.3 101.2 86.9 105.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD2
REMARK 620 2 ATP A 404 O1B 100.0
REMARK 620 3 ATP A 404 O2A 173.1 86.2
REMARK 620 4 MPD A 406 O4 65.8 165.3 107.7
REMARK 620 5 HOH A 589 O 91.2 91.0 85.7 85.7
REMARK 620 6 HOH A 590 O 67.6 97.5 114.8 81.0 158.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 235 OD1
REMARK 620 2 GT1 A 410 O2 98.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 118 OD2
REMARK 620 2 ATP B 404 O1A 150.0
REMARK 620 3 ATP B 404 O2B 80.6 77.0
REMARK 620 4 MPD B 407 O4 87.1 103.8 152.0
REMARK 620 5 HOH B 505 O 71.6 86.0 83.0 69.3
REMARK 620 6 HOH B 506 O 97.4 95.4 74.2 132.6 156.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 148 O
REMARK 620 2 THR B 186 OG1 102.7
REMARK 620 3 ATP B 404 O3B 169.8 85.7
REMARK 620 4 ATP B 404 O1G 112.3 128.7 57.5
REMARK 620 5 HOH B 507 O 94.2 110.5 88.1 103.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 235 OD1
REMARK 620 2 ATP B 404 O2G 111.6
REMARK 620 3 GT1 B 405 O2 85.6 99.4
REMARK 620 N 1 2
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GT0 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GT1 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GT1 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GT0 B 414
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YXU RELATED DB: PDB
REMARK 900 RELATED ID: 4EOH RELATED DB: PDB
DBREF 4EN4 A 1 312 UNP O00764 PDXK_HUMAN 1 312
DBREF 4EN4 B 1 312 UNP O00764 PDXK_HUMAN 1 312
SEQRES 1 A 312 MET GLU GLU GLU CYS ARG VAL LEU SER ILE GLN SER HIS
SEQRES 2 A 312 VAL ILE ARG GLY TYR VAL GLY ASN ARG ALA ALA THR PHE
SEQRES 3 A 312 PRO LEU GLN VAL LEU GLY PHE GLU ILE ASP ALA VAL ASN
SEQRES 4 A 312 SER VAL GLN PHE SER ASN HIS THR GLY TYR ALA HIS TRP
SEQRES 5 A 312 LYS GLY GLN VAL LEU ASN SER ASP GLU LEU GLN GLU LEU
SEQRES 6 A 312 TYR GLU GLY LEU ARG LEU ASN ASN MET ASN LYS TYR ASP
SEQRES 7 A 312 TYR VAL LEU THR GLY TYR THR ARG ASP LYS SER PHE LEU
SEQRES 8 A 312 ALA MET VAL VAL ASP ILE VAL GLN GLU LEU LYS GLN GLN
SEQRES 9 A 312 ASN PRO ARG LEU VAL TYR VAL CYS ASP PRO VAL LEU GLY
SEQRES 10 A 312 ASP LYS TRP ASP GLY GLU GLY SER MET TYR VAL PRO GLU
SEQRES 11 A 312 ASP LEU LEU PRO VAL TYR LYS GLU LYS VAL VAL PRO LEU
SEQRES 12 A 312 ALA ASP ILE ILE THR PRO ASN GLN PHE GLU ALA GLU LEU
SEQRES 13 A 312 LEU SER GLY ARG LYS ILE HIS SER GLN GLU GLU ALA LEU
SEQRES 14 A 312 ARG VAL MET ASP MET LEU HIS SER MET GLY PRO ASP THR
SEQRES 15 A 312 VAL VAL ILE THR SER SER ASP LEU PRO SER PRO GLN GLY
SEQRES 16 A 312 SER ASN TYR LEU ILE VAL LEU GLY SER GLN ARG ARG ARG
SEQRES 17 A 312 ASN PRO ALA GLY SER VAL VAL MET GLU ARG ILE ARG MET
SEQRES 18 A 312 ASP ILE ARG LYS VAL ASP ALA VAL PHE VAL GLY THR GLY
SEQRES 19 A 312 ASP LEU PHE ALA ALA MET LEU LEU ALA TRP THR HIS LYS
SEQRES 20 A 312 HIS PRO ASN ASN LEU LYS VAL ALA CYS GLU LYS THR VAL
SEQRES 21 A 312 SER THR LEU HIS HIS VAL LEU GLN ARG THR ILE GLN CYS
SEQRES 22 A 312 ALA LYS ALA GLN ALA GLY GLU GLY VAL ARG PRO SER PRO
SEQRES 23 A 312 MET GLN LEU GLU LEU ARG MET VAL GLN SER LYS ARG ASP
SEQRES 24 A 312 ILE GLU ASP PRO GLU ILE VAL VAL GLN ALA THR VAL LEU
SEQRES 1 B 312 MET GLU GLU GLU CYS ARG VAL LEU SER ILE GLN SER HIS
SEQRES 2 B 312 VAL ILE ARG GLY TYR VAL GLY ASN ARG ALA ALA THR PHE
SEQRES 3 B 312 PRO LEU GLN VAL LEU GLY PHE GLU ILE ASP ALA VAL ASN
SEQRES 4 B 312 SER VAL GLN PHE SER ASN HIS THR GLY TYR ALA HIS TRP
SEQRES 5 B 312 LYS GLY GLN VAL LEU ASN SER ASP GLU LEU GLN GLU LEU
SEQRES 6 B 312 TYR GLU GLY LEU ARG LEU ASN ASN MET ASN LYS TYR ASP
SEQRES 7 B 312 TYR VAL LEU THR GLY TYR THR ARG ASP LYS SER PHE LEU
SEQRES 8 B 312 ALA MET VAL VAL ASP ILE VAL GLN GLU LEU LYS GLN GLN
SEQRES 9 B 312 ASN PRO ARG LEU VAL TYR VAL CYS ASP PRO VAL LEU GLY
SEQRES 10 B 312 ASP LYS TRP ASP GLY GLU GLY SER MET TYR VAL PRO GLU
SEQRES 11 B 312 ASP LEU LEU PRO VAL TYR LYS GLU LYS VAL VAL PRO LEU
SEQRES 12 B 312 ALA ASP ILE ILE THR PRO ASN GLN PHE GLU ALA GLU LEU
SEQRES 13 B 312 LEU SER GLY ARG LYS ILE HIS SER GLN GLU GLU ALA LEU
SEQRES 14 B 312 ARG VAL MET ASP MET LEU HIS SER MET GLY PRO ASP THR
SEQRES 15 B 312 VAL VAL ILE THR SER SER ASP LEU PRO SER PRO GLN GLY
SEQRES 16 B 312 SER ASN TYR LEU ILE VAL LEU GLY SER GLN ARG ARG ARG
SEQRES 17 B 312 ASN PRO ALA GLY SER VAL VAL MET GLU ARG ILE ARG MET
SEQRES 18 B 312 ASP ILE ARG LYS VAL ASP ALA VAL PHE VAL GLY THR GLY
SEQRES 19 B 312 ASP LEU PHE ALA ALA MET LEU LEU ALA TRP THR HIS LYS
SEQRES 20 B 312 HIS PRO ASN ASN LEU LYS VAL ALA CYS GLU LYS THR VAL
SEQRES 21 B 312 SER THR LEU HIS HIS VAL LEU GLN ARG THR ILE GLN CYS
SEQRES 22 B 312 ALA LYS ALA GLN ALA GLY GLU GLY VAL ARG PRO SER PRO
SEQRES 23 B 312 MET GLN LEU GLU LEU ARG MET VAL GLN SER LYS ARG ASP
SEQRES 24 B 312 ILE GLU ASP PRO GLU ILE VAL VAL GLN ALA THR VAL LEU
HET MG A 401 1
HET NA A 402 1
HET MG A 403 1
HET ATP A 404 31
HET GT0 A 405 13
HET MPD A 406 8
HET SO4 A 407 5
HET SO4 A 408 5
HET SO4 A 409 5
HET GT1 A 410 17
HET MG B 401 1
HET NA B 402 1
HET MG B 403 1
HET ATP B 404 31
HET GT1 B 405 17
HET MPD B 406 8
HET MPD B 407 8
HET MPD B 408 8
HET MPD B 409 8
HET MPD B 410 8
HET SO4 B 411 5
HET SO4 B 412 5
HET SO4 B 413 5
HET GT0 B 414 13
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM GT0 5-(HYDROXYMETHYL)-4-(METHOXYMETHYL)-2-METHYLPYRIDIN-3-
HETNAM 2 GT0 OL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SO4 SULFATE ION
HETNAM GT1 [5-HYDROXY-4-(METHOXYMETHYL)-6-METHYLPYRIDIN-3-
HETNAM 2 GT1 YL]METHYL DIHYDROGEN PHOSPHATE
HETSYN GT0 GINKGOTOXIN
HETSYN GT1 GINKGOTOXIN, PHOSPHORYLATED
FORMUL 3 MG 4(MG 2+)
FORMUL 4 NA 2(NA 1+)
FORMUL 6 ATP 2(C10 H16 N5 O13 P3)
FORMUL 7 GT0 2(C9 H13 N O3)
FORMUL 8 MPD 6(C6 H14 O2)
FORMUL 9 SO4 6(O4 S 2-)
FORMUL 12 GT1 2(C9 H14 N O6 P)
FORMUL 27 HOH *268(H2 O)
HELIX 1 1 GLY A 20 LEU A 31 1 12
HELIX 2 2 ASN A 58 ASN A 72 1 15
HELIX 3 3 ASP A 87 ASN A 105 1 19
HELIX 4 4 ASP A 131 LYS A 139 1 9
HELIX 5 5 LYS A 139 ALA A 144 1 6
HELIX 6 6 ASN A 150 GLY A 159 1 10
HELIX 7 7 SER A 164 MET A 178 1 15
HELIX 8 8 GLY A 232 HIS A 248 1 17
HELIX 9 9 ASN A 251 GLY A 279 1 29
HELIX 10 10 SER A 285 GLU A 290 1 6
HELIX 11 11 MET A 293 GLN A 295 5 3
HELIX 12 12 SER A 296 ASP A 302 1 7
HELIX 13 13 GLY B 20 LEU B 31 1 12
HELIX 14 14 ASN B 58 ASN B 72 1 15
HELIX 15 15 ASP B 87 ASN B 105 1 19
HELIX 16 16 PRO B 129 ASP B 131 5 3
HELIX 17 17 LEU B 132 LYS B 139 1 8
HELIX 18 18 LYS B 139 ALA B 144 1 6
HELIX 19 19 ASN B 150 GLY B 159 1 10
HELIX 20 20 SER B 164 GLY B 179 1 16
HELIX 21 21 GLY B 232 HIS B 248 1 17
HELIX 22 22 ASN B 251 ALA B 278 1 28
HELIX 23 23 MET B 293 GLN B 295 5 3
HELIX 24 24 SER B 296 ASP B 302 1 7
SHEET 1 A10 GLY A 54 VAL A 56 0
SHEET 2 A10 GLU A 34 PHE A 43 -1 N GLN A 42 O GLN A 55
SHEET 3 A10 ARG A 6 VAL A 14 1 N VAL A 7 O ASP A 36
SHEET 4 A10 TYR A 79 THR A 82 1 O LEU A 81 N LEU A 8
SHEET 5 A10 VAL A 109 CYS A 112 1 O VAL A 111 N VAL A 80
SHEET 6 A10 ILE A 146 ILE A 147 1 O ILE A 146 N CYS A 112
SHEET 7 A10 THR A 182 ILE A 185 1 O THR A 182 N ILE A 147
SHEET 8 A10 TYR A 198 ARG A 208 -1 O LEU A 202 N ILE A 185
SHEET 9 A10 VAL A 214 ARG A 224 -1 O VAL A 215 N ARG A 207
SHEET 10 A10 THR A 310 VAL A 311 -1 O THR A 310 N ARG A 220
SHEET 1 B 2 GLY A 117 TRP A 120 0
SHEET 2 B 2 GLU A 123 MET A 126 -1 O SER A 125 N ASP A 118
SHEET 1 C10 GLY B 54 VAL B 56 0
SHEET 2 C10 GLU B 34 PHE B 43 -1 N GLN B 42 O GLN B 55
SHEET 3 C10 ARG B 6 VAL B 14 1 N SER B 9 O VAL B 38
SHEET 4 C10 TYR B 79 THR B 82 1 O LEU B 81 N LEU B 8
SHEET 5 C10 VAL B 109 CYS B 112 1 O VAL B 111 N VAL B 80
SHEET 6 C10 ILE B 146 ILE B 147 1 O ILE B 146 N CYS B 112
SHEET 7 C10 THR B 182 ILE B 185 1 O THR B 182 N ILE B 147
SHEET 8 C10 TYR B 198 ARG B 208 -1 O SER B 204 N VAL B 183
SHEET 9 C10 VAL B 214 ARG B 224 -1 O ILE B 219 N GLY B 203
SHEET 10 C10 THR B 310 LEU B 312 -1 O THR B 310 N ARG B 220
SHEET 1 D 2 GLY B 117 TRP B 120 0
SHEET 2 D 2 GLU B 123 MET B 126 -1 O GLU B 123 N TRP B 120
LINK OD1 ASP A 113 NA NA A 402 1555 1555 3.12
LINK OD2 ASP A 118 MG MG A 401 1555 1555 2.29
LINK O THR A 148 NA NA A 402 1555 1555 2.43
LINK OG1 THR A 186 NA NA A 402 1555 1555 2.71
LINK OD1 ASP A 235 MG MG A 403 1555 1555 2.65
LINK MG MG A 401 O1B ATP A 404 1555 1555 2.03
LINK MG MG A 401 O2A ATP A 404 1555 1555 2.16
LINK MG MG A 401 O4 MPD A 406 1555 1555 2.16
LINK MG MG A 401 O HOH A 589 1555 1555 2.41
LINK MG MG A 401 O HOH A 590 1555 1555 2.29
LINK NA NA A 402 O3B ATP A 404 1555 1555 2.62
LINK NA NA A 402 O2G ATP A 404 1555 1555 2.83
LINK NA NA A 402 O HOH A 518 1555 1555 2.63
LINK MG MG A 403 O2 BGT1 A 410 1555 1555 2.38
LINK OD2 ASP B 118 MG MG B 401 1555 1555 2.15
LINK O THR B 148 NA NA B 402 1555 1555 2.41
LINK OG1 THR B 186 NA NA B 402 1555 1555 2.52
LINK OD1 ASP B 235 MG MG B 403 1555 1555 2.75
LINK MG MG B 401 O1A ATP B 404 1555 1555 2.22
LINK MG MG B 401 O2B ATP B 404 1555 1555 2.31
LINK MG MG B 401 O4 MPD B 407 1555 1555 2.50
LINK MG MG B 401 O HOH B 505 1555 1555 2.47
LINK MG MG B 401 O HOH B 506 1555 1555 2.34
LINK NA NA B 402 O3B ATP B 404 1555 1555 2.56
LINK NA NA B 402 O1G ATP B 404 1555 1555 2.74
LINK NA NA B 402 O HOH B 507 1555 1555 2.47
LINK MG MG B 403 O2G ATP B 404 1555 1555 2.99
LINK MG MG B 403 O2 BGT1 B 405 1555 1555 2.88
SITE 1 AC1 5 ASP A 118 ATP A 404 MPD A 406 HOH A 589
SITE 2 AC1 5 HOH A 590
SITE 1 AC2 7 ASP A 113 THR A 148 PRO A 149 ASN A 150
SITE 2 AC2 7 THR A 186 ATP A 404 HOH A 518
SITE 1 AC3 4 ASP A 235 ATP A 404 GT0 A 405 GT1 A 410
SITE 1 AC4 24 ASP A 113 ASP A 118 ASN A 150 GLU A 153
SITE 2 AC4 24 THR A 186 SER A 187 VAL A 201 ARG A 224
SITE 3 AC4 24 LYS A 225 VAL A 226 ALA A 228 THR A 233
SITE 4 AC4 24 GLY A 234 PHE A 237 LEU A 267 MG A 401
SITE 5 AC4 24 NA A 402 MG A 403 MPD A 406 GT1 A 410
SITE 6 AC4 24 HOH A 509 HOH A 515 HOH A 595 HOH A 596
SITE 1 AC5 9 SER A 12 GLY A 20 HIS A 46 THR A 47
SITE 2 AC5 9 TYR A 84 VAL A 231 ASP A 235 MG A 403
SITE 3 AC5 9 HOH A 501
SITE 1 AC6 8 ASP A 118 TRP A 120 LEU A 199 MG A 401
SITE 2 AC6 8 ATP A 404 HOH A 589 HOH A 590 HOH A 594
SITE 1 AC7 4 GLN A 63 ARG A 70 MET A 93 GLU A 100
SITE 1 AC8 2 GLY A 159 LYS A 161
SITE 1 AC9 4 LEU A 31 GLY A 32 HIS A 246 LYS A 247
SITE 1 BC1 11 SER A 12 THR A 47 TYR A 84 VAL A 231
SITE 2 BC1 11 GLY A 232 THR A 233 GLY A 234 ASP A 235
SITE 3 BC1 11 MG A 403 ATP A 404 HOH A 590
SITE 1 BC2 5 ASP B 118 ATP B 404 MPD B 407 HOH B 505
SITE 2 BC2 5 HOH B 506
SITE 1 BC3 6 ASP B 113 THR B 148 PRO B 149 THR B 186
SITE 2 BC3 6 ATP B 404 HOH B 507
SITE 1 BC4 5 VAL B 115 ASP B 235 ATP B 404 GT1 B 405
SITE 2 BC4 5 GT0 B 414
SITE 1 BC5 26 ASP B 113 ASP B 118 ASN B 150 GLU B 153
SITE 2 BC5 26 THR B 186 SER B 187 LEU B 199 VAL B 201
SITE 3 BC5 26 ARG B 224 LYS B 225 VAL B 226 ALA B 228
SITE 4 BC5 26 THR B 233 GLY B 234 LEU B 263 LEU B 267
SITE 5 BC5 26 MG B 401 NA B 402 MG B 403 GT1 B 405
SITE 6 BC5 26 MPD B 407 HOH B 506 HOH B 546 HOH B 576
SITE 7 BC5 26 HOH B 577 HOH B 626
SITE 1 BC6 11 SER B 12 THR B 47 TYR B 84 VAL B 231
SITE 2 BC6 11 GLY B 232 THR B 233 GLY B 234 ASP B 235
SITE 3 BC6 11 MG B 403 ATP B 404 HOH B 506
SITE 1 BC7 4 ASP B 181 ARG B 207 ARG B 208 MPD B 410
SITE 1 BC8 6 ASP B 118 MG B 401 ATP B 404 HOH B 505
SITE 2 BC8 6 HOH B 547 HOH B 605
SITE 1 BC9 5 ASP B 173 SER B 177 ARG B 206 LEU B 312
SITE 2 BC9 5 HOH B 633
SITE 1 CC1 2 GLN B 165 PRO B 193
SITE 1 CC2 6 GLY B 179 ASP B 181 MPD B 406 HOH B 528
SITE 2 CC2 6 HOH B 529 HOH B 602
SITE 1 CC3 1 GLY B 159
SITE 1 CC4 2 ARG B 70 GLU B 100
SITE 1 CC5 3 LEU B 31 GLY B 32 LYS B 247
SITE 1 CC6 8 SER B 12 VAL B 19 PHE B 43 HIS B 46
SITE 2 CC6 8 THR B 47 VAL B 231 ASP B 235 MG B 403
CRYST1 92.749 115.221 169.554 90.00 90.00 90.00 I 2 2 2 16
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 0.010782 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008679 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
