HEADER TRANSFERASE 22-JUN-05 2A2C
TITLE X-RAY STRUCTURE OF HUMAN N-ACETYL GALACTOSAMINE KINASE COMPLEXED WITH
TITLE 2 MG-ADP AND N-ACETYL GALACTOSAMINE 1-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLGALACTOSAMINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GALNAC KINASE, GALACTOKINASE 2;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: GALK2, GK2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS KINASE, GALACTOKINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.THODEN,H.M.HOLDEN
REVDAT 6 14-FEB-24 2A2C 1 HETSYN
REVDAT 5 29-JUL-20 2A2C 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 13-NOV-19 2A2C 1 KEYWDS SEQADV
REVDAT 3 24-FEB-09 2A2C 1 VERSN
REVDAT 2 04-OCT-05 2A2C 1 JRNL
REVDAT 1 26-JUL-05 2A2C 0
JRNL AUTH J.B.THODEN,H.M.HOLDEN
JRNL TITL THE MOLECULAR ARCHITECTURE OF HUMAN N-ACETYLGALACTOSAMINE
JRNL TITL 2 KINASE.
JRNL REF J.BIOL.CHEM. V. 280 32784 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16006554
JRNL DOI 10.1074/JBC.M505730200
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 59826
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5980
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1680
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 59826
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3433
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 457
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.013 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.370 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH & HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926, 0.97940, 0.96411
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, D*TREK
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59826
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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 (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-3400, MES, NACL, MG-ATP, N-ACETYL
REMARK 280 GALACTOSAMINE, PH 6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 40.06667
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 20.03333
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 30.05000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 10.01667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.08333
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: MONOMERIC
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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER 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 MET A 1
REMARK 465 ILE A 98
REMARK 465 GLN A 99
REMARK 465 ARG A 431
REMARK 465 SER A 432
REMARK 465 ASP A 433
REMARK 465 GLY A 434
REMARK 465 SER A 435
REMARK 465 LEU A 436
REMARK 465 ALA A 437
REMARK 465 PRO A 438
REMARK 465 GLU A 439
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 GLN A 430 CG CD OE1 NE2
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 A 662 O HOH A 713 2655 2.19
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 GLU A 4 CD GLU A 4 OE2 0.071
REMARK 500 GLU A 49 CD GLU A 49 OE2 0.088
REMARK 500 GLU A 64 CD GLU A 64 OE2 0.066
REMARK 500 GLU A 120 CD GLU A 120 OE2 0.067
REMARK 500 GLU A 179 CD GLU A 179 OE2 0.070
REMARK 500 GLU A 206 CD GLU A 206 OE1 -0.068
REMARK 500 GLU A 299 CD GLU A 299 OE2 0.070
REMARK 500 GLU A 309 CD GLU A 309 OE2 0.070
REMARK 500 GLU A 338 CD GLU A 338 OE2 0.073
REMARK 500 GLU A 350 CD GLU A 350 OE2 0.072
REMARK 500 GLU A 354 CD GLU A 354 OE2 0.078
REMARK 500 GLU A 376 CD GLU A 376 OE2 0.075
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 ALA A 2 CB - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 THR A 8 CA - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 52 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 52 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP A 135 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 180 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 181 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 190 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 214 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR A 257 CB - CG - CD2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 257 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 288 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 288 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP A 322 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 PHE A 345 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 373 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 373 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP A 383 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 383 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP A 387 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 398 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 398 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LEU A 453 CB - CA - C ANGL. DEV. = -13.7 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 TYR A 77 52.55 -108.14
REMARK 500 LYS A 102 67.53 38.35
REMARK 500 THR A 103 -28.30 -145.78
REMARK 500 GLU A 185 46.90 -103.59
REMARK 500 SER A 208 77.66 41.83
REMARK 500 ASN A 319 2.95 -68.26
REMARK 500 SER A 378 -166.47 -101.74
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 460 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 147 OG
REMARK 620 2 NG1 A 459 OP1 165.6
REMARK 620 3 ADP A 463 O1B 88.6 98.9
REMARK 620 4 ADP A 463 O2A 82.7 110.8 78.9
REMARK 620 5 HOH A 470 O 76.2 91.1 92.1 157.3
REMARK 620 6 HOH A 471 O 91.7 84.3 164.6 85.9 102.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 462 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 207 O
REMARK 620 2 SER A 208 O 65.8
REMARK 620 3 ARG A 211 NH2 76.6 85.9
REMARK 620 4 HOH A 626 O 97.2 155.5 108.1
REMARK 620 5 HOH A 833 O 164.0 98.2 104.4 97.6
REMARK 620 6 HOH A 871 O 87.7 73.3 157.8 89.2 86.5
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A2C RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN N-ACETYL GALACTOSAMINE KINASE COMPLEXED
REMARK 900 WITH MG-ADP AND N-ACETYL GALACTOSAMINE 1-PHOSPHATE.
DBREF 2A2C A 1 458 UNP Q01415 GALK2_HUMAN 1 458
SEQADV 2A2C MET A -19 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C GLY A -18 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C SER A -17 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C SER A -16 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C HIS A -15 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C HIS A -14 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C HIS A -13 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C HIS A -12 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C HIS A -11 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C HIS A -10 UNP Q01415 EXPRESSION TAG
SEQADV 2A2C SER A -9 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C SER A -8 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C GLU A -7 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C ASN A -6 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C LEU A -5 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C TYR A -4 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C PHE A -3 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C GLN A -2 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C GLY A -1 UNP Q01415 CLONING ARTIFACT
SEQADV 2A2C HIS A 0 UNP Q01415 CLONING ARTIFACT
SEQRES 1 A 478 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 478 ASN LEU TYR PHE GLN GLY HIS MET ALA THR GLU SER PRO
SEQRES 3 A 478 ALA THR ARG ARG VAL GLN VAL ALA GLU HIS PRO ARG LEU
SEQRES 4 A 478 LEU LYS LEU LYS GLU MET PHE ASN SER LYS PHE GLY SER
SEQRES 5 A 478 ILE PRO LYS PHE TYR VAL ARG ALA PRO GLY ARG VAL ASN
SEQRES 6 A 478 ILE ILE GLY GLU HIS ILE ASP TYR CYS GLY TYR SER VAL
SEQRES 7 A 478 LEU PRO MET ALA VAL GLU GLN ASP VAL LEU ILE ALA VAL
SEQRES 8 A 478 GLU PRO VAL LYS THR TYR ALA LEU GLN LEU ALA ASN THR
SEQRES 9 A 478 ASN PRO LEU TYR PRO ASP PHE SER THR SER ALA ASN ASN
SEQRES 10 A 478 ILE GLN ILE ASP LYS THR LYS PRO LEU TRP HIS ASN TYR
SEQRES 11 A 478 PHE LEU CYS GLY LEU LYS GLY ILE GLN GLU HIS PHE GLY
SEQRES 12 A 478 LEU SER ASN LEU THR GLY MET ASN CYS LEU VAL ASP GLY
SEQRES 13 A 478 ASN ILE PRO PRO SER SER GLY LEU SER SER SER SER ALA
SEQRES 14 A 478 LEU VAL CYS CYS ALA GLY LEU VAL THR LEU THR VAL LEU
SEQRES 15 A 478 GLY ARG ASN LEU SER LYS VAL GLU LEU ALA GLU ILE CYS
SEQRES 16 A 478 ALA LYS SER GLU ARG TYR ILE GLY THR GLU GLY GLY GLY
SEQRES 17 A 478 MET ASP GLN SER ILE SER PHE LEU ALA GLU GLU GLY THR
SEQRES 18 A 478 ALA LYS LEU ILE GLU PHE SER PRO LEU ARG ALA THR ASP
SEQRES 19 A 478 VAL LYS LEU PRO SER GLY ALA VAL PHE VAL ILE ALA ASN
SEQRES 20 A 478 SER CYS VAL GLU MET ASN LYS ALA ALA THR SER HIS PHE
SEQRES 21 A 478 ASN ILE ARG VAL MET GLU CYS ARG LEU ALA ALA LYS LEU
SEQRES 22 A 478 LEU ALA LYS TYR LYS SER LEU GLN TRP ASP LYS VAL LEU
SEQRES 23 A 478 ARG LEU GLU GLU VAL GLN ALA LYS LEU GLY ILE SER LEU
SEQRES 24 A 478 GLU GLU MET LEU LEU VAL THR GLU ASP ALA LEU HIS PRO
SEQRES 25 A 478 GLU PRO TYR ASN PRO GLU GLU ILE CYS ARG CYS LEU GLY
SEQRES 26 A 478 ILE SER LEU GLU GLU LEU ARG THR GLN ILE LEU SER PRO
SEQRES 27 A 478 ASN THR GLN ASP VAL LEU ILE PHE LYS LEU TYR GLN ARG
SEQRES 28 A 478 ALA LYS HIS VAL TYR SER GLU ALA ALA ARG VAL LEU GLN
SEQRES 29 A 478 PHE LYS LYS ILE CYS GLU GLU ALA PRO GLU ASN MET VAL
SEQRES 30 A 478 GLN LEU LEU GLY GLU LEU MET ASN GLN SER HIS MET SER
SEQRES 31 A 478 CYS ARG ASP MET TYR GLU CYS SER CYS PRO GLU LEU ASP
SEQRES 32 A 478 GLN LEU VAL ASP ILE CYS ARG LYS PHE GLY ALA GLN GLY
SEQRES 33 A 478 SER ARG LEU THR GLY ALA GLY TRP GLY GLY CYS THR VAL
SEQRES 34 A 478 SER MET VAL PRO ALA ASP LYS LEU PRO SER PHE LEU ALA
SEQRES 35 A 478 ASN VAL HIS LYS ALA TYR TYR GLN ARG SER ASP GLY SER
SEQRES 36 A 478 LEU ALA PRO GLU LYS GLN SER LEU PHE ALA THR LYS PRO
SEQRES 37 A 478 GLY GLY GLY ALA LEU VAL LEU LEU GLU ALA
HET NG1 A 459 19
HET MG A 460 1
HET CL A 461 1
HET NA A 462 1
HET ADP A 463 27
HETNAM NG1 2-ACETAMIDO-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-
HETNAM 2 NG1 GALACTOPYRANOSE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN NG1 N-ACETYL-ALPHA-D-GALACTOSAMINE 1-PHOSPHATE; N-ACETYL-1-
HETSYN 2 NG1 O-PHOSPHONO-ALPHA-D-GALACTOSAMINE; 2-ACETAMIDO-2-
HETSYN 3 NG1 DEOXY-1-O-PHOSPHONO-ALPHA-D-GALACTOSE; 2-ACETAMIDO-2-
HETSYN 4 NG1 DEOXY-1-O-PHOSPHONO-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-
HETSYN 5 NG1 1-O-PHOSPHONO-GALACTOSE
FORMUL 2 NG1 C8 H16 N O9 P
FORMUL 3 MG MG 2+
FORMUL 4 CL CL 1-
FORMUL 5 NA NA 1+
FORMUL 6 ADP C10 H15 N5 O10 P2
FORMUL 7 HOH *457(H2 O)
HELIX 1 1 GLN A 12 GLU A 15 5 4
HELIX 2 2 HIS A 16 GLY A 31 1 16
HELIX 3 3 ILE A 51 GLY A 55 5 5
HELIX 4 4 LEU A 106 PHE A 122 1 17
HELIX 5 5 SER A 145 GLY A 163 1 19
HELIX 6 6 SER A 167 ARG A 180 1 14
HELIX 7 7 TYR A 181 GLY A 183 5 3
HELIX 8 8 GLY A 188 ALA A 197 1 10
HELIX 9 9 ASN A 233 THR A 237 5 5
HELIX 10 10 SER A 238 LYS A 258 1 21
HELIX 11 11 ARG A 267 GLY A 276 1 10
HELIX 12 12 SER A 278 LEU A 290 1 13
HELIX 13 13 ASN A 296 GLY A 305 1 10
HELIX 14 14 SER A 307 ILE A 315 1 9
HELIX 15 15 SER A 317 GLN A 321 5 5
HELIX 16 16 LYS A 327 ALA A 352 1 26
HELIX 17 17 ASN A 355 MET A 374 1 20
HELIX 18 18 CYS A 379 PHE A 392 1 14
HELIX 19 19 LYS A 416 GLN A 430 1 15
SHEET 1 A 7 THR A 8 VAL A 11 0
SHEET 2 A 7 LEU A 453 GLU A 457 1 O VAL A 454 N ARG A 9
SHEET 3 A 7 PHE A 36 ILE A 47 -1 N TYR A 37 O LEU A 455
SHEET 4 A 7 LEU A 59 PRO A 73 -1 O VAL A 71 N PHE A 36
SHEET 5 A 7 MET A 130 GLY A 136 -1 O ASP A 135 N LEU A 68
SHEET 6 A 7 LEU A 79 ASN A 83 1 N ALA A 82 O VAL A 134
SHEET 7 A 7 PHE A 91 THR A 93 -1 O THR A 93 N LEU A 79
SHEET 1 B 2 ALA A 202 GLU A 206 0
SHEET 2 B 2 ARG A 211 VAL A 215 -1 O ARG A 211 N GLU A 206
SHEET 1 C 4 GLY A 396 LEU A 399 0
SHEET 2 C 4 CYS A 407 PRO A 413 -1 O VAL A 409 N ARG A 398
SHEET 3 C 4 ALA A 221 ASN A 227 -1 N VAL A 222 O VAL A 412
SHEET 4 C 4 LEU A 443 THR A 446 -1 O THR A 446 N PHE A 223
LINK OG SER A 147 MG MG A 460 1555 1555 2.39
LINK O PHE A 207 NA NA A 462 1555 1555 2.40
LINK O SER A 208 NA NA A 462 1555 1555 2.86
LINK NH2 ARG A 211 NA NA A 462 1555 1555 2.55
LINK OP1 NG1 A 459 MG MG A 460 1555 1555 2.22
LINK MG MG A 460 O1B ADP A 463 1555 1555 2.28
LINK MG MG A 460 O2A ADP A 463 1555 1555 2.34
LINK MG MG A 460 O HOH A 470 1555 1555 2.33
LINK MG MG A 460 O HOH A 471 1555 1555 2.19
LINK NA NA A 462 O HOH A 626 1555 1555 2.42
LINK NA NA A 462 O HOH A 833 1555 1555 2.40
LINK NA NA A 462 O HOH A 871 1555 1555 2.17
CISPEP 1 SER A 208 PRO A 209 0 0.99
CRYST1 123.800 123.800 60.100 90.00 90.00 120.00 P 65 6
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 0.008078 0.004664 0.000000 0.00000
SCALE2 0.000000 0.009327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016639 0.00000
(ATOM LINES ARE NOT SHOWN.)
END