HEADER TRANSFERASE 07-JUN-10 3NDP
TITLE CRYSTAL STRUCTURE OF HUMAN AK4(L171P)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE KINASE ISOENZYME 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADENYLATE KINASE 3-LIKE, ATP-AMP TRANSPHOSPHORYLASE;
COMPND 5 EC: 2.7.4.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AK4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PARALLEL BETA-SHEET, ALPHA-HELICES, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.LIU,Y.WANG,Z.WEI,W.GONG
REVDAT 4 03-APR-24 3NDP 1 REMARK
REVDAT 3 20-MAR-24 3NDP 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3NDP 1 REMARK
REVDAT 1 23-JUN-10 3NDP 0
JRNL AUTH R.LIU,H.XU,Z.WEI,Y.WANG,Y.LIN,W.GONG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ADENYLATE KINASE 4 (L171P)
JRNL TITL 2 SUGGESTS THE ROLE OF HINGE REGION IN PROTEIN DOMAIN MOTION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 379 92 2009
JRNL REFN ISSN 0006-291X
JRNL PMID 19073142
JRNL DOI 10.1016/J.BBRC.2008.12.012
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2710518.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 20311
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) : 0.226
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1037
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3090
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3290
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74000
REMARK 3 B22 (A**2) : 0.74000
REMARK 3 B33 (A**2) : -1.48000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.230 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.030 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.780 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 35.87
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-05
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 : BSRF
REMARK 200 BEAMLINE : 3W1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20375
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.46500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: SOLVED MODEL BY SAD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.22-1.28M (NH4)2SO4, 0.1M TRISHCL, PH
REMARK 280 8.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 72.32000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.89500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.89500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.16000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.89500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.89500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 108.48000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.89500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.16000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.89500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.89500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 108.48000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.32000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 77.79000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 77.79000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 72.32000
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 ALA A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 ASP A 162
REMARK 465 LYS A 163
REMARK 465 PRO A 164
REMARK 465 GLU A 165
REMARK 465 ALA A 166
REMARK 465 VAL A 167
REMARK 465 ALA A 168
REMARK 465 ALA A 169
REMARK 465 ARG A 170
REMARK 465 PRO A 171
REMARK 465 ARG A 172
REMARK 465 GLN A 173
REMARK 465 TYR A 174
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 PRO B 115
REMARK 465 PHE B 116
REMARK 465 GLU B 117
REMARK 465 THR B 118
REMARK 465 LEU B 119
REMARK 465 LYS B 120
REMARK 465 ASP B 121
REMARK 465 LYS B 163
REMARK 465 PRO B 164
REMARK 465 GLU B 165
REMARK 465 ALA B 166
REMARK 465 VAL B 167
REMARK 465 ALA B 168
REMARK 465 ALA B 169
REMARK 465 ARG B 170
REMARK 465 PRO B 171
REMARK 465 ARG B 172
REMARK 465 GLN B 173
REMARK 465 TYR B 174
REMARK 465 LYS B 175
REMARK 465 ASP B 176
REMARK 465 VAL B 177
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 60 CG CD CE NZ
REMARK 470 VAL A 68 CG1 CG2
REMARK 470 ARG A 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 HIS A 228 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 45 CG CD CE NZ
REMARK 470 SER B 47 OG
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ILE B 58 CG1 CG2 CD1
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 162 CG OD1 OD2
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 THR B 197 OG1 CG2
REMARK 470 GLU B 198 CG CD OE1 OE2
REMARK 470 LYS B 201 CG CD CE NZ
REMARK 470 HIS B 228 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 230 CG ND1 CD2 CE1 NE2
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 ARG A 122 75.79 27.99
REMARK 500 PHE A 140 -15.25 -146.28
REMARK 500 ASN A 141 62.83 -152.66
REMARK 500 PHE B 140 -17.89 -144.47
REMARK 500 ASN B 141 62.49 -150.44
REMARK 500 THR B 197 -65.79 -96.27
REMARK 500 HIS B 228 45.29 -97.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1504
DBREF 3NDP A 1 223 UNP P27144 KAD4_HUMAN 1 223
DBREF 3NDP B 1 223 UNP P27144 KAD4_HUMAN 1 223
SEQADV 3NDP PRO A 171 UNP P27144 LEU 171 ENGINEERED MUTATION
SEQADV 3NDP LEU A 224 UNP P27144 EXPRESSION TAG
SEQADV 3NDP GLU A 225 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 226 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 227 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 228 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 229 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 230 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS A 231 UNP P27144 EXPRESSION TAG
SEQADV 3NDP PRO B 171 UNP P27144 LEU 171 ENGINEERED MUTATION
SEQADV 3NDP LEU B 224 UNP P27144 EXPRESSION TAG
SEQADV 3NDP GLU B 225 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 226 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 227 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 228 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 229 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 230 UNP P27144 EXPRESSION TAG
SEQADV 3NDP HIS B 231 UNP P27144 EXPRESSION TAG
SEQRES 1 A 231 MET ALA SER LYS LEU LEU ARG ALA VAL ILE LEU GLY PRO
SEQRES 2 A 231 PRO GLY SER GLY LYS GLY THR VAL CYS GLN ARG ILE ALA
SEQRES 3 A 231 GLN ASN PHE GLY LEU GLN HIS LEU SER SER GLY HIS PHE
SEQRES 4 A 231 LEU ARG GLU ASN ILE LYS ALA SER THR GLU VAL GLY GLU
SEQRES 5 A 231 MET ALA LYS GLN TYR ILE GLU LYS SER LEU LEU VAL PRO
SEQRES 6 A 231 ASP HIS VAL ILE THR ARG LEU MET MET SER GLU LEU GLU
SEQRES 7 A 231 ASN ARG ARG GLY GLN HIS TRP LEU LEU ASP GLY PHE PRO
SEQRES 8 A 231 ARG THR LEU GLY GLN ALA GLU ALA LEU ASP LYS ILE CYS
SEQRES 9 A 231 GLU VAL ASP LEU VAL ILE SER LEU ASN ILE PRO PHE GLU
SEQRES 10 A 231 THR LEU LYS ASP ARG LEU SER ARG ARG TRP ILE HIS PRO
SEQRES 11 A 231 PRO SER GLY ARG VAL TYR ASN LEU ASP PHE ASN PRO PRO
SEQRES 12 A 231 HIS VAL HIS GLY ILE ASP ASP VAL THR GLY GLU PRO LEU
SEQRES 13 A 231 VAL GLN GLN GLU ASP ASP LYS PRO GLU ALA VAL ALA ALA
SEQRES 14 A 231 ARG PRO ARG GLN TYR LYS ASP VAL ALA LYS PRO VAL ILE
SEQRES 15 A 231 GLU LEU TYR LYS SER ARG GLY VAL LEU HIS GLN PHE SER
SEQRES 16 A 231 GLY THR GLU THR ASN LYS ILE TRP PRO TYR VAL TYR THR
SEQRES 17 A 231 LEU PHE SER ASN LYS ILE THR PRO ILE GLN SER LYS GLU
SEQRES 18 A 231 ALA TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 231 MET ALA SER LYS LEU LEU ARG ALA VAL ILE LEU GLY PRO
SEQRES 2 B 231 PRO GLY SER GLY LYS GLY THR VAL CYS GLN ARG ILE ALA
SEQRES 3 B 231 GLN ASN PHE GLY LEU GLN HIS LEU SER SER GLY HIS PHE
SEQRES 4 B 231 LEU ARG GLU ASN ILE LYS ALA SER THR GLU VAL GLY GLU
SEQRES 5 B 231 MET ALA LYS GLN TYR ILE GLU LYS SER LEU LEU VAL PRO
SEQRES 6 B 231 ASP HIS VAL ILE THR ARG LEU MET MET SER GLU LEU GLU
SEQRES 7 B 231 ASN ARG ARG GLY GLN HIS TRP LEU LEU ASP GLY PHE PRO
SEQRES 8 B 231 ARG THR LEU GLY GLN ALA GLU ALA LEU ASP LYS ILE CYS
SEQRES 9 B 231 GLU VAL ASP LEU VAL ILE SER LEU ASN ILE PRO PHE GLU
SEQRES 10 B 231 THR LEU LYS ASP ARG LEU SER ARG ARG TRP ILE HIS PRO
SEQRES 11 B 231 PRO SER GLY ARG VAL TYR ASN LEU ASP PHE ASN PRO PRO
SEQRES 12 B 231 HIS VAL HIS GLY ILE ASP ASP VAL THR GLY GLU PRO LEU
SEQRES 13 B 231 VAL GLN GLN GLU ASP ASP LYS PRO GLU ALA VAL ALA ALA
SEQRES 14 B 231 ARG PRO ARG GLN TYR LYS ASP VAL ALA LYS PRO VAL ILE
SEQRES 15 B 231 GLU LEU TYR LYS SER ARG GLY VAL LEU HIS GLN PHE SER
SEQRES 16 B 231 GLY THR GLU THR ASN LYS ILE TRP PRO TYR VAL TYR THR
SEQRES 17 B 231 LEU PHE SER ASN LYS ILE THR PRO ILE GLN SER LYS GLU
SEQRES 18 B 231 ALA TYR LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 B1501 5
HET SO4 B1502 5
HET SO4 B1503 5
HET SO4 B1504 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 11 HOH *282(H2 O)
HELIX 1 1 GLY A 17 GLY A 30 1 14
HELIX 2 2 SER A 35 SER A 47 1 13
HELIX 3 3 THR A 48 LYS A 60 1 13
HELIX 4 4 PRO A 65 ASN A 79 1 15
HELIX 5 5 THR A 93 LYS A 102 1 10
HELIX 6 6 PRO A 115 LYS A 120 1 6
HELIX 7 7 ALA A 178 ARG A 188 1 11
HELIX 8 8 GLU A 198 ASN A 212 1 15
HELIX 9 9 PRO A 216 LYS A 220 5 5
HELIX 10 10 GLY B 17 GLY B 30 1 14
HELIX 11 11 SER B 35 ALA B 46 1 12
HELIX 12 12 THR B 48 LYS B 60 1 13
HELIX 13 13 PRO B 65 ASN B 79 1 15
HELIX 14 14 THR B 93 LYS B 102 1 10
HELIX 15 15 ALA B 178 ARG B 188 1 11
HELIX 16 16 GLU B 198 ASN B 212 1 15
HELIX 17 17 PRO B 216 LYS B 220 5 5
SHEET 1 A 5 HIS A 33 LEU A 34 0
SHEET 2 A 5 TRP A 85 ASP A 88 1 O ASP A 88 N LEU A 34
SHEET 3 A 5 ARG A 7 LEU A 11 1 N ALA A 8 O LEU A 87
SHEET 4 A 5 LEU A 108 SER A 111 1 O ILE A 110 N VAL A 9
SHEET 5 A 5 LEU A 191 GLN A 193 1 O HIS A 192 N VAL A 109
SHEET 1 B 3 VAL A 135 ASN A 137 0
SHEET 2 B 3 LEU A 123 ILE A 128 -1 N TRP A 127 O TYR A 136
SHEET 3 B 3 VAL A 157 GLU A 160 -1 O GLN A 159 N ARG A 126
SHEET 1 C 5 HIS B 33 LEU B 34 0
SHEET 2 C 5 TRP B 85 ASP B 88 1 O ASP B 88 N LEU B 34
SHEET 3 C 5 ARG B 7 LEU B 11 1 N ALA B 8 O LEU B 87
SHEET 4 C 5 LEU B 108 ASN B 113 1 O ILE B 110 N VAL B 9
SHEET 5 C 5 LEU B 191 SER B 195 1 O PHE B 194 N SER B 111
SHEET 1 D 3 VAL B 135 ASN B 137 0
SHEET 2 D 3 LEU B 123 ILE B 128 -1 N TRP B 127 O TYR B 136
SHEET 3 D 3 VAL B 157 GLU B 160 -1 O GLN B 159 N ARG B 126
CISPEP 1 PHE A 90 PRO A 91 0 0.50
CISPEP 2 PHE B 90 PRO B 91 0 0.85
SITE 1 AC1 13 PRO A 13 PRO A 14 GLY A 15 SER A 16
SITE 2 AC1 13 GLY A 17 LYS A 18 GLY A 19 GLN A 158
SITE 3 AC1 13 HOH A 241 HOH A 263 HOH A 284 HOH A 286
SITE 4 AC1 13 HOH A 381
SITE 1 AC2 6 ARG A 7 ILE A 103 CYS A 104 GLU A 105
SITE 2 AC2 6 HOH A 348 HOH A 369
SITE 1 AC3 4 LYS A 220 GLU A 221 ALA A 222 HOH A 257
SITE 1 AC4 2 THR A 48 GLU A 49
SITE 1 AC5 13 PRO B 13 PRO B 14 GLY B 15 SER B 16
SITE 2 AC5 13 GLY B 17 LYS B 18 GLY B 19 GLN B 158
SITE 3 AC5 13 HOH B 243 HOH B 246 HOH B 251 HOH B 258
SITE 4 AC5 13 HOH B 314
SITE 1 AC6 4 ARG B 7 CYS B 104 GLU B 105 HOH B 272
SITE 1 AC7 5 LYS B 220 GLU B 221 ALA B 222 HOH B 237
SITE 2 AC7 5 HOH B 293
SITE 1 AC8 2 THR B 48 GLU B 49
CRYST1 77.790 77.790 144.640 90.00 90.00 90.00 P 41 21 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 0.012855 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
