HEADER TRANSFERASE/TRANSFERASE INHIBITOR 20-DEC-10 3Q2J
TITLE CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE IIIA
TITLE 2 PROTEIN KINASE INHIBITOR CKI-7 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOGLYCOSIDE 3'-PHOSPHOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: APH(3')III, KANAMYCIN KINASE, TYPE III, NEOMYCIN-KANAMYCIN
COMPND 5 PHOSPHOTRANSFERASE TYPE III;
COMPND 6 EC: 2.7.1.95;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS FAECALIS;
SOURCE 4 ORGANISM_TAXID: 1351;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBR322
KEYWDS SER/THR/TYR PROTEIN KINASE, KINASE, PHOSPHORYLATION, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.FONG,B.XIONG,J.HWANG,A.M.BERGHUIS
REVDAT 4 13-SEP-23 3Q2J 1 REMARK LINK
REVDAT 3 17-JUL-19 3Q2J 1 REMARK
REVDAT 2 19-JUN-13 3Q2J 1 JRNL VERSN
REVDAT 1 18-MAY-11 3Q2J 0
JRNL AUTH D.H.FONG,B.XIONG,J.HWANG,A.M.BERGHUIS
JRNL TITL CRYSTAL STRUCTURES OF TWO AMINOGLYCOSIDE KINASES BOUND WITH
JRNL TITL 2 A EUKARYOTIC PROTEIN KINASE INHIBITOR.
JRNL REF PLOS ONE V. 6 19589 2011
JRNL REFN ESSN 1932-6203
JRNL PMID 21573013
JRNL DOI 10.1371/JOURNAL.PONE.0019589
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 31372
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.620
REMARK 3 FREE R VALUE TEST SET COUNT : 3018
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.5977 - 4.6309 0.99 3226 317 0.1957 0.2271
REMARK 3 2 4.6309 - 3.6762 1.00 3080 330 0.1558 0.1871
REMARK 3 3 3.6762 - 3.2116 1.00 3044 316 0.1798 0.2252
REMARK 3 4 3.2116 - 2.9180 0.99 2996 311 0.1919 0.2442
REMARK 3 5 2.9180 - 2.7089 0.98 2941 354 0.2028 0.2629
REMARK 3 6 2.7089 - 2.5492 0.98 2892 354 0.2123 0.2762
REMARK 3 7 2.5492 - 2.4215 0.96 2934 251 0.2121 0.2608
REMARK 3 8 2.4215 - 2.3161 0.91 2748 288 0.2071 0.2810
REMARK 3 9 2.3161 - 2.2270 0.82 2414 272 0.2085 0.2629
REMARK 3 10 2.2270 - 2.1501 0.70 2079 225 0.2173 0.2705
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 41.65
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.040
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41930
REMARK 3 B22 (A**2) : -1.47440
REMARK 3 B33 (A**2) : 1.05510
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4462
REMARK 3 ANGLE : 1.081 6022
REMARK 3 CHIRALITY : 0.075 628
REMARK 3 PLANARITY : 0.004 776
REMARK 3 DIHEDRAL : 14.269 1710
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3Q2J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063112.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32199
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
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 (%) : 75.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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 1J7L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3000, TRIS PH O8.0, 0.2M
REMARK 280 CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K,
REMARK 280 PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.91850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.57500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.92600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.57500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.91850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.92600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 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 LYS A 3
REMARK 465 MET B 1
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 12 CD CE NZ
REMARK 480 GLU A 103 CD OE1 OE2
REMARK 480 ASP A 104 CB CG OD1 OD2
REMARK 480 GLN A 106 CB CG CD OE1 NE2
REMARK 480 SER A 107 CB OG
REMARK 480 GLU A 109 CD OE1 OE2
REMARK 480 LYS A 110 CG CD CE NZ
REMARK 480 ILE A 111 CD1
REMARK 480 GLU A 161 CD OE1 OE2
REMARK 480 ASP A 162 CG OD1 OD2
REMARK 480 THR A 163 OG1 CG2
REMARK 480 GLU A 183 CD OE1 OE2
REMARK 480 LYS A 202 CD CE NZ
REMARK 480 GLU A 234 CD OE1 OE2
REMARK 480 LYS B 3 NZ
REMARK 480 ASP B 22 CG OD1 OD2
REMARK 480 THR B 23 CB OG1 CG2
REMARK 480 LYS B 30 NZ
REMARK 480 LYS B 75 CD CE NZ
REMARK 480 TYR B 102 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 GLU B 103 CB CG CD OE1 OE2
REMARK 480 ASP B 104 CB CG OD1 OD2
REMARK 480 GLU B 105 CB CG CD OE1 OE2
REMARK 480 GLN B 106 CA CB CG CD OE1 NE2
REMARK 480 ASP B 162 CB CG OD1 OD2
REMARK 480 THR B 163 CB OG1 CG2
REMARK 480 LYS B 166 CB CG CD CE NZ
REMARK 480 LYS B 248 CG CD CE 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 O HOH B 316 O HOH B 331 1.83
REMARK 500 OG SER A 48 O HOH A 267 1.87
REMARK 500 OE1 GLU B 113 O HOH B 381 2.00
REMARK 500 O HOH B 361 O HOH B 382 2.02
REMARK 500 O HOH B 276 O HOH B 380 2.03
REMARK 500 NH1 ARG B 211 O HOH B 330 2.12
REMARK 500 OD2 ASP B 129 O HOH B 370 2.16
REMARK 500 O HOH B 368 O HOH B 372 2.16
REMARK 500 OE1 GLU A 181 O HOH A 381 2.18
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 O HOH A 385 O HOH B 387 4546 2.17
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 ARG A 5 -41.86 81.82
REMARK 500 THR A 23 24.05 -74.72
REMARK 500 GLN A 106 22.03 -76.91
REMARK 500 ASN A 134 48.80 -98.85
REMARK 500 ASP A 155 -153.62 -164.87
REMARK 500 ASP A 190 54.55 -153.55
REMARK 500 ASN A 195 13.96 -140.03
REMARK 500 ASP A 208 60.68 61.46
REMARK 500 ASP A 231 -101.37 -80.47
REMARK 500 ILE A 232 142.40 -37.74
REMARK 500 ARG B 5 -34.46 75.84
REMARK 500 SER B 107 68.70 -108.05
REMARK 500 ASP B 155 -151.41 -161.54
REMARK 500 ASP B 190 49.16 -151.70
REMARK 500 ASP B 200 39.15 81.62
REMARK 500 ASP B 208 64.90 62.47
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 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 153 O
REMARK 620 2 ASP A 155 OD2 88.1
REMARK 620 3 ASP A 155 OD1 81.3 46.2
REMARK 620 4 GLU A 157 OE2 176.7 93.7 102.0
REMARK 620 5 GLU A 262 O 94.4 156.9 156.8 82.9
REMARK 620 6 HOH A 352 O 101.3 117.4 74.0 80.4 84.7
REMARK 620 7 HOH A 357 O 82.3 78.5 122.4 95.3 79.0 163.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 153 O
REMARK 620 2 ASP B 155 OD1 89.2
REMARK 620 3 ASP B 155 OD2 88.8 46.6
REMARK 620 4 GLU B 157 OE2 173.3 85.8 84.5
REMARK 620 5 GLU B 262 O 100.3 164.6 144.6 85.6
REMARK 620 6 HOH B 360 O 87.9 84.0 130.5 96.1 84.3
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 CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CKI A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CKI B 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J7L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA ADP COMPLEX
REMARK 900 RELATED ID: 1J7I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA APOENZYME
REMARK 900 RELATED ID: 1J7U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA AMPPNP COMPLEX
REMARK 900 RELATED ID: 1L8T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA ADP KANAMYCIN A COMPLEX
REMARK 900 RELATED ID: 2B0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA ADP NEOMYCIN B COMPLEX
REMARK 900 RELATED ID: 3H8P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3',5"-AMINOGLYCOSIDE PHOSPHOTRANSFERASE TYPE
REMARK 900 IIIA AMPPNP BUTIROSIN A COMPLEX
DBREF 3Q2J A 1 264 UNP P0A3Y5 KKA3_ENTFA 1 264
DBREF 3Q2J B 1 264 UNP P0A3Y5 KKA3_ENTFA 1 264
SEQRES 1 A 264 MET ALA LYS MET ARG ILE SER PRO GLU LEU LYS LYS LEU
SEQRES 2 A 264 ILE GLU LYS TYR ARG CYS VAL LYS ASP THR GLU GLY MET
SEQRES 3 A 264 SER PRO ALA LYS VAL TYR LYS LEU VAL GLY GLU ASN GLU
SEQRES 4 A 264 ASN LEU TYR LEU LYS MET THR ASP SER ARG TYR LYS GLY
SEQRES 5 A 264 THR THR TYR ASP VAL GLU ARG GLU LYS ASP MET MET LEU
SEQRES 6 A 264 TRP LEU GLU GLY LYS LEU PRO VAL PRO LYS VAL LEU HIS
SEQRES 7 A 264 PHE GLU ARG HIS ASP GLY TRP SER ASN LEU LEU MET SER
SEQRES 8 A 264 GLU ALA ASP GLY VAL LEU CYS SER GLU GLU TYR GLU ASP
SEQRES 9 A 264 GLU GLN SER PRO GLU LYS ILE ILE GLU LEU TYR ALA GLU
SEQRES 10 A 264 CYS ILE ARG LEU PHE HIS SER ILE ASP ILE SER ASP CYS
SEQRES 11 A 264 PRO TYR THR ASN SER LEU ASP SER ARG LEU ALA GLU LEU
SEQRES 12 A 264 ASP TYR LEU LEU ASN ASN ASP LEU ALA ASP VAL ASP CYS
SEQRES 13 A 264 GLU ASN TRP GLU GLU ASP THR PRO PHE LYS ASP PRO ARG
SEQRES 14 A 264 GLU LEU TYR ASP PHE LEU LYS THR GLU LYS PRO GLU GLU
SEQRES 15 A 264 GLU LEU VAL PHE SER HIS GLY ASP LEU GLY ASP SER ASN
SEQRES 16 A 264 ILE PHE VAL LYS ASP GLY LYS VAL SER GLY PHE ILE ASP
SEQRES 17 A 264 LEU GLY ARG SER GLY ARG ALA ASP LYS TRP TYR ASP ILE
SEQRES 18 A 264 ALA PHE CYS VAL ARG SER ILE ARG GLU ASP ILE GLY GLU
SEQRES 19 A 264 GLU GLN TYR VAL GLU LEU PHE PHE ASP LEU LEU GLY ILE
SEQRES 20 A 264 LYS PRO ASP TRP GLU LYS ILE LYS TYR TYR ILE LEU LEU
SEQRES 21 A 264 ASP GLU LEU PHE
SEQRES 1 B 264 MET ALA LYS MET ARG ILE SER PRO GLU LEU LYS LYS LEU
SEQRES 2 B 264 ILE GLU LYS TYR ARG CYS VAL LYS ASP THR GLU GLY MET
SEQRES 3 B 264 SER PRO ALA LYS VAL TYR LYS LEU VAL GLY GLU ASN GLU
SEQRES 4 B 264 ASN LEU TYR LEU LYS MET THR ASP SER ARG TYR LYS GLY
SEQRES 5 B 264 THR THR TYR ASP VAL GLU ARG GLU LYS ASP MET MET LEU
SEQRES 6 B 264 TRP LEU GLU GLY LYS LEU PRO VAL PRO LYS VAL LEU HIS
SEQRES 7 B 264 PHE GLU ARG HIS ASP GLY TRP SER ASN LEU LEU MET SER
SEQRES 8 B 264 GLU ALA ASP GLY VAL LEU CYS SER GLU GLU TYR GLU ASP
SEQRES 9 B 264 GLU GLN SER PRO GLU LYS ILE ILE GLU LEU TYR ALA GLU
SEQRES 10 B 264 CYS ILE ARG LEU PHE HIS SER ILE ASP ILE SER ASP CYS
SEQRES 11 B 264 PRO TYR THR ASN SER LEU ASP SER ARG LEU ALA GLU LEU
SEQRES 12 B 264 ASP TYR LEU LEU ASN ASN ASP LEU ALA ASP VAL ASP CYS
SEQRES 13 B 264 GLU ASN TRP GLU GLU ASP THR PRO PHE LYS ASP PRO ARG
SEQRES 14 B 264 GLU LEU TYR ASP PHE LEU LYS THR GLU LYS PRO GLU GLU
SEQRES 15 B 264 GLU LEU VAL PHE SER HIS GLY ASP LEU GLY ASP SER ASN
SEQRES 16 B 264 ILE PHE VAL LYS ASP GLY LYS VAL SER GLY PHE ILE ASP
SEQRES 17 B 264 LEU GLY ARG SER GLY ARG ALA ASP LYS TRP TYR ASP ILE
SEQRES 18 B 264 ALA PHE CYS VAL ARG SER ILE ARG GLU ASP ILE GLY GLU
SEQRES 19 B 264 GLU GLN TYR VAL GLU LEU PHE PHE ASP LEU LEU GLY ILE
SEQRES 20 B 264 LYS PRO ASP TRP GLU LYS ILE LYS TYR TYR ILE LEU LEU
SEQRES 21 B 264 ASP GLU LEU PHE
HET CA A 301 1
HET CKI A 300 18
HET CA B 301 1
HET CKI B 300 18
HETNAM CA CALCIUM ION
HETNAM CKI N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 CKI 2(C11 H12 CL N3 O2 S)
FORMUL 7 HOH *281(H2 O)
HELIX 1 1 SER A 7 GLU A 15 1 9
HELIX 2 2 ASP A 47 LYS A 51 5 5
HELIX 3 3 ASP A 56 GLU A 68 1 13
HELIX 4 4 CYS A 98 TYR A 102 1 5
HELIX 5 5 SER A 107 SER A 124 1 18
HELIX 6 6 SER A 135 ASN A 149 1 15
HELIX 7 7 ASP A 155 GLU A 160 1 6
HELIX 8 8 ASP A 167 GLU A 178 1 12
HELIX 9 9 LYS A 217 ASP A 231 1 15
HELIX 10 10 GLU A 235 GLY A 246 1 12
HELIX 11 11 ASP A 250 GLU A 262 1 13
HELIX 12 12 SER B 7 ILE B 14 1 8
HELIX 13 13 ASP B 47 LYS B 51 5 5
HELIX 14 14 ASP B 56 GLU B 68 1 13
HELIX 15 15 CYS B 98 TYR B 102 1 5
HELIX 16 16 SER B 107 ILE B 125 1 19
HELIX 17 17 SER B 135 ASN B 149 1 15
HELIX 18 18 ASP B 155 GLU B 160 1 6
HELIX 19 19 ASP B 167 GLU B 178 1 12
HELIX 20 20 LYS B 217 ILE B 232 1 16
HELIX 21 21 GLU B 235 GLY B 246 1 12
HELIX 22 22 ASP B 250 GLU B 262 1 13
SHEET 1 A 5 ARG A 18 LYS A 21 0
SHEET 2 A 5 LYS A 30 VAL A 35 -1 O LYS A 33 N VAL A 20
SHEET 3 A 5 ASN A 40 THR A 46 -1 O LEU A 43 N TYR A 32
SHEET 4 A 5 TRP A 85 SER A 91 -1 O MET A 90 N TYR A 42
SHEET 5 A 5 VAL A 76 HIS A 82 -1 N GLU A 80 O ASN A 87
SHEET 1 B 3 VAL A 96 LEU A 97 0
SHEET 2 B 3 ILE A 196 LYS A 199 -1 O VAL A 198 N VAL A 96
SHEET 3 B 3 LYS A 202 PHE A 206 -1 O SER A 204 N PHE A 197
SHEET 1 C 2 LEU A 184 SER A 187 0
SHEET 2 C 2 GLY A 213 ASP A 216 -1 O GLY A 213 N SER A 187
SHEET 1 D 5 ARG B 18 LYS B 21 0
SHEET 2 D 5 LYS B 30 VAL B 35 -1 O VAL B 35 N ARG B 18
SHEET 3 D 5 ASN B 40 THR B 46 -1 O MET B 45 N LYS B 30
SHEET 4 D 5 TRP B 85 SER B 91 -1 O LEU B 88 N LYS B 44
SHEET 5 D 5 VAL B 76 HIS B 82 -1 N HIS B 78 O LEU B 89
SHEET 1 E 3 VAL B 96 LEU B 97 0
SHEET 2 E 3 ILE B 196 VAL B 198 -1 O VAL B 198 N VAL B 96
SHEET 3 E 3 VAL B 203 PHE B 206 -1 O SER B 204 N PHE B 197
SHEET 1 F 2 LEU B 184 SER B 187 0
SHEET 2 F 2 GLY B 213 ASP B 216 -1 O GLY B 213 N SER B 187
SSBOND 1 CYS A 19 CYS B 156 1555 1555 2.04
SSBOND 2 CYS A 156 CYS B 19 1555 1555 2.04
LINK O ASP A 153 CA CA A 301 1555 1555 2.60
LINK OD2 ASP A 155 CA CA A 301 1555 1555 2.75
LINK OD1 ASP A 155 CA CA A 301 1555 1555 2.87
LINK OE2 GLU A 157 CA CA A 301 1555 1555 2.58
LINK O GLU A 262 CA CA A 301 1555 1555 2.46
LINK CA CA A 301 O HOH A 352 1555 1555 2.21
LINK CA CA A 301 O HOH A 357 1555 1555 2.48
LINK O ASP B 153 CA CA B 301 1555 1555 2.57
LINK OD1 ASP B 155 CA CA B 301 1555 1555 2.64
LINK OD2 ASP B 155 CA CA B 301 1555 1555 2.91
LINK OE2 GLU B 157 CA CA B 301 1555 1555 2.57
LINK O GLU B 262 CA CA B 301 1555 1555 2.55
LINK CA CA B 301 O HOH B 360 1555 1555 2.64
CISPEP 1 SER A 27 PRO A 28 0 8.91
CISPEP 2 SER B 27 PRO B 28 0 7.41
SITE 1 AC1 6 ASP A 153 ASP A 155 GLU A 157 GLU A 262
SITE 2 AC1 6 HOH A 352 HOH A 357
SITE 1 AC2 11 VAL A 31 TYR A 42 MET A 90 SER A 91
SITE 2 AC2 11 GLU A 92 ALA A 93 LEU A 97 SER A 194
SITE 3 AC2 11 PHE A 197 ILE A 207 HOH A 410
SITE 1 AC3 5 ASP B 153 ASP B 155 GLU B 157 GLU B 262
SITE 2 AC3 5 HOH B 360
SITE 1 AC4 7 TYR B 42 SER B 91 ALA B 93 LEU B 97
SITE 2 AC4 7 SER B 194 PHE B 197 HOH B 364
CRYST1 49.837 91.852 131.150 90.00 90.00 90.00 P 21 21 21 8
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 0.020065 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007625 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
