HEADER TRANSFERASE, HYDROLASE 29-SEP-08 3EPS
TITLE THE CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE
TITLE 2 FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IDH KINASE/PHOSPHATASE, IDHK/P;
COMPND 5 EC: 2.7.11.5, 3.1.3.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: ACEK, ECS4934, Z5602;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS KINASE PHOSPHATASE, ATP-BINDING, GLYOXYLATE BYPASS, KINASE,
KEYWDS 2 NUCLEOTIDE-BINDING, PROTEIN PHOSPHATASE, TRICARBOXYLIC ACID CYCLE,
KEYWDS 3 STRUCTURAL GENOMICS, MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS
KEYWDS 4 INITIATIVE, BSGI, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHENG,Z.JIA,MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS
AUTHOR 2 INITIATIVE (BSGI)
REVDAT 3 21-FEB-24 3EPS 1 REMARK LINK
REVDAT 2 30-JUN-10 3EPS 1 JRNL
REVDAT 1 14-APR-10 3EPS 0
JRNL AUTH J.ZHENG,Z.JIA
JRNL TITL STRUCTURE OF THE BIFUNCTIONAL ISOCITRATE DEHYDROGENASE
JRNL TITL 2 KINASE/PHOSPHATASE.
JRNL REF NATURE V. 465 961 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20505668
JRNL DOI 10.1038/NATURE09088
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 45600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 43301
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9307
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EPS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049623.
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 : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45600
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 86.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 305.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG8000, 0.2M MAGNESIUM CHLORIDE,
REMARK 280 0.1M MES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 133.81750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.29750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.29750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.90875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.29750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.29750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 200.72625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.29750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.29750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 66.90875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.29750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.29750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 200.72625
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 133.81750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 1
REMARK 465 GLU A 497
REMARK 465 ASP A 498
REMARK 465 GLU A 499
REMARK 465 LEU A 500
REMARK 465 ALA A 501
REMARK 465 SER A 502
REMARK 465 GLU A 503
REMARK 465 GLU A 575
REMARK 465 MET A 576
REMARK 465 LEU A 577
REMARK 465 PHE A 578
REMARK 465 SER B 1
REMARK 465 PRO B 492
REMARK 465 PRO B 493
REMARK 465 ARG B 494
REMARK 465 TYR B 495
REMARK 465 PRO B 496
REMARK 465 GLU B 497
REMARK 465 ASP B 498
REMARK 465 GLU B 499
REMARK 465 LEU B 500
REMARK 465 ALA B 501
REMARK 465 SER B 502
REMARK 465 GLU B 503
REMARK 465 PRO B 504
REMARK 465 TRP B 505
REMARK 465 GLU B 575
REMARK 465 MET B 576
REMARK 465 LEU B 577
REMARK 465 PHE B 578
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 OD2 ASP A 475 O1G ATP A 1605 1.99
REMARK 500 OD2 ASP B 475 O1G ATP B 1605 2.08
REMARK 500 NH1 ARG B 272 OG1 THR B 280 2.19
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 PRO A 138 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 LEU A 359 CA - CB - CG ANGL. DEV. = 13.9 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 ALA A 38 28.86 40.24
REMARK 500 THR A 69 -57.43 -159.61
REMARK 500 ASN A 70 -49.33 67.83
REMARK 500 TYR A 93 121.63 -34.62
REMARK 500 PHE A 122 58.57 -68.87
REMARK 500 SER A 125 -45.72 142.87
REMARK 500 SER A 126 -25.35 71.33
REMARK 500 ARG A 130 -70.39 -44.63
REMARK 500 PHE A 132 141.62 -15.34
REMARK 500 ARG A 133 -103.66 -102.05
REMARK 500 ARG A 137 118.70 -160.54
REMARK 500 PRO A 138 -71.80 0.88
REMARK 500 LEU A 139 -13.80 78.73
REMARK 500 HIS A 147 -4.79 -163.70
REMARK 500 TRP A 149 93.76 64.86
REMARK 500 GLU A 150 -34.98 106.32
REMARK 500 SER A 158 39.75 -92.87
REMARK 500 ARG A 163 59.76 -96.55
REMARK 500 ASN A 168 79.00 90.43
REMARK 500 GLU A 187 -75.66 -58.46
REMARK 500 ASN A 204 -131.23 54.28
REMARK 500 ASP A 230 -14.85 -47.24
REMARK 500 THR A 238 170.49 55.64
REMARK 500 LEU A 275 75.36 28.06
REMARK 500 ASN A 309 52.98 -109.07
REMARK 500 ARG A 365 -14.02 -47.56
REMARK 500 VAL A 366 11.37 49.21
REMARK 500 LEU A 404 41.78 -147.93
REMARK 500 PHE A 460 -39.09 -37.11
REMARK 500 GLU A 484 4.58 179.31
REMARK 500 ARG A 494 -66.24 -127.41
REMARK 500 PRO A 515 -16.36 -45.72
REMARK 500 TRP A 521 -66.10 -92.05
REMARK 500 LEU A 522 -6.50 -56.17
REMARK 500 HIS A 536 42.62 -140.36
REMARK 500 ALA A 562 45.96 -78.95
REMARK 500 SER A 570 2.32 -61.25
REMARK 500 ALA B 38 36.97 39.18
REMARK 500 ASN B 49 -70.81 -60.22
REMARK 500 THR B 69 -92.64 -149.02
REMARK 500 ASN B 70 -10.43 54.37
REMARK 500 GLN B 72 20.63 -79.41
REMARK 500 SER B 73 25.81 -72.26
REMARK 500 LEU B 79 6.76 -69.74
REMARK 500 PRO B 91 -18.17 -37.16
REMARK 500 ARG B 120 -21.04 -149.16
REMARK 500 PHE B 122 51.33 -91.80
REMARK 500 SER B 125 124.55 92.23
REMARK 500 GLN B 127 132.03 68.56
REMARK 500 PRO B 128 -169.85 -75.83
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
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 A1606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 462 OD1
REMARK 620 2 ASP A 475 OD1 66.0
REMARK 620 3 ATP A1605 O1A 94.9 66.5
REMARK 620 4 ATP A1605 O2B 128.3 62.3 62.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 462 OD1
REMARK 620 2 ASP B 475 OD1 57.6
REMARK 620 3 ATP B1605 O2B 118.7 66.6
REMARK 620 4 ATP B1605 O1A 73.6 60.5 57.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ACEK_ECO57 RELATED DB: TARGETDB
DBREF 3EPS A 2 578 UNP Q8X607 ACEK_ECO57 2 578
DBREF 3EPS B 2 578 UNP Q8X607 ACEK_ECO57 2 578
SEQADV 3EPS SER A 1 UNP Q8X607 EXPRESSION TAG
SEQADV 3EPS SER B 1 UNP Q8X607 EXPRESSION TAG
SEQRES 1 A 578 SER PRO ARG GLY LEU GLU LEU LEU ILE ALA GLN THR ILE
SEQRES 2 A 578 LEU GLN GLY PHE ASP ALA GLN TYR GLY ARG PHE LEU GLU
SEQRES 3 A 578 VAL THR SER GLY ALA GLN GLN ARG PHE GLU GLN ALA ASP
SEQRES 4 A 578 TRP HIS ALA VAL GLN GLN ALA MET LYS ASN ARG ILE HIS
SEQRES 5 A 578 LEU TYR ASP HIS HIS VAL GLY LEU VAL VAL GLU GLN LEU
SEQRES 6 A 578 ARG CYS ILE THR ASN GLY GLN SER THR ASP ALA GLU PHE
SEQRES 7 A 578 LEU LEU ARG VAL LYS GLU HIS TYR THR ARG LEU LEU PRO
SEQRES 8 A 578 ASP TYR PRO ARG PHE GLU ILE ALA GLU SER PHE PHE ASN
SEQRES 9 A 578 SER VAL TYR CYS ARG LEU PHE ASP HIS ARG SER LEU THR
SEQRES 10 A 578 PRO GLU ARG LEU PHE ILE PHE SER SER GLN PRO GLU ARG
SEQRES 11 A 578 ARG PHE ARG THR ILE PRO ARG PRO LEU ALA LYS ASP PHE
SEQRES 12 A 578 HIS PRO ASP HIS GLY TRP GLU SER LEU LEU MET ARG VAL
SEQRES 13 A 578 ILE SER ASP LEU PRO LEU ARG LEU HIS TRP GLN ASN LYS
SEQRES 14 A 578 SER ARG ASP ILE HIS TYR ILE ILE ARG HIS LEU THR GLU
SEQRES 15 A 578 THR LEU GLY PRO GLU ASN LEU SER LYS SER HIS LEU GLN
SEQRES 16 A 578 VAL ALA ASN GLU LEU PHE TYR ARG ASN LYS ALA ALA TRP
SEQRES 17 A 578 LEU VAL GLY LYS LEU ILE THR PRO SER GLY THR LEU PRO
SEQRES 18 A 578 PHE LEU LEU PRO ILE HIS GLN THR ASP ASP GLY GLU LEU
SEQRES 19 A 578 PHE ILE ASP THR CYS LEU THR THR THR ALA GLU ALA SER
SEQRES 20 A 578 ILE VAL PHE GLY PHE ALA ARG SER TYR PHE MET VAL TYR
SEQRES 21 A 578 ALA PRO LEU PRO ALA ALA LEU VAL GLU TRP LEU ARG GLU
SEQRES 22 A 578 ILE LEU PRO GLY LYS THR THR ALA GLU LEU TYR MET ALA
SEQRES 23 A 578 ILE GLY CYS GLN LYS HIS ALA LYS THR GLU SER TYR ARG
SEQRES 24 A 578 GLU TYR LEU VAL TYR LEU GLN GLY CYS ASN GLU GLN PHE
SEQRES 25 A 578 ILE GLU ALA PRO GLY ILE ARG GLY MET VAL MET LEU VAL
SEQRES 26 A 578 PHE THR LEU PRO GLY PHE ASP ARG VAL PHE LYS VAL ILE
SEQRES 27 A 578 LYS ASP LYS PHE ALA PRO GLN LYS GLU MET SER ALA ALA
SEQRES 28 A 578 HIS VAL ARG ALA CYS TYR GLN LEU VAL LYS GLU HIS ASP
SEQRES 29 A 578 ARG VAL GLY ARG MET ALA ASP THR GLN GLU PHE GLU ASN
SEQRES 30 A 578 PHE VAL LEU GLU LYS ARG HIS ILE SER PRO ALA LEU MET
SEQRES 31 A 578 GLU LEU LEU LEU GLN GLU ALA ALA GLU LYS ILE THR ASP
SEQRES 32 A 578 LEU GLY GLU GLN ILE VAL ILE ARG HIS LEU TYR ILE GLU
SEQRES 33 A 578 ARG ARG MET VAL PRO LEU ASN ILE TRP LEU GLU GLN VAL
SEQRES 34 A 578 GLU GLY GLN GLN LEU ARG ASP ALA ILE GLU GLU TYR GLY
SEQRES 35 A 578 ASN ALA ILE ARG GLN LEU ALA ALA ALA ASN ILE PHE PRO
SEQRES 36 A 578 GLY ASP MET LEU PHE LYS ASN PHE GLY VAL THR ARG HIS
SEQRES 37 A 578 GLY ARG VAL VAL PHE TYR ASP TYR ASP GLU ILE CYS TYR
SEQRES 38 A 578 MET THR GLU VAL ASN PHE ARG ASP ILE PRO PRO PRO ARG
SEQRES 39 A 578 TYR PRO GLU ASP GLU LEU ALA SER GLU PRO TRP TYR SER
SEQRES 40 A 578 VAL SER PRO GLY ASP VAL PHE PRO GLU GLU PHE ARG HIS
SEQRES 41 A 578 TRP LEU CYS ALA ASP PRO ARG ILE GLY PRO LEU PHE GLU
SEQRES 42 A 578 GLU MET HIS ALA ASP LEU PHE ARG ALA ASP TYR TRP ARG
SEQRES 43 A 578 ALA LEU GLN ASN ARG ILE ARG GLU GLY HIS VAL GLU ASP
SEQRES 44 A 578 VAL TYR ALA TYR ARG ARG ARG GLN ARG PHE SER VAL ARG
SEQRES 45 A 578 TYR GLY GLU MET LEU PHE
SEQRES 1 B 578 SER PRO ARG GLY LEU GLU LEU LEU ILE ALA GLN THR ILE
SEQRES 2 B 578 LEU GLN GLY PHE ASP ALA GLN TYR GLY ARG PHE LEU GLU
SEQRES 3 B 578 VAL THR SER GLY ALA GLN GLN ARG PHE GLU GLN ALA ASP
SEQRES 4 B 578 TRP HIS ALA VAL GLN GLN ALA MET LYS ASN ARG ILE HIS
SEQRES 5 B 578 LEU TYR ASP HIS HIS VAL GLY LEU VAL VAL GLU GLN LEU
SEQRES 6 B 578 ARG CYS ILE THR ASN GLY GLN SER THR ASP ALA GLU PHE
SEQRES 7 B 578 LEU LEU ARG VAL LYS GLU HIS TYR THR ARG LEU LEU PRO
SEQRES 8 B 578 ASP TYR PRO ARG PHE GLU ILE ALA GLU SER PHE PHE ASN
SEQRES 9 B 578 SER VAL TYR CYS ARG LEU PHE ASP HIS ARG SER LEU THR
SEQRES 10 B 578 PRO GLU ARG LEU PHE ILE PHE SER SER GLN PRO GLU ARG
SEQRES 11 B 578 ARG PHE ARG THR ILE PRO ARG PRO LEU ALA LYS ASP PHE
SEQRES 12 B 578 HIS PRO ASP HIS GLY TRP GLU SER LEU LEU MET ARG VAL
SEQRES 13 B 578 ILE SER ASP LEU PRO LEU ARG LEU HIS TRP GLN ASN LYS
SEQRES 14 B 578 SER ARG ASP ILE HIS TYR ILE ILE ARG HIS LEU THR GLU
SEQRES 15 B 578 THR LEU GLY PRO GLU ASN LEU SER LYS SER HIS LEU GLN
SEQRES 16 B 578 VAL ALA ASN GLU LEU PHE TYR ARG ASN LYS ALA ALA TRP
SEQRES 17 B 578 LEU VAL GLY LYS LEU ILE THR PRO SER GLY THR LEU PRO
SEQRES 18 B 578 PHE LEU LEU PRO ILE HIS GLN THR ASP ASP GLY GLU LEU
SEQRES 19 B 578 PHE ILE ASP THR CYS LEU THR THR THR ALA GLU ALA SER
SEQRES 20 B 578 ILE VAL PHE GLY PHE ALA ARG SER TYR PHE MET VAL TYR
SEQRES 21 B 578 ALA PRO LEU PRO ALA ALA LEU VAL GLU TRP LEU ARG GLU
SEQRES 22 B 578 ILE LEU PRO GLY LYS THR THR ALA GLU LEU TYR MET ALA
SEQRES 23 B 578 ILE GLY CYS GLN LYS HIS ALA LYS THR GLU SER TYR ARG
SEQRES 24 B 578 GLU TYR LEU VAL TYR LEU GLN GLY CYS ASN GLU GLN PHE
SEQRES 25 B 578 ILE GLU ALA PRO GLY ILE ARG GLY MET VAL MET LEU VAL
SEQRES 26 B 578 PHE THR LEU PRO GLY PHE ASP ARG VAL PHE LYS VAL ILE
SEQRES 27 B 578 LYS ASP LYS PHE ALA PRO GLN LYS GLU MET SER ALA ALA
SEQRES 28 B 578 HIS VAL ARG ALA CYS TYR GLN LEU VAL LYS GLU HIS ASP
SEQRES 29 B 578 ARG VAL GLY ARG MET ALA ASP THR GLN GLU PHE GLU ASN
SEQRES 30 B 578 PHE VAL LEU GLU LYS ARG HIS ILE SER PRO ALA LEU MET
SEQRES 31 B 578 GLU LEU LEU LEU GLN GLU ALA ALA GLU LYS ILE THR ASP
SEQRES 32 B 578 LEU GLY GLU GLN ILE VAL ILE ARG HIS LEU TYR ILE GLU
SEQRES 33 B 578 ARG ARG MET VAL PRO LEU ASN ILE TRP LEU GLU GLN VAL
SEQRES 34 B 578 GLU GLY GLN GLN LEU ARG ASP ALA ILE GLU GLU TYR GLY
SEQRES 35 B 578 ASN ALA ILE ARG GLN LEU ALA ALA ALA ASN ILE PHE PRO
SEQRES 36 B 578 GLY ASP MET LEU PHE LYS ASN PHE GLY VAL THR ARG HIS
SEQRES 37 B 578 GLY ARG VAL VAL PHE TYR ASP TYR ASP GLU ILE CYS TYR
SEQRES 38 B 578 MET THR GLU VAL ASN PHE ARG ASP ILE PRO PRO PRO ARG
SEQRES 39 B 578 TYR PRO GLU ASP GLU LEU ALA SER GLU PRO TRP TYR SER
SEQRES 40 B 578 VAL SER PRO GLY ASP VAL PHE PRO GLU GLU PHE ARG HIS
SEQRES 41 B 578 TRP LEU CYS ALA ASP PRO ARG ILE GLY PRO LEU PHE GLU
SEQRES 42 B 578 GLU MET HIS ALA ASP LEU PHE ARG ALA ASP TYR TRP ARG
SEQRES 43 B 578 ALA LEU GLN ASN ARG ILE ARG GLU GLY HIS VAL GLU ASP
SEQRES 44 B 578 VAL TYR ALA TYR ARG ARG ARG GLN ARG PHE SER VAL ARG
SEQRES 45 B 578 TYR GLY GLU MET LEU PHE
HET AMP A1604 23
HET ATP A1605 31
HET MG A1606 1
HET AMP B1604 23
HET ATP B1605 31
HET MG B1606 1
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 4 ATP 2(C10 H16 N5 O13 P3)
FORMUL 5 MG 2(MG 2+)
FORMUL 9 HOH *50(H2 O)
HELIX 1 1 PRO A 2 SER A 29 1 28
HELIX 2 2 GLY A 30 GLN A 37 1 8
HELIX 3 3 ASP A 39 ILE A 68 1 30
HELIX 4 4 ASP A 75 ARG A 88 1 14
HELIX 5 5 ARG A 95 PHE A 111 1 17
HELIX 6 6 SER A 151 SER A 158 1 8
HELIX 7 7 ASN A 168 GLY A 185 1 18
HELIX 8 8 GLY A 185 SER A 190 1 6
HELIX 9 9 THR A 242 PHE A 250 1 9
HELIX 10 10 LEU A 263 ILE A 274 1 12
HELIX 11 11 THR A 279 GLY A 288 1 10
HELIX 12 12 CYS A 289 GLY A 307 1 19
HELIX 13 13 SER A 349 GLU A 362 1 14
HELIX 14 14 ARG A 383 ILE A 385 5 3
HELIX 15 15 SER A 386 ALA A 397 1 12
HELIX 16 16 LEU A 422 VAL A 429 1 8
HELIX 17 17 GLY A 431 ALA A 451 1 21
HELIX 18 18 LEU A 459 LYS A 461 5 3
HELIX 19 19 ASP A 475 ILE A 479 5 5
HELIX 20 20 GLU A 516 CYS A 523 1 8
HELIX 21 21 ILE A 528 HIS A 536 1 9
HELIX 22 22 ALA A 537 PHE A 540 5 4
HELIX 23 23 ARG A 541 GLU A 554 1 14
HELIX 24 24 ARG A 564 GLN A 567 5 4
HELIX 25 25 ARG A 568 TYR A 573 1 6
HELIX 26 26 PRO B 2 GLY B 30 1 29
HELIX 27 27 GLY B 30 GLN B 37 1 8
HELIX 28 28 ASP B 39 THR B 69 1 31
HELIX 29 29 GLU B 77 LEU B 90 1 14
HELIX 30 30 PRO B 91 TYR B 93 5 3
HELIX 31 31 ARG B 95 PHE B 111 1 17
HELIX 32 32 SER B 151 ILE B 157 1 7
HELIX 33 33 SER B 158 LEU B 160 5 3
HELIX 34 34 ASN B 168 SER B 190 1 23
HELIX 35 35 THR B 242 PHE B 250 1 9
HELIX 36 36 LEU B 263 ARG B 272 1 10
HELIX 37 37 THR B 279 ILE B 287 1 9
HELIX 38 38 CYS B 289 CYS B 308 1 20
HELIX 39 39 SER B 349 GLU B 362 1 14
HELIX 40 40 ARG B 383 ILE B 385 5 3
HELIX 41 41 SER B 386 ALA B 397 1 12
HELIX 42 42 LEU B 422 LEU B 426 1 5
HELIX 43 43 GLU B 427 VAL B 429 5 3
HELIX 44 44 GLY B 431 ALA B 451 1 21
HELIX 45 45 LEU B 459 LYS B 461 5 3
HELIX 46 46 ASP B 475 ILE B 479 5 5
HELIX 47 47 THR B 483 VAL B 485 5 3
HELIX 48 48 PHE B 514 GLU B 517 5 4
HELIX 49 49 PHE B 518 CYS B 523 1 6
HELIX 50 50 ARG B 527 HIS B 536 1 10
HELIX 51 51 ALA B 537 PHE B 540 5 4
HELIX 52 52 ARG B 541 ARG B 553 1 13
HELIX 53 53 ARG B 568 TYR B 573 1 6
SHEET 1 A 6 ALA A 140 PHE A 143 0
SHEET 2 A 6 HIS A 193 ALA A 197 -1 O LEU A 194 N PHE A 143
SHEET 3 A 6 ALA A 206 THR A 215 -1 O VAL A 210 N ALA A 197
SHEET 4 A 6 GLY A 218 GLN A 228 -1 O LEU A 220 N LEU A 213
SHEET 5 A 6 GLU A 233 ILE A 236 -1 O PHE A 235 N HIS A 227
SHEET 6 A 6 HIS A 165 TRP A 166 1 N HIS A 165 O LEU A 234
SHEET 1 B 4 ALA A 140 PHE A 143 0
SHEET 2 B 4 HIS A 193 ALA A 197 -1 O LEU A 194 N PHE A 143
SHEET 3 B 4 ALA A 206 THR A 215 -1 O VAL A 210 N ALA A 197
SHEET 4 B 4 PHE A 201 ARG A 203 -1 N PHE A 201 O TRP A 208
SHEET 1 C 5 ILE A 313 GLU A 314 0
SHEET 2 C 5 MET A 323 THR A 327 -1 O THR A 327 N ILE A 313
SHEET 3 C 5 ARG A 333 ILE A 338 -1 O VAL A 337 N LEU A 324
SHEET 4 C 5 GLN A 407 ARG A 417 -1 O TYR A 414 N LYS A 336
SHEET 5 C 5 GLN A 373 GLU A 381 -1 N ASN A 377 O ARG A 411
SHEET 1 D 5 ILE A 313 GLU A 314 0
SHEET 2 D 5 MET A 323 THR A 327 -1 O THR A 327 N ILE A 313
SHEET 3 D 5 ARG A 333 ILE A 338 -1 O VAL A 337 N LEU A 324
SHEET 4 D 5 GLN A 407 ARG A 417 -1 O TYR A 414 N LYS A 336
SHEET 5 D 5 ILE A 401 LEU A 404 -1 N THR A 402 O VAL A 409
SHEET 1 E 3 VAL A 420 PRO A 421 0
SHEET 2 E 3 PHE A 463 VAL A 465 -1 O VAL A 465 N VAL A 420
SHEET 3 E 3 VAL A 471 PHE A 473 -1 O VAL A 472 N GLY A 464
SHEET 1 F 2 ILE A 453 PHE A 454 0
SHEET 2 F 2 CYS A 480 TYR A 481 -1 O CYS A 480 N PHE A 454
SHEET 1 G 2 ASN A 486 PHE A 487 0
SHEET 2 G 2 ASP A 512 VAL A 513 1 O VAL A 513 N ASN A 486
SHEET 1 H 4 ALA B 140 LYS B 141 0
SHEET 2 H 4 LEU B 194 ALA B 197 -1 O VAL B 196 N LYS B 141
SHEET 3 H 4 VAL B 210 THR B 215 -1 O LYS B 212 N GLN B 195
SHEET 4 H 4 GLY B 218 LEU B 223 -1 O LEU B 220 N LEU B 213
SHEET 1 I 2 PHE B 201 ARG B 203 0
SHEET 2 I 2 ALA B 206 TRP B 208 -1 O TRP B 208 N PHE B 201
SHEET 1 J 2 ILE B 226 GLN B 228 0
SHEET 2 J 2 LEU B 234 ILE B 236 -1 O PHE B 235 N HIS B 227
SHEET 1 K 5 ILE B 313 GLU B 314 0
SHEET 2 K 5 MET B 323 THR B 327 -1 O THR B 327 N ILE B 313
SHEET 3 K 5 ARG B 333 ILE B 338 -1 O VAL B 337 N LEU B 324
SHEET 4 K 5 GLN B 407 ARG B 417 -1 O TYR B 414 N LYS B 336
SHEET 5 K 5 THR B 372 GLU B 381 -1 N GLN B 373 O ILE B 415
SHEET 1 L 5 ILE B 313 GLU B 314 0
SHEET 2 L 5 MET B 323 THR B 327 -1 O THR B 327 N ILE B 313
SHEET 3 L 5 ARG B 333 ILE B 338 -1 O VAL B 337 N LEU B 324
SHEET 4 L 5 GLN B 407 ARG B 417 -1 O TYR B 414 N LYS B 336
SHEET 5 L 5 ILE B 401 ASP B 403 -1 N THR B 402 O VAL B 409
SHEET 1 M 3 VAL B 420 PRO B 421 0
SHEET 2 M 3 PHE B 463 VAL B 465 -1 O VAL B 465 N VAL B 420
SHEET 3 M 3 VAL B 471 PHE B 473 -1 O VAL B 472 N GLY B 464
SHEET 1 N 2 ILE B 453 PHE B 454 0
SHEET 2 N 2 CYS B 480 TYR B 481 -1 O CYS B 480 N PHE B 454
SHEET 1 O 2 ASN B 486 PHE B 487 0
SHEET 2 O 2 ASP B 512 VAL B 513 1 O VAL B 513 N ASN B 486
LINK OD1 ASN A 462 MG MG A1606 1555 1555 2.21
LINK OD1 ASP A 475 MG MG A1606 1555 1555 2.40
LINK O1A ATP A1605 MG MG A1606 1555 1555 2.27
LINK O2B ATP A1605 MG MG A1606 1555 1555 2.36
LINK OD1 ASN B 462 MG MG B1606 1555 1555 2.25
LINK OD1 ASP B 475 MG MG B1606 1555 1555 2.50
LINK O2B ATP B1605 MG MG B1606 1555 1555 2.47
LINK O1A ATP B1605 MG MG B1606 1555 1555 2.49
SITE 1 AC1 10 ASN A 104 SER A 105 HIS A 113 LEU A 116
SITE 2 AC1 10 LYS A 291 LYS A 294 THR A 295 TYR A 298
SITE 3 AC1 10 GLU A 376 ASN A 377
SITE 1 AC2 18 PRO A 316 GLY A 317 ILE A 318 VAL A 322
SITE 2 AC2 18 MET A 323 VAL A 325 LYS A 336 GLU A 416
SITE 3 AC2 18 ARG A 417 ARG A 418 MET A 419 PRO A 421
SITE 4 AC2 18 ASN A 462 TYR A 474 ASP A 475 ASP A 477
SITE 5 AC2 18 GLU A 478 MG A1606
SITE 1 AC3 3 ASN A 462 ASP A 475 ATP A1605
SITE 1 AC4 11 ASN B 104 SER B 105 HIS B 113 LEU B 116
SITE 2 AC4 11 LYS B 291 LYS B 294 THR B 295 TYR B 298
SITE 3 AC4 11 GLU B 376 ASN B 377 HOH B 580
SITE 1 AC5 20 PRO B 316 GLY B 317 ILE B 318 VAL B 322
SITE 2 AC5 20 MET B 323 VAL B 325 VAL B 334 LYS B 336
SITE 3 AC5 20 GLU B 416 ARG B 417 ARG B 418 MET B 419
SITE 4 AC5 20 PRO B 421 ASN B 462 TYR B 474 ASP B 475
SITE 5 AC5 20 ASP B 477 GLU B 478 HOH B 594 MG B1606
SITE 1 AC6 3 ASN B 462 ASP B 475 ATP B1605
CRYST1 124.595 124.595 267.635 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 0.008026 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008026 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
