HEADER TRANSFERASE 28-MAR-19 6OF8
TITLE STRUCTURE OF THR354ASN, GLU355GLN, THR412ASN, ILE414MET, ILE464HIS,
TITLE 2 AND PHE467MET MUTANT HUMAN CAMKII-ALPHA HUB DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND 3 ALPHA;
COMPND 4 CHAIN: F, B, C, G, E, A, D;
COMPND 5 SYNONYM: CAMK-II SUBUNIT ALPHA;
COMPND 6 EC: 2.7.11.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: CAMK2A, CAMKA, KIAA0968;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CAMKII HUB DOMAIN, SIGNALING PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.D.MCSPADDEN,C.C.CHI,C.L.GEE,J.KURIYAN
REVDAT 4 11-OCT-23 6OF8 1 LINK
REVDAT 3 20-NOV-19 6OF8 1 REMARK
REVDAT 2 29-MAY-19 6OF8 1 JRNL
REVDAT 1 17-APR-19 6OF8 0
JRNL AUTH E.D.MCSPADDEN,Z.XIA,C.C.CHI,A.C.SUSA,N.H.SHAH,C.L.GEE,
JRNL AUTH 2 E.R.WILLIAMS,J.KURIYAN
JRNL TITL VARIATION IN ASSEMBLY STOICHIOMETRY IN NON-METAZOAN HOMOLOGS
JRNL TITL 2 OF THE HUB DOMAIN OF CA2+/CALMODULIN-DEPENDENT PROTEIN
JRNL TITL 3 KINASE II.
JRNL REF PROTEIN SCI. V. 28 1071 2019
JRNL REFN ESSN 1469-896X
JRNL PMID 30942928
JRNL DOI 10.1002/PRO.3614
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 60303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 3071
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 47.5167 - 5.8807 0.99 2639 154 0.1960 0.2452
REMARK 3 2 5.8807 - 4.6690 1.00 2621 142 0.1837 0.2139
REMARK 3 3 4.6690 - 4.0792 1.00 2633 128 0.1820 0.2197
REMARK 3 4 4.0792 - 3.7064 1.00 2618 140 0.1952 0.2298
REMARK 3 5 3.7064 - 3.4408 1.00 2637 113 0.2082 0.2499
REMARK 3 6 3.4408 - 3.2380 1.00 2656 122 0.2197 0.2319
REMARK 3 7 3.2380 - 3.0759 1.00 2591 147 0.2382 0.2890
REMARK 3 8 3.0759 - 2.9420 1.00 2603 140 0.2499 0.2743
REMARK 3 9 2.9420 - 2.8288 1.00 2573 155 0.2554 0.2852
REMARK 3 10 2.8288 - 2.7311 0.99 2595 148 0.2719 0.2936
REMARK 3 11 2.7311 - 2.6458 0.99 2597 146 0.2822 0.3395
REMARK 3 12 2.6458 - 2.5701 1.00 2596 131 0.2735 0.2763
REMARK 3 13 2.5701 - 2.5025 1.00 2605 155 0.2886 0.3214
REMARK 3 14 2.5025 - 2.4414 1.00 2592 128 0.2683 0.2812
REMARK 3 15 2.4414 - 2.3859 1.00 2618 137 0.2724 0.3277
REMARK 3 16 2.3859 - 2.3352 1.00 2593 142 0.2783 0.3043
REMARK 3 17 2.3352 - 2.2884 0.99 2556 155 0.2972 0.3231
REMARK 3 18 2.2884 - 2.2453 0.99 2561 149 0.3060 0.3478
REMARK 3 19 2.2453 - 2.2052 0.99 2592 141 0.3071 0.3738
REMARK 3 20 2.2052 - 2.1678 1.00 2598 129 0.3066 0.3070
REMARK 3 21 2.1678 - 2.1328 1.00 2632 127 0.3192 0.3588
REMARK 3 22 2.1328 - 2.1000 0.98 2526 142 0.3487 0.3783
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.960
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) : 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 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 : 0.002 7569
REMARK 3 ANGLE : 0.511 10217
REMARK 3 CHIRALITY : 0.042 1043
REMARK 3 PLANARITY : 0.003 1339
REMARK 3 DIHEDRAL : 18.344 4477
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 6OF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000239516.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115830
REMARK 200 MONOCHROMATOR : S111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60334
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.83100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1HKX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17 MG/ML MUTANT HUB IN 25 MM TRIS, 150
REMARK 280 MM KCL, 10% (V/V) GLYCEROL, 2 MM DTT, 1 MM TCEP, PH 8.0 WAS
REMARK 280 MIXED 1:1 WITH 235 MM K3CITRATE, 15% (W/V) PEG 3350, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 81.49250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.67150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.49250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 60.67150
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 75450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -237.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, B, C, G, E, A, D
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 -1.000000 0.000000 0.000000 110.42868
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 160.32236
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 GLY F 341
REMARK 465 PRO F 342
REMARK 465 HIS F 343
REMARK 465 MET F 344
REMARK 465 VAL F 345
REMARK 465 SER F 474
REMARK 465 VAL F 475
REMARK 465 GLY B 341
REMARK 465 PRO B 342
REMARK 465 PRO B 473
REMARK 465 SER B 474
REMARK 465 VAL B 475
REMARK 465 GLY C 341
REMARK 465 PRO C 342
REMARK 465 PRO C 473
REMARK 465 SER C 474
REMARK 465 VAL C 475
REMARK 465 GLY G 341
REMARK 465 PRO G 342
REMARK 465 SER G 404
REMARK 465 ARG G 405
REMARK 465 ASN G 406
REMARK 465 SER G 407
REMARK 465 LYS G 408
REMARK 465 PRO G 473
REMARK 465 SER G 474
REMARK 465 VAL G 475
REMARK 465 GLY E 341
REMARK 465 PRO E 342
REMARK 465 HIS E 343
REMARK 465 MET E 344
REMARK 465 VAL E 345
REMARK 465 GLY A 341
REMARK 465 PRO A 473
REMARK 465 SER A 474
REMARK 465 VAL A 475
REMARK 465 GLY D 341
REMARK 465 PRO D 342
REMARK 465 ARG D 405
REMARK 465 ASN D 406
REMARK 465 VAL D 475
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 LEU F 402 -78.80 -146.00
REMARK 500 ASN F 416 72.31 43.30
REMARK 500 ASN B 401 -79.56 -123.72
REMARK 500 ASP C 365 86.36 -57.96
REMARK 500 LEU C 402 -84.99 -141.40
REMARK 500 ARG C 405 -114.84 -13.39
REMARK 500 ASN C 416 69.87 36.04
REMARK 500 ASN G 401 -62.09 -138.89
REMARK 500 ASP G 439 39.99 -91.01
REMARK 500 ALA G 440 -19.88 64.24
REMARK 500 LEU E 402 -62.63 -159.77
REMARK 500 ASN E 416 63.73 39.79
REMARK 500 ASP E 439 -158.92 -88.84
REMARK 500 ASP A 365 86.60 -68.25
REMARK 500 LEU A 402 -26.48 -142.28
REMARK 500 ASN A 406 60.44 -156.49
REMARK 500 ASP A 439 -169.44 -75.53
REMARK 500 LEU D 402 -71.31 -145.90
REMARK 500 ASP D 439 -157.33 -75.24
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 K F 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 370 O
REMARK 620 2 LYS F 371 O 75.0
REMARK 620 3 CYS F 373 O 68.8 110.8
REMARK 620 4 GLN F 463 OE1 136.8 82.4 86.3
REMARK 620 5 GLN D 348 OE1 62.7 36.1 74.8 77.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K F 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET F 377 O
REMARK 620 2 VAL F 389 O 77.2
REMARK 620 3 GLY F 391 O 79.0 129.0
REMARK 620 4 HOH F 601 O 129.8 140.7 52.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 370 O
REMARK 620 2 LYS E 371 O 75.3
REMARK 620 3 CYS E 373 O 67.4 111.0
REMARK 620 4 GLN E 463 OE1 137.7 83.2 87.9
REMARK 620 5 GLN A 348 OE1 64.8 138.9 45.0 120.4
REMARK 620 6 HOH A 605 O 130.1 145.8 101.1 86.7 73.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 370 O
REMARK 620 2 LYS A 371 O 70.6
REMARK 620 3 CYS A 373 O 71.4 103.5
REMARK 620 4 GLN A 463 OE1 137.4 94.7 73.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 370 O
REMARK 620 2 LYS D 371 O 70.9
REMARK 620 3 CYS D 373 O 69.1 102.8
REMARK 620 4 GLN D 463 OE1 131.9 88.8 74.0
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 K F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K D 501
DBREF 6OF8 F 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 B 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 C 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 G 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 E 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 A 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 6OF8 D 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
SEQADV 6OF8 GLY F 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO F 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS F 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET F 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN F 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN F 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN F 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET F 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS F 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET F 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY B 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO B 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS B 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET B 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN B 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN B 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN B 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET B 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS B 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET B 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY C 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO C 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS C 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET C 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN C 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN C 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN C 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET C 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS C 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET C 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY G 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO G 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS G 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET G 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN G 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN G 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN G 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET G 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS G 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET G 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY E 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO E 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS E 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET E 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN E 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN E 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN E 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET E 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS E 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET E 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY A 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO A 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS A 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET A 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN A 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN A 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN A 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET A 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS A 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET A 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQADV 6OF8 GLY D 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 PRO D 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 HIS D 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 MET D 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 6OF8 ASN D 354 UNP Q9UQM7 THR 354 ENGINEERED MUTATION
SEQADV 6OF8 GLN D 355 UNP Q9UQM7 GLU 355 ENGINEERED MUTATION
SEQADV 6OF8 ASN D 412 UNP Q9UQM7 THR 412 ENGINEERED MUTATION
SEQADV 6OF8 MET D 414 UNP Q9UQM7 ILE 414 ENGINEERED MUTATION
SEQADV 6OF8 HIS D 464 UNP Q9UQM7 ILE 464 ENGINEERED MUTATION
SEQADV 6OF8 MET D 467 UNP Q9UQM7 PHE 467 ENGINEERED MUTATION
SEQRES 1 F 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 F 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 F 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 F 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 F 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 F 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 F 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 F 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 F 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 F 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 F 135 GLY ALA PRO SER VAL
SEQRES 1 B 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 B 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 B 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 B 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 B 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 B 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 B 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 B 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 B 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 B 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 B 135 GLY ALA PRO SER VAL
SEQRES 1 C 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 C 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 C 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 C 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 C 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 C 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 C 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 C 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 C 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 C 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 C 135 GLY ALA PRO SER VAL
SEQRES 1 G 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 G 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 G 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 G 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 G 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 G 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 G 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 G 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 G 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 G 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 G 135 GLY ALA PRO SER VAL
SEQRES 1 E 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 E 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 E 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 E 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 E 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 E 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 E 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 E 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 E 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 E 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 E 135 GLY ALA PRO SER VAL
SEQRES 1 A 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 A 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 A 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 A 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 A 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 A 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 A 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 A 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 A 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 A 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 A 135 GLY ALA PRO SER VAL
SEQRES 1 D 135 GLY PRO HIS MET VAL ARG LYS GLN GLU ILE ILE LYS VAL
SEQRES 2 D 135 ASN GLN GLN LEU ILE GLU ALA ILE SER ASN GLY ASP PHE
SEQRES 3 D 135 GLU SER TYR THR LYS MET CYS ASP PRO GLY MET THR ALA
SEQRES 4 D 135 PHE GLU PRO GLU ALA LEU GLY ASN LEU VAL GLU GLY LEU
SEQRES 5 D 135 ASP PHE HIS ARG PHE TYR PHE GLU ASN LEU TRP SER ARG
SEQRES 6 D 135 ASN SER LYS PRO VAL HIS ASN THR MET LEU ASN PRO HIS
SEQRES 7 D 135 ILE HIS LEU MET GLY ASP GLU SER ALA CYS ILE ALA TYR
SEQRES 8 D 135 ILE ARG ILE THR GLN TYR LEU ASP ALA GLY GLY ILE PRO
SEQRES 9 D 135 ARG THR ALA GLN SER GLU GLU THR ARG VAL TRP HIS ARG
SEQRES 10 D 135 ARG ASP GLY LYS TRP GLN HIS VAL HIS MET HIS ARG SER
SEQRES 11 D 135 GLY ALA PRO SER VAL
HET K F 501 1
HET K F 502 1
HET GOL C 501 6
HET GOL E 501 6
HET K E 502 1
HET GOL A 501 6
HET K A 502 1
HET K D 501 1
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 8 K 5(K 1+)
FORMUL 10 GOL 3(C3 H8 O3)
FORMUL 16 HOH *105(H2 O)
HELIX 1 AA1 ARG F 346 ASN F 363 1 18
HELIX 2 AA2 ASP F 365 MET F 372 1 8
HELIX 3 AA3 PRO F 382 LEU F 385 5 4
HELIX 4 AA4 LEU F 392 LEU F 402 1 11
HELIX 5 AA5 MET B 344 GLY B 364 1 21
HELIX 6 AA6 ASP B 365 MET B 372 1 8
HELIX 7 AA7 PRO B 382 LEU B 385 5 4
HELIX 8 AA8 LEU B 392 ASN B 401 1 10
HELIX 9 AA9 MET C 344 GLY C 364 1 21
HELIX 10 AB1 ASP C 365 MET C 372 1 8
HELIX 11 AB2 GLU C 381 LEU C 385 5 5
HELIX 12 AB3 LEU C 392 ASN C 401 1 10
HELIX 13 AB4 MET G 344 GLY G 364 1 21
HELIX 14 AB5 ASP G 365 MET G 372 1 8
HELIX 15 AB6 GLU G 381 LEU G 385 5 5
HELIX 16 AB7 GLY G 391 ASN G 401 1 11
HELIX 17 AB8 LYS E 347 GLY E 364 1 18
HELIX 18 AB9 ASP E 365 MET E 372 1 8
HELIX 19 AC1 PRO E 382 LEU E 385 5 4
HELIX 20 AC2 LEU E 392 ASN E 401 1 10
HELIX 21 AC3 HIS A 343 ASN A 363 1 21
HELIX 22 AC4 ASP A 365 MET A 372 1 8
HELIX 23 AC5 PRO A 382 LEU A 385 5 4
HELIX 24 AC6 LEU A 392 LEU A 402 1 11
HELIX 25 AC7 MET D 344 GLY D 364 1 21
HELIX 26 AC8 ASP D 365 MET D 372 1 8
HELIX 27 AC9 PRO D 382 LEU D 385 5 4
HELIX 28 AD1 LEU D 392 LEU D 402 1 11
SHEET 1 AA1 6 LEU F 388 GLU F 390 0
SHEET 2 AA1 6 CYS F 373 PHE F 380 -1 N ALA F 379 O VAL F 389
SHEET 3 AA1 6 LYS F 461 GLY F 471 1 O ARG F 469 N PHE F 380
SHEET 4 AA1 6 PRO F 444 ARG F 458 -1 N VAL F 454 O HIS F 466
SHEET 5 AA1 6 SER F 426 LEU F 438 -1 N ARG F 433 O SER F 449
SHEET 6 AA1 6 VAL F 410 MET F 422 -1 N HIS F 411 O GLN F 436
SHEET 1 AA2 6 LEU B 388 GLU B 390 0
SHEET 2 AA2 6 CYS B 373 PHE B 380 -1 N ALA B 379 O VAL B 389
SHEET 3 AA2 6 LYS B 461 SER B 470 1 O ARG B 469 N PHE B 380
SHEET 4 AA2 6 PRO B 444 ARG B 458 -1 N VAL B 454 O HIS B 466
SHEET 5 AA2 6 SER B 426 LEU B 438 -1 N ARG B 433 O SER B 449
SHEET 6 AA2 6 HIS B 411 MET B 422 -1 N HIS B 420 O CYS B 428
SHEET 1 AA3 6 VAL C 389 GLU C 390 0
SHEET 2 AA3 6 CYS C 373 PHE C 380 -1 N ALA C 379 O VAL C 389
SHEET 3 AA3 6 LYS C 461 GLY C 471 1 O ARG C 469 N PHE C 380
SHEET 4 AA3 6 PRO C 444 ARG C 458 -1 N VAL C 454 O HIS C 466
SHEET 5 AA3 6 SER C 426 LEU C 438 -1 N ARG C 433 O SER C 449
SHEET 6 AA3 6 HIS C 411 LEU C 421 -1 N HIS C 411 O GLN C 436
SHEET 1 AA4 6 VAL G 389 GLU G 390 0
SHEET 2 AA4 6 CYS G 373 PHE G 380 -1 N ALA G 379 O VAL G 389
SHEET 3 AA4 6 TRP G 462 SER G 470 1 O ARG G 469 N PHE G 380
SHEET 4 AA4 6 PRO G 444 ARG G 457 -1 N VAL G 454 O HIS G 466
SHEET 5 AA4 6 SER G 426 LEU G 438 -1 N ARG G 433 O SER G 449
SHEET 6 AA4 6 HIS G 411 MET G 422 -1 N HIS G 420 O CYS G 428
SHEET 1 AA5 6 LEU E 388 GLU E 390 0
SHEET 2 AA5 6 CYS E 373 PHE E 380 -1 N ALA E 379 O VAL E 389
SHEET 3 AA5 6 LYS E 461 GLY E 471 1 O ARG E 469 N PHE E 380
SHEET 4 AA5 6 PRO E 444 ARG E 458 -1 N HIS E 456 O GLN E 463
SHEET 5 AA5 6 SER E 426 LEU E 438 -1 N TYR E 437 O ARG E 445
SHEET 6 AA5 6 HIS E 411 LEU E 421 -1 N HIS E 418 O ALA E 430
SHEET 1 AA6 6 LEU A 388 GLU A 390 0
SHEET 2 AA6 6 CYS A 373 PHE A 380 -1 N ALA A 379 O VAL A 389
SHEET 3 AA6 6 LYS A 461 GLY A 471 1 O ARG A 469 N PHE A 380
SHEET 4 AA6 6 PRO A 444 ARG A 458 -1 N VAL A 454 O HIS A 466
SHEET 5 AA6 6 SER A 426 LEU A 438 -1 N ARG A 433 O SER A 449
SHEET 6 AA6 6 VAL A 410 LEU A 421 -1 N HIS A 420 O CYS A 428
SHEET 1 AA7 6 LEU D 388 GLU D 390 0
SHEET 2 AA7 6 CYS D 373 PHE D 380 -1 N ALA D 379 O VAL D 389
SHEET 3 AA7 6 LYS D 461 GLY D 471 1 O ARG D 469 N PHE D 380
SHEET 4 AA7 6 PRO D 444 ARG D 458 -1 N ARG D 458 O LYS D 461
SHEET 5 AA7 6 SER D 426 LEU D 438 -1 N ARG D 433 O SER D 449
SHEET 6 AA7 6 HIS D 411 LEU D 421 -1 N HIS D 418 O ALA D 430
LINK O THR F 370 K K F 501 1555 1555 2.83
LINK O LYS F 371 K K F 501 1555 1555 3.10
LINK O CYS F 373 K K F 501 1555 1555 2.84
LINK O MET F 377 K K F 502 1555 1555 3.32
LINK O VAL F 389 K K F 502 1555 1555 2.94
LINK O GLY F 391 K K F 502 1555 1555 2.74
LINK OE1 GLN F 463 K K F 501 1555 1555 2.70
LINK K K F 501 OE1 GLN D 348 4547 1555 2.74
LINK K K F 502 O HOH F 601 1555 1555 3.26
LINK O THR E 370 K K E 502 1555 1555 2.81
LINK O LYS E 371 K K E 502 1555 1555 3.08
LINK O CYS E 373 K K E 502 1555 1555 2.80
LINK OE1 GLN E 463 K K E 502 1555 1555 2.72
LINK K K E 502 OE1 GLN A 348 4548 1555 2.66
LINK K K E 502 O HOH A 605 1555 4558 3.02
LINK O THR A 370 K K A 502 1555 1555 2.81
LINK O LYS A 371 K K A 502 1555 1555 3.18
LINK O CYS A 373 K K A 502 1555 1555 2.76
LINK OE1 GLN A 463 K K A 502 1555 1555 2.92
LINK O THR D 370 K K D 501 1555 1555 2.92
LINK O LYS D 371 K K D 501 1555 1555 2.96
LINK O CYS D 373 K K D 501 1555 1555 2.77
LINK OE1 GLN D 463 K K D 501 1555 1555 2.97
SITE 1 AC1 5 GLN D 348 THR F 370 LYS F 371 CYS F 373
SITE 2 AC1 5 GLN F 463
SITE 1 AC2 4 MET F 377 ALA F 379 VAL F 389 GLY F 391
SITE 1 AC3 8 GLN C 448 LEU D 385 GLY D 386 ASN D 387
SITE 2 AC3 8 LEU E 385 GLY E 386 ASN E 387 GLN F 448
SITE 1 AC4 4 GLN E 448 LEU F 385 ASN F 387 GLN G 448
SITE 1 AC5 4 THR E 370 LYS E 371 CYS E 373 GLN E 463
SITE 1 AC6 5 LEU A 385 GLY A 386 ASN A 387 ILE B 432
SITE 2 AC6 5 GLN B 448
SITE 1 AC7 4 THR A 370 LYS A 371 CYS A 373 GLN A 463
SITE 1 AC8 4 THR D 370 LYS D 371 CYS D 373 GLN D 463
CRYST1 162.985 121.343 56.239 90.00 108.15 90.00 C 1 2 1 28
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 0.006136 0.000000 0.002011 0.00000
SCALE2 0.000000 0.008241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018712 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
