HEADER TRANSFERASE 26-FEB-16 5IG3
TITLE CRYSTAL STRUCTURE OF THE HUMAN CAMKII-ALPHA HUB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND 3 ALPHA;
COMPND 4 CHAIN: A, B, C, D, E, F;
COMPND 5 FRAGMENT: UNP RESIDUES 345-475;
COMPND 6 SYNONYM: CAMK-II SUBUNIT ALPHA;
COMPND 7 EC: 2.7.11.17;
COMPND 8 ENGINEERED: 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CA2+/CAM-DEPENDENT KINASE ALPHA, HUB, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MCSPADDEN,Y.M.CAO,M.BHATTACHARYYA,C.L.GEE,T.BARROS,J.KURIYAN
REVDAT 6 27-SEP-23 5IG3 1 REMARK
REVDAT 5 20-NOV-19 5IG3 1 REMARK
REVDAT 4 27-SEP-17 5IG3 1 REMARK
REVDAT 3 13-JUL-16 5IG3 1 REMARK
REVDAT 2 06-APR-16 5IG3 1 AUTHOR
REVDAT 1 23-MAR-16 5IG3 0
JRNL AUTH M.BHATTACHARYYA,M.M.STRATTON,C.C.GOING,E.D.MCSPADDEN,
JRNL AUTH 2 Y.HUANG,A.C.SUSA,A.ELLEMAN,Y.M.CAO,N.PAPPIREDDI,P.BURKHARDT,
JRNL AUTH 3 C.L.GEE,T.BARROS,H.SCHULMAN,E.R.WILLIAMS,J.KURIYAN
JRNL TITL MOLECULAR MECHANISM OF ACTIVATION-TRIGGERED SUBUNIT EXCHANGE
JRNL TITL 2 IN CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 26949248
JRNL DOI 10.7554/ELIFE.13405
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23820
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710
REMARK 3 FREE R VALUE TEST SET COUNT : 1184
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 48.6384 - 6.7764 1.00 2914 161 0.2166 0.2508
REMARK 3 2 6.7764 - 5.3809 1.00 2904 170 0.2439 0.2737
REMARK 3 3 5.3809 - 4.7013 1.00 2919 145 0.1745 0.2222
REMARK 3 4 4.7013 - 4.2718 1.00 2894 151 0.1654 0.2027
REMARK 3 5 4.2718 - 3.9657 1.00 2938 162 0.1845 0.2421
REMARK 3 6 3.9657 - 3.7320 1.00 2907 140 0.2030 0.2804
REMARK 3 7 3.7320 - 3.5452 1.00 2945 145 0.2220 0.3004
REMARK 3 8 3.5452 - 3.3909 1.00 2977 124 0.2465 0.3612
REMARK 3 9 3.3909 - 3.2604 1.00 2910 132 0.2655 0.3352
REMARK 3 10 3.2604 - 3.1479 1.00 2910 153 0.2488 0.3070
REMARK 3 11 3.1479 - 3.0495 1.00 2930 160 0.2620 0.3020
REMARK 3 12 3.0495 - 2.9623 1.00 2909 154 0.2879 0.3351
REMARK 3 13 2.9623 - 2.8843 1.00 2914 124 0.3073 0.3641
REMARK 3 14 2.8843 - 2.8140 1.00 2969 102 0.3379 0.3618
REMARK 3 15 2.8140 - 2.7500 1.00 2950 146 0.4093 0.4363
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.00
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 6459
REMARK 3 ANGLE : 0.505 8727
REMARK 3 CHIRALITY : 0.042 921
REMARK 3 PLANARITY : 0.003 1131
REMARK 3 DIHEDRAL : 11.499 3798
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 329 THROUGH 472)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0728 75.2717 -10.6222
REMARK 3 T TENSOR
REMARK 3 T11: 0.6364 T22: 0.6067
REMARK 3 T33: 0.5676 T12: -0.0422
REMARK 3 T13: 0.1766 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 4.3460 L22: 3.6227
REMARK 3 L33: 4.6260 L12: 0.5762
REMARK 3 L13: 0.8026 L23: -2.0140
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: 0.3885 S13: -0.1134
REMARK 3 S21: -0.6569 S22: -0.0480 S23: -0.2542
REMARK 3 S31: 0.1548 S32: 0.5510 S33: 0.0478
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 344 THROUGH 473)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.0853 49.4096 -27.8143
REMARK 3 T TENSOR
REMARK 3 T11: 0.6917 T22: 0.5191
REMARK 3 T33: 0.5444 T12: 0.0791
REMARK 3 T13: -0.0506 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 3.6877 L22: 5.4568
REMARK 3 L33: 5.3146 L12: 0.6597
REMARK 3 L13: -0.4139 L23: -1.0112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.4719 S13: -0.4200
REMARK 3 S21: -0.7411 S22: -0.0312 S23: 0.0858
REMARK 3 S31: 0.4074 S32: -0.1636 S33: 0.0390
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 331 THROUGH 472)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.0029 24.3888 -5.5590
REMARK 3 T TENSOR
REMARK 3 T11: 0.8046 T22: 0.4616
REMARK 3 T33: 0.6548 T12: 0.0360
REMARK 3 T13: -0.0625 T23: 0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 3.8488 L22: 4.3143
REMARK 3 L33: 6.0667 L12: -1.7309
REMARK 3 L13: 1.6302 L23: -0.8191
REMARK 3 S TENSOR
REMARK 3 S11: 0.2155 S12: 0.0288 S13: -0.7827
REMARK 3 S21: -0.6741 S22: 0.0057 S23: 0.3548
REMARK 3 S31: 1.0598 S32: 0.0127 S33: -0.1751
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 331 THROUGH 473)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7258 24.6518 15.0052
REMARK 3 T TENSOR
REMARK 3 T11: 0.6892 T22: 0.6674
REMARK 3 T33: 0.7338 T12: 0.2513
REMARK 3 T13: 0.0374 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 5.5725 L22: 4.8471
REMARK 3 L33: 3.7395 L12: -0.0060
REMARK 3 L13: 1.4812 L23: -0.2240
REMARK 3 S TENSOR
REMARK 3 S11: 0.1072 S12: 0.2654 S13: -0.6975
REMARK 3 S21: -0.3122 S22: -0.1248 S23: -0.3376
REMARK 3 S31: 0.8125 S32: 0.6089 S33: 0.0802
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 344 THROUGH 473)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9364 75.3487 -29.6994
REMARK 3 T TENSOR
REMARK 3 T11: 1.1827 T22: 0.6504
REMARK 3 T33: 0.5702 T12: -0.0432
REMARK 3 T13: -0.0378 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 7.4790 L22: 1.4467
REMARK 3 L33: 4.1374 L12: 0.6252
REMARK 3 L13: 0.4026 L23: 1.2998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0444 S12: 0.8949 S13: 0.2399
REMARK 3 S21: -0.8751 S22: -0.0450 S23: -0.0139
REMARK 3 S31: -1.0488 S32: 0.4395 S33: 0.0704
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 344 THROUGH 472)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0041 49.3238 12.8680
REMARK 3 T TENSOR
REMARK 3 T11: 0.5275 T22: 1.1771
REMARK 3 T33: 0.8518 T12: 0.0278
REMARK 3 T13: 0.0657 T23: 0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 4.1560 L22: 5.0761
REMARK 3 L33: 1.8555 L12: -0.2782
REMARK 3 L13: -0.4964 L23: -0.9169
REMARK 3 S TENSOR
REMARK 3 S11: -0.1455 S12: -0.6869 S13: -0.4616
REMARK 3 S21: -0.2924 S22: -0.0542 S23: -1.1331
REMARK 3 S31: 0.0206 S32: 1.2963 S33: 0.0954
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 5IG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218779.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : M1: PARABOLA M2: TORROID
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25096
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 48.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 1.12400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 (%): 43.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % (V/V) MPD, 0.1 M HEPES PH 7.3,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 113.28850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.94400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.94400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 169.93275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.94400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.94400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.64425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.94400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.94400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 169.93275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.94400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.94400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.64425
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 113.28850
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 -89.88800
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 89.88800
REMARK 350 BIOMT3 2 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 GLY A 323
REMARK 465 SER A 324
REMARK 465 SER A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 PRO A 473
REMARK 465 SER A 474
REMARK 465 VAL A 475
REMARK 465 GLY B 323
REMARK 465 SER B 324
REMARK 465 SER B 325
REMARK 465 HIS B 326
REMARK 465 HIS B 327
REMARK 465 HIS B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 SER B 332
REMARK 465 SER B 333
REMARK 465 GLY B 334
REMARK 465 LEU B 335
REMARK 465 GLU B 336
REMARK 465 VAL B 337
REMARK 465 LEU B 338
REMARK 465 PHE B 339
REMARK 465 GLN B 340
REMARK 465 GLY B 341
REMARK 465 PRO B 342
REMARK 465 HIS B 343
REMARK 465 SER B 404
REMARK 465 ARG B 405
REMARK 465 ASN B 406
REMARK 465 SER B 474
REMARK 465 VAL B 475
REMARK 465 GLY C 323
REMARK 465 SER C 324
REMARK 465 SER C 325
REMARK 465 HIS C 326
REMARK 465 HIS C 327
REMARK 465 HIS C 328
REMARK 465 HIS C 329
REMARK 465 HIS C 330
REMARK 465 LEU C 335
REMARK 465 GLU C 336
REMARK 465 VAL C 337
REMARK 465 LEU C 338
REMARK 465 PHE C 339
REMARK 465 GLN C 340
REMARK 465 GLY C 341
REMARK 465 PRO C 342
REMARK 465 ARG C 405
REMARK 465 ASN C 406
REMARK 465 PRO C 473
REMARK 465 SER C 474
REMARK 465 VAL C 475
REMARK 465 GLY D 323
REMARK 465 SER D 324
REMARK 465 SER D 325
REMARK 465 HIS D 326
REMARK 465 HIS D 327
REMARK 465 HIS D 328
REMARK 465 HIS D 329
REMARK 465 HIS D 330
REMARK 465 GLY D 334
REMARK 465 LEU D 335
REMARK 465 GLU D 336
REMARK 465 VAL D 337
REMARK 465 LEU D 338
REMARK 465 PHE D 339
REMARK 465 GLN D 340
REMARK 465 GLY D 341
REMARK 465 PRO D 342
REMARK 465 HIS D 343
REMARK 465 TRP D 403
REMARK 465 SER D 404
REMARK 465 ARG D 405
REMARK 465 ASN D 406
REMARK 465 SER D 407
REMARK 465 LYS D 408
REMARK 465 SER D 474
REMARK 465 VAL D 475
REMARK 465 GLY E 323
REMARK 465 SER E 324
REMARK 465 SER E 325
REMARK 465 HIS E 326
REMARK 465 HIS E 327
REMARK 465 HIS E 328
REMARK 465 HIS E 329
REMARK 465 HIS E 330
REMARK 465 HIS E 331
REMARK 465 SER E 332
REMARK 465 SER E 333
REMARK 465 GLY E 334
REMARK 465 LEU E 335
REMARK 465 GLU E 336
REMARK 465 VAL E 337
REMARK 465 LEU E 338
REMARK 465 PHE E 339
REMARK 465 GLN E 340
REMARK 465 GLY E 341
REMARK 465 PRO E 342
REMARK 465 TRP E 403
REMARK 465 SER E 404
REMARK 465 ARG E 405
REMARK 465 ASN E 406
REMARK 465 SER E 407
REMARK 465 LYS E 408
REMARK 465 SER E 474
REMARK 465 VAL E 475
REMARK 465 GLY F 323
REMARK 465 SER F 324
REMARK 465 SER F 325
REMARK 465 HIS F 326
REMARK 465 HIS F 327
REMARK 465 HIS F 328
REMARK 465 HIS F 329
REMARK 465 HIS F 330
REMARK 465 HIS F 331
REMARK 465 SER F 332
REMARK 465 SER F 333
REMARK 465 GLY F 334
REMARK 465 LEU F 335
REMARK 465 GLU F 336
REMARK 465 VAL F 337
REMARK 465 LEU F 338
REMARK 465 PHE F 339
REMARK 465 GLN F 340
REMARK 465 GLY F 341
REMARK 465 PRO F 342
REMARK 465 HIS F 343
REMARK 465 LEU F 402
REMARK 465 TRP F 403
REMARK 465 SER F 404
REMARK 465 ARG F 405
REMARK 465 ASN F 406
REMARK 465 SER F 407
REMARK 465 PRO F 473
REMARK 465 SER F 474
REMARK 465 VAL F 475
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 C 374 NH1 ARG C 458 1.90
REMARK 500 OD1 ASP B 374 NH1 ARG B 458 1.93
REMARK 500 OD2 ASP E 365 OG SER E 368 2.15
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 HIS A 343 73.18 -107.25
REMARK 500 ASP A 439 -160.06 -77.18
REMARK 500 ASN C 401 -73.80 -83.73
REMARK 500 ALA C 440 -107.30 51.55
REMARK 500 ILE C 443 77.43 57.08
REMARK 500 GLU D 425 13.97 -143.68
REMARK 500 ASN E 401 13.96 -142.10
REMARK 500 MET E 422 66.60 -119.88
REMARK 500 GLU E 425 11.29 -151.93
REMARK 500 ALA F 440 -62.31 18.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IG0 RELATED DB: PDB
REMARK 900 RELATED ID: 5IG1 RELATED DB: PDB
REMARK 900 RELATED ID: 5IG4 RELATED DB: PDB
REMARK 900 RELATED ID: 5IG5 RELATED DB: PDB
DBREF 5IG3 A 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 5IG3 B 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 5IG3 C 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 5IG3 D 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 5IG3 E 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
DBREF 5IG3 F 345 475 UNP Q9UQM7 KCC2A_HUMAN 345 475
SEQADV 5IG3 GLY A 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER A 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER A 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER A 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER A 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY A 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU A 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU A 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL A 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU A 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE A 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN A 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY A 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO A 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS A 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET A 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY B 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER B 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER B 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER B 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER B 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY B 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU B 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU B 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL B 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU B 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE B 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN B 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY B 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO B 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS B 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET B 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY C 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER C 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER C 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER C 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER C 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY C 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU C 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU C 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL C 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU C 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE C 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN C 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY C 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO C 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS C 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET C 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY D 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER D 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER D 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER D 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER D 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY D 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU D 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU D 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL D 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU D 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE D 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN D 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY D 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO D 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS D 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET D 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY E 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER E 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER E 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER E 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER E 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY E 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU E 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU E 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL E 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU E 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE E 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN E 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY E 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO E 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS E 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET E 344 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY F 323 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER F 324 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER F 325 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 326 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 327 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 328 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 329 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 330 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 331 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER F 332 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 SER F 333 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY F 334 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU F 335 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLU F 336 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 VAL F 337 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 LEU F 338 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PHE F 339 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLN F 340 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 GLY F 341 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 PRO F 342 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 HIS F 343 UNP Q9UQM7 EXPRESSION TAG
SEQADV 5IG3 MET F 344 UNP Q9UQM7 EXPRESSION TAG
SEQRES 1 A 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 A 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 A 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 A 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 A 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 A 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 A 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 A 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 A 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 A 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 A 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
SEQRES 1 B 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 B 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 B 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 B 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 B 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 B 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 B 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 B 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 B 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 B 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 B 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
SEQRES 1 C 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 C 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 C 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 C 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 C 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 C 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 C 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 C 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 C 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 C 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 C 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 C 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
SEQRES 1 D 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 D 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 D 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 D 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 D 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 D 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 D 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 D 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 D 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 D 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 D 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 D 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
SEQRES 1 E 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 E 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 E 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 E 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 E 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 E 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 E 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 E 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 E 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 E 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 E 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 E 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
SEQRES 1 F 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 F 153 GLU VAL LEU PHE GLN GLY PRO HIS MET VAL ARG LYS GLN
SEQRES 3 F 153 GLU ILE ILE LYS VAL THR GLU GLN LEU ILE GLU ALA ILE
SEQRES 4 F 153 SER ASN GLY ASP PHE GLU SER TYR THR LYS MET CYS ASP
SEQRES 5 F 153 PRO GLY MET THR ALA PHE GLU PRO GLU ALA LEU GLY ASN
SEQRES 6 F 153 LEU VAL GLU GLY LEU ASP PHE HIS ARG PHE TYR PHE GLU
SEQRES 7 F 153 ASN LEU TRP SER ARG ASN SER LYS PRO VAL HIS THR THR
SEQRES 8 F 153 ILE LEU ASN PRO HIS ILE HIS LEU MET GLY ASP GLU SER
SEQRES 9 F 153 ALA CYS ILE ALA TYR ILE ARG ILE THR GLN TYR LEU ASP
SEQRES 10 F 153 ALA GLY GLY ILE PRO ARG THR ALA GLN SER GLU GLU THR
SEQRES 11 F 153 ARG VAL TRP HIS ARG ARG ASP GLY LYS TRP GLN ILE VAL
SEQRES 12 F 153 HIS PHE HIS ARG SER GLY ALA PRO SER VAL
FORMUL 7 HOH *15(H2 O)
HELIX 1 AA1 LEU A 335 GLN A 340 1 6
HELIX 2 AA2 HIS A 343 ASN A 363 1 21
HELIX 3 AA3 ASP A 365 MET A 372 1 8
HELIX 4 AA4 GLU A 381 LEU A 385 5 5
HELIX 5 AA5 LEU A 392 ASN A 401 1 10
HELIX 6 AA6 ASN A 401 ASN A 406 1 6
HELIX 7 AA7 VAL B 345 GLY B 364 1 20
HELIX 8 AA8 ASP B 365 MET B 372 1 8
HELIX 9 AA9 GLU B 381 LEU B 385 5 5
HELIX 10 AB1 LEU B 392 ASN B 401 1 10
HELIX 11 AB2 MET C 344 ASN C 363 1 20
HELIX 12 AB3 ASP C 365 MET C 372 1 8
HELIX 13 AB4 PRO C 382 LEU C 385 5 4
HELIX 14 AB5 LEU C 392 ASN C 401 1 10
HELIX 15 AB6 ARG D 346 ASN D 363 1 18
HELIX 16 AB7 ASP D 365 MET D 372 1 8
HELIX 17 AB8 GLU D 381 LEU D 385 5 5
HELIX 18 AB9 LEU D 392 LEU D 402 1 11
HELIX 19 AC1 ARG E 346 ASN E 363 1 18
HELIX 20 AC2 ASP E 365 MET E 372 1 8
HELIX 21 AC3 GLU E 381 LEU E 385 5 5
HELIX 22 AC4 LEU E 392 GLU E 400 1 9
HELIX 23 AC5 ARG F 346 ASN F 363 1 18
HELIX 24 AC6 ASP F 365 MET F 372 1 8
HELIX 25 AC7 GLU F 381 LEU F 385 5 5
HELIX 26 AC8 LEU F 392 PHE F 397 1 6
SHEET 1 AA1 7 HIS A 330 SER A 332 0
SHEET 2 AA1 7 HIS A 411 LEU A 421 1 O THR A 412 N HIS A 330
SHEET 3 AA1 7 SER A 426 LEU A 438 -1 O ILE A 432 N LEU A 415
SHEET 4 AA1 7 PRO A 444 ARG A 458 -1 O ARG A 453 N ILE A 429
SHEET 5 AA1 7 LYS A 461 SER A 470 -1 O GLN A 463 N HIS A 456
SHEET 6 AA1 7 CYS A 373 PHE A 380 1 N ASP A 374 O ILE A 464
SHEET 7 AA1 7 VAL A 389 GLU A 390 -1 O VAL A 389 N ALA A 379
SHEET 1 AA2 6 VAL B 389 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 GLY B 471 1 O ILE B 464 N ASP B 374
SHEET 4 AA2 6 PRO B 444 ARG B 458 -1 N ARG B 458 O LYS B 461
SHEET 5 AA2 6 SER B 426 LEU B 438 -1 N ILE B 429 O ARG B 453
SHEET 6 AA2 6 HIS B 411 LEU B 421 -1 N LEU B 415 O ILE B 432
SHEET 1 AA3 7 SER C 332 GLY C 334 0
SHEET 2 AA3 7 HIS C 411 LEU C 421 1 O ILE C 414 N SER C 332
SHEET 3 AA3 7 SER C 426 LEU C 438 -1 O CYS C 428 N HIS C 420
SHEET 4 AA3 7 PRO C 444 ARG C 457 -1 O ARG C 453 N ILE C 429
SHEET 5 AA3 7 TRP C 462 SER C 470 -1 O HIS C 468 N THR C 452
SHEET 6 AA3 7 CYS C 373 PHE C 380 1 N ASP C 374 O ILE C 464
SHEET 7 AA3 7 LEU C 388 GLU C 390 -1 O VAL C 389 N ALA C 379
SHEET 1 AA4 6 VAL D 389 GLU D 390 0
SHEET 2 AA4 6 CYS D 373 PHE D 380 -1 N ALA D 379 O VAL D 389
SHEET 3 AA4 6 TRP D 462 GLY D 471 1 O ILE D 464 N ASP D 374
SHEET 4 AA4 6 PRO D 444 ARG D 457 -1 N VAL D 454 O VAL D 465
SHEET 5 AA4 6 SER D 426 LEU D 438 -1 N ILE D 429 O ARG D 453
SHEET 6 AA4 6 HIS D 411 LEU D 421 -1 N HIS D 411 O GLN D 436
SHEET 1 AA5 6 VAL E 389 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 TRP E 462 SER E 470 1 O PHE E 467 N PHE E 380
SHEET 4 AA5 6 PRO E 444 ARG E 457 -1 N GLU E 450 O SER E 470
SHEET 5 AA5 6 SER E 426 LEU E 438 -1 N ILE E 429 O ARG E 453
SHEET 6 AA5 6 HIS E 411 LEU E 421 -1 N LEU E 415 O ILE E 432
SHEET 1 AA6 6 VAL F 389 GLU F 390 0
SHEET 2 AA6 6 CYS F 373 PHE F 380 -1 N ALA F 379 O VAL F 389
SHEET 3 AA6 6 TRP F 462 GLY F 471 1 O PHE F 467 N PHE F 380
SHEET 4 AA6 6 ILE F 443 ARG F 457 -1 N VAL F 454 O VAL F 465
SHEET 5 AA6 6 SER F 426 ASP F 439 -1 N ILE F 429 O ARG F 453
SHEET 6 AA6 6 HIS F 411 LEU F 421 -1 N LEU F 415 O ILE F 432
CISPEP 1 GLY C 442 ILE C 443 0 0.64
CISPEP 2 SER E 470 GLY E 471 0 -2.54
CRYST1 89.888 89.888 226.577 90.00 90.00 90.00 P 43 21 2 48
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 0.011125 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011125 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004414 0.00000
(ATOM LINES ARE NOT SHOWN.)
END