HEADER OXIDOREDUCTASE 30-MAY-13 4L06
TITLE CRYSTAL STRUCTURE ANALYSIS OF HUMAN IDH1 MUTANTS IN COMPLEX WITH NADP+
TITLE 2 AND CA2+/ALPHA-KETOGLUTARATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: IDH, CYTOSOLIC NADP-ISOCITRATE DEHYDROGENASE, IDP, NADP(+)-
COMPND 5 SPECIFIC ICDH, OXALOSUCCINATE DECARBOXYLASE;
COMPND 6 EC: 1.1.1.42;
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: IDH1, PICD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET41A
KEYWDS CYTOSOLIC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.O.CONCHA,A.M.SMALLWOOD
REVDAT 3 28-FEB-24 4L06 1 REMARK SEQADV LINK
REVDAT 2 15-NOV-17 4L06 1 REMARK
REVDAT 1 24-JUL-13 4L06 0
JRNL AUTH A.R.RENDINA,B.PIETRAK,A.SMALLWOOD,H.ZHAO,H.QI,C.QUINN,
JRNL AUTH 2 N.D.ADAMS,N.CONCHA,C.DURAISWAMI,S.H.THRALL,S.SWEITZER,
JRNL AUTH 3 B.SCHWARTZ
JRNL TITL MUTANT IDH1 ENHANCES THE PRODUCTION OF 2-HYDROXYGLUTARATE
JRNL TITL 2 DUE TO ITS KINETIC MECHANISM.
JRNL REF BIOCHEMISTRY V. 52 4563 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23731180
JRNL DOI 10.1021/BI400514K
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 141182
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7077
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 72.2025 - 7.0882 0.97 4684 251 0.1792 0.1970
REMARK 3 2 7.0882 - 5.6268 1.00 4626 216 0.1958 0.2131
REMARK 3 3 5.6268 - 4.9157 1.00 4571 248 0.1737 0.1997
REMARK 3 4 4.9157 - 4.4663 1.00 4551 229 0.1599 0.2097
REMARK 3 5 4.4663 - 4.1462 1.00 4511 238 0.1718 0.2324
REMARK 3 6 4.1462 - 3.9018 1.00 4520 229 0.1931 0.2214
REMARK 3 7 3.9018 - 3.7064 1.00 4459 261 0.2049 0.2419
REMARK 3 8 3.7064 - 3.5451 1.00 4475 257 0.2101 0.2620
REMARK 3 9 3.5451 - 3.4086 1.00 4482 229 0.2272 0.2762
REMARK 3 10 3.4086 - 3.2910 1.00 4517 207 0.2389 0.3316
REMARK 3 11 3.2910 - 3.1881 1.00 4448 250 0.2478 0.3346
REMARK 3 12 3.1881 - 3.0969 1.00 4420 258 0.2460 0.2977
REMARK 3 13 3.0969 - 3.0154 1.00 4461 226 0.2541 0.3008
REMARK 3 14 3.0154 - 2.9418 1.00 4481 240 0.2591 0.2950
REMARK 3 15 2.9418 - 2.8750 1.00 4460 235 0.2682 0.3282
REMARK 3 16 2.8750 - 2.8138 1.00 4431 231 0.2685 0.3084
REMARK 3 17 2.8138 - 2.7575 1.00 4438 216 0.2705 0.3516
REMARK 3 18 2.7575 - 2.7054 1.00 4441 239 0.2807 0.3461
REMARK 3 19 2.7054 - 2.6571 1.00 4448 233 0.2783 0.3251
REMARK 3 20 2.6571 - 2.6121 1.00 4419 244 0.2907 0.3595
REMARK 3 21 2.6121 - 2.5699 1.00 4479 219 0.2898 0.3363
REMARK 3 22 2.5699 - 2.5304 1.00 4368 254 0.2990 0.3441
REMARK 3 23 2.5304 - 2.4932 1.00 4461 243 0.3039 0.4001
REMARK 3 24 2.4932 - 2.4581 1.00 4470 209 0.3092 0.3341
REMARK 3 25 2.4581 - 2.4248 1.00 4376 255 0.2999 0.3405
REMARK 3 26 2.4248 - 2.3934 1.00 4377 258 0.3112 0.3782
REMARK 3 27 2.3934 - 2.3634 1.00 4445 222 0.3287 0.3782
REMARK 3 28 2.3634 - 2.3350 1.00 4431 206 0.3285 0.3743
REMARK 3 29 2.3350 - 2.3078 1.00 4442 257 0.3227 0.3690
REMARK 3 30 2.3078 - 2.2820 1.00 4413 217 0.3172 0.3489
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.77
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 : 0.005 20113
REMARK 3 ANGLE : 0.887 27241
REMARK 3 CHIRALITY : 0.076 2961
REMARK 3 PLANARITY : 0.005 3484
REMARK 3 DIHEDRAL : 16.233 7414
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 3:415
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8626 -10.5494 -26.6470
REMARK 3 T TENSOR
REMARK 3 T11: 0.3233 T22: 0.1918
REMARK 3 T33: 0.1570 T12: 0.0582
REMARK 3 T13: -0.2387 T23: -0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 0.1721 L22: 0.3613
REMARK 3 L33: 0.3813 L12: 0.1151
REMARK 3 L13: 0.0553 L23: -0.0524
REMARK 3 S TENSOR
REMARK 3 S11: 0.0830 S12: 0.0556 S13: -0.0387
REMARK 3 S21: 0.5766 S22: 0.0765 S23: -0.3036
REMARK 3 S31: -0.0734 S32: -0.0091 S33: 0.0630
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND RESID 3:414
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8262 -41.2937 -30.6764
REMARK 3 T TENSOR
REMARK 3 T11: 0.3744 T22: 0.2585
REMARK 3 T33: 0.3348 T12: -0.0356
REMARK 3 T13: -0.1234 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.4545 L22: 0.5635
REMARK 3 L33: 0.7648 L12: 0.1277
REMARK 3 L13: -0.1942 L23: -0.2744
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0850 S13: -0.3407
REMARK 3 S21: 0.2211 S22: 0.0250 S23: -0.2721
REMARK 3 S31: 0.4189 S32: -0.1417 S33: -0.0414
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C AND RESID 3:413
REMARK 3 ORIGIN FOR THE GROUP (A): 69.1809 -44.3678 -70.8514
REMARK 3 T TENSOR
REMARK 3 T11: -0.5900 T22: 0.1184
REMARK 3 T33: -0.1680 T12: -0.0311
REMARK 3 T13: -0.0155 T23: -0.3226
REMARK 3 L TENSOR
REMARK 3 L11: 0.0616 L22: 0.0089
REMARK 3 L33: 0.0135 L12: 0.0390
REMARK 3 L13: -0.0261 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: 0.1236 S12: -0.0613 S13: -0.0609
REMARK 3 S21: 0.0413 S22: 0.1616 S23: -0.0550
REMARK 3 S31: 0.0678 S32: 0.3071 S33: 0.2983
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D AND RESID 4:414
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8748 -13.9801 -67.8209
REMARK 3 T TENSOR
REMARK 3 T11: -0.2386 T22: 0.2646
REMARK 3 T33: 0.4412 T12: -0.4530
REMARK 3 T13: 0.3746 T23: -0.2137
REMARK 3 L TENSOR
REMARK 3 L11: 0.0265 L22: 0.0634
REMARK 3 L33: -0.0136 L12: 0.0558
REMARK 3 L13: -0.0351 L23: -0.0226
REMARK 3 S TENSOR
REMARK 3 S11: 0.1302 S12: -0.1376 S13: 0.3965
REMARK 3 S21: 0.2227 S22: 0.1726 S23: -0.0239
REMARK 3 S31: -0.3985 S32: 0.3203 S33: 0.3140
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E AND RESID 3:415
REMARK 3 ORIGIN FOR THE GROUP (A): 73.5155 10.6589 -25.7802
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.0188
REMARK 3 T33: -0.3262 T12: -0.0025
REMARK 3 T13: 0.5358 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.0205 L22: 0.0203
REMARK 3 L33: 0.0283 L12: 0.0169
REMARK 3 L13: 0.0214 L23: -0.0136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: 0.0525 S13: -0.1754
REMARK 3 S21: 0.3145 S22: 0.1505 S23: 0.1460
REMARK 3 S31: 0.1122 S32: 0.0322 S33: 0.1397
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN F AND RESID 3:414
REMARK 3 ORIGIN FOR THE GROUP (A): 76.2089 41.3576 -29.8170
REMARK 3 T TENSOR
REMARK 3 T11: 0.2875 T22: 0.0391
REMARK 3 T33: -0.2921 T12: -0.0477
REMARK 3 T13: 0.2958 T23: -0.1672
REMARK 3 L TENSOR
REMARK 3 L11: 0.0309 L22: 0.0344
REMARK 3 L33: 0.0299 L12: 0.0070
REMARK 3 L13: 0.0313 L23: 0.0057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.1017 S13: 0.1695
REMARK 3 S21: 0.1952 S22: 0.0313 S23: -0.0004
REMARK 3 S31: -0.2040 S32: 0.0831 S33: -0.0037
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 4L06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080014.
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 : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141183
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.282
REMARK 200 RESOLUTION RANGE LOW (A) : 72.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.64300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG MME 2000, 100MM MES, PH
REMARK 280 6.9, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 48.11000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.85500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.27500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 137.85500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.11000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.27500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LEU A 416
REMARK 465 GLU A 417
REMARK 465 HIS A 418
REMARK 465 HIS A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 415
REMARK 465 LEU B 416
REMARK 465 GLU B 417
REMARK 465 HIS B 418
REMARK 465 HIS B 419
REMARK 465 HIS B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LEU C 414
REMARK 465 SER C 415
REMARK 465 LEU C 416
REMARK 465 GLU C 417
REMARK 465 HIS C 418
REMARK 465 HIS C 419
REMARK 465 HIS C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 HIS C 423
REMARK 465 HIS C 424
REMARK 465 HIS C 425
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 SER D 415
REMARK 465 LEU D 416
REMARK 465 GLU D 417
REMARK 465 HIS D 418
REMARK 465 HIS D 419
REMARK 465 HIS D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
REMARK 465 HIS D 423
REMARK 465 HIS D 424
REMARK 465 HIS D 425
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 LEU E 416
REMARK 465 GLU E 417
REMARK 465 HIS E 418
REMARK 465 HIS E 419
REMARK 465 HIS E 420
REMARK 465 HIS E 421
REMARK 465 HIS E 422
REMARK 465 HIS E 423
REMARK 465 HIS E 424
REMARK 465 HIS E 425
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 SER F 415
REMARK 465 LEU F 416
REMARK 465 GLU F 417
REMARK 465 HIS F 418
REMARK 465 HIS F 419
REMARK 465 HIS F 420
REMARK 465 HIS F 421
REMARK 465 HIS F 422
REMARK 465 HIS F 423
REMARK 465 HIS F 424
REMARK 465 HIS F 425
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 3 CG CD CE NZ
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 GLU A 174 CG CD OE1 OE2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 LYS A 236 CG CD CE NZ
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 GLU A 262 CG CD OE1 OE2
REMARK 470 LYS A 301 CD CE NZ
REMARK 470 LYS A 350 CG CD CE NZ
REMARK 470 LYS A 413 CG CD CE NZ
REMARK 470 LYS B 3 CG CD CE NZ
REMARK 470 GLU B 28 CG CD OE1 OE2
REMARK 470 GLU B 84 CG CD OE1 OE2
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 LYS B 89 CG CD CE NZ
REMARK 470 LYS B 115 CD CE NZ
REMARK 470 LYS B 151 CG CD CE NZ
REMARK 470 LYS B 321 CG CD CE NZ
REMARK 470 GLN B 323 CG CD OE1 NE2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 LYS B 381 CG CD CE NZ
REMARK 470 GLN B 411 CG CD OE1 NE2
REMARK 470 LYS B 413 CE NZ
REMARK 470 LEU B 414 CG CD1 CD2
REMARK 470 LYS C 3 CG CD CE NZ
REMARK 470 LYS C 4 CG CD CE NZ
REMARK 470 GLU C 174 CG CD OE1 OE2
REMARK 470 LYS C 233 CG CD CE NZ
REMARK 470 LYS C 350 CG CD CE NZ
REMARK 470 LYS D 4 CG CD CE NZ
REMARK 470 ILE D 5 CG1 CG2 CD1
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 ILE D 21 CG1 CG2 CD1
REMARK 470 PHE D 32 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 36 CG CD OE1 OE2
REMARK 470 ASP D 50 CG OD1 OD2
REMARK 470 LYS D 66 CG CD CE NZ
REMARK 470 GLU D 84 CG CD OE1 OE2
REMARK 470 GLU D 85 CG CD OE1 OE2
REMARK 470 LYS D 89 CG CD CE NZ
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 GLU D 229 CG CD OE1 OE2
REMARK 470 LYS D 233 CG CD CE NZ
REMARK 470 GLN D 234 CG CD OE1 NE2
REMARK 470 LYS D 301 CG CD CE NZ
REMARK 470 LYS D 350 CG CD CE NZ
REMARK 470 GLU D 351 CG CD OE1 OE2
REMARK 470 LYS D 406 CG CD CE NZ
REMARK 470 LYS D 408 CG CD CE NZ
REMARK 470 LEU D 409 CG CD1 CD2
REMARK 470 LYS D 413 CG CD CE NZ
REMARK 470 LEU D 414 CG CD1 CD2
REMARK 470 LYS E 3 CG CD CE NZ
REMARK 470 LYS E 4 CG CD CE NZ
REMARK 470 GLU E 174 CG CD OE1 OE2
REMARK 470 LYS E 233 CG CD CE NZ
REMARK 470 LYS E 243 CG CD CE NZ
REMARK 470 ASP E 299 CG OD1 OD2
REMARK 470 LYS E 301 CG CD CE NZ
REMARK 470 LYS E 345 CG CD CE NZ
REMARK 470 ASN E 348 CG OD1 ND2
REMARK 470 LYS E 350 CG CD CE NZ
REMARK 470 LYS E 413 CG CD CE NZ
REMARK 470 LYS F 3 CG CD CE NZ
REMARK 470 ASP F 299 CG OD1 OD2
REMARK 470 LYS F 301 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS D 29 OD1 ASP D 399 2.04
REMARK 500 OD2 ASP A 139 O HOH A 611 2.10
REMARK 500 N LYS C 3 O PRO C 33 2.12
REMARK 500 OE1 GLU F 324 NH1 ARG F 388 2.13
REMARK 500 OD2 ASP D 160 OG1 THR D 162 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 GLY F 382 C - N - CA ANGL. DEV. = 13.5 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 GLU A 17 -134.50 57.92
REMARK 500 ILE A 31 -71.88 -119.48
REMARK 500 ASP A 54 -1.56 71.47
REMARK 500 ASN A 68 -9.32 77.64
REMARK 500 ASP A 137 -135.12 57.85
REMARK 500 ILE A 215 -60.23 -91.60
REMARK 500 LYS A 301 -60.21 -124.98
REMARK 500 GLU B 17 -137.13 52.04
REMARK 500 ASP B 54 -2.34 71.31
REMARK 500 ASN B 68 -10.54 71.61
REMARK 500 ASP B 137 -133.00 47.47
REMARK 500 THR B 162 -71.41 -55.18
REMARK 500 ILE B 215 -60.06 -102.73
REMARK 500 GLN B 234 -62.48 -129.29
REMARK 500 LYS B 301 -59.70 -120.79
REMARK 500 GLU C 17 -138.72 57.06
REMARK 500 ASN C 68 -8.89 74.35
REMARK 500 ASP C 137 -128.80 55.49
REMARK 500 ILE C 215 -60.25 -100.73
REMARK 500 LYS C 301 -59.56 -130.40
REMARK 500 GLU D 17 -139.19 54.89
REMARK 500 ILE D 31 -63.11 -125.64
REMARK 500 ASP D 54 -2.68 70.84
REMARK 500 ASN D 68 -5.83 83.53
REMARK 500 LYS D 93 -143.65 58.41
REMARK 500 ASP D 137 -124.76 61.03
REMARK 500 ILE D 215 -62.52 -91.22
REMARK 500 GLN D 234 -65.16 -130.03
REMARK 500 GLU E 17 -136.03 57.08
REMARK 500 LEU E 30 -59.71 -127.67
REMARK 500 ASN E 68 -7.14 71.80
REMARK 500 ASP E 137 -137.68 57.46
REMARK 500 GLN E 234 -64.49 -131.52
REMARK 500 GLU F 17 -136.71 52.57
REMARK 500 LEU F 30 -60.62 -127.75
REMARK 500 ASP F 54 -1.90 68.42
REMARK 500 ASN F 68 -8.41 71.52
REMARK 500 ASP F 137 -135.05 57.02
REMARK 500 GLN F 234 -62.62 -128.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 160 GLY A 161 -109.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 252 OD2
REMARK 620 2 ASP B 275 OD1 68.6
REMARK 620 3 ASP B 275 O 93.2 62.5
REMARK 620 4 ASP B 279 OD1 106.7 120.8 58.8
REMARK 620 5 AKG B 503 O2 124.6 77.5 108.5 128.4
REMARK 620 6 AKG B 503 O5 69.7 80.6 143.0 156.3 62.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 275 OD1
REMARK 620 2 ASP A 275 O 64.9
REMARK 620 3 ASP A 279 OD1 123.1 61.4
REMARK 620 4 AKG A 503 O2 70.2 109.5 145.6
REMARK 620 5 AKG A 503 O5 74.2 138.3 149.3 60.5
REMARK 620 6 ASP B 252 OD1 76.6 87.4 83.8 130.4 75.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 252 OD2
REMARK 620 2 ASP D 275 OD1 68.7
REMARK 620 3 ASP D 275 O 94.9 63.8
REMARK 620 4 ASP D 279 OD2 109.3 135.7 72.6
REMARK 620 5 AKG D 503 O2 109.9 72.7 116.7 138.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 275 OD1
REMARK 620 2 ASP C 275 O 66.0
REMARK 620 3 ASP C 279 OD2 118.9 73.8
REMARK 620 4 AKG C 503 O2 74.2 116.4 166.7
REMARK 620 5 HOH C 610 O 140.3 150.2 78.8 89.2
REMARK 620 6 ASP D 252 OD2 68.7 98.3 73.9 111.2 85.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 252 OD1
REMARK 620 2 ASP F 275 OD1 73.6
REMARK 620 3 ASP F 275 O 87.9 66.3
REMARK 620 4 ASP F 279 OD2 92.5 160.9 100.9
REMARK 620 5 AKG F 503 O2 124.4 75.1 118.9 123.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 275 OD1
REMARK 620 2 ASP E 275 O 69.4
REMARK 620 3 ASP E 279 OD2 131.0 63.7
REMARK 620 4 AKG E 503 O2 84.7 119.2 130.3
REMARK 620 5 AKG E 503 O5 70.5 139.3 150.2 62.8
REMARK 620 6 HOH E 624 O 150.0 139.5 75.9 84.5 79.7
REMARK 620 7 ASP F 252 OD1 74.5 87.5 89.9 137.7 75.5 95.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG F 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KZO RELATED DB: PDB
REMARK 900 RELATED ID: 4L03 RELATED DB: PDB
REMARK 900 RELATED ID: 4L04 RELATED DB: PDB
DBREF 4L06 A 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 4L06 B 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 4L06 C 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 4L06 D 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 4L06 E 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 4L06 F 1 414 UNP O75874 IDHC_HUMAN 1 414
SEQADV 4L06 ASP A 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER A 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU A 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU A 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS A 425 UNP O75874 EXPRESSION TAG
SEQADV 4L06 ASP B 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER B 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU B 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU B 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS B 425 UNP O75874 EXPRESSION TAG
SEQADV 4L06 ASP C 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER C 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU C 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU C 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS C 425 UNP O75874 EXPRESSION TAG
SEQADV 4L06 ASP D 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER D 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU D 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU D 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS D 425 UNP O75874 EXPRESSION TAG
SEQADV 4L06 ASP E 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER E 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU E 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU E 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS E 425 UNP O75874 EXPRESSION TAG
SEQADV 4L06 ASP F 139 UNP O75874 TYR 139 ENGINEERED MUTATION
SEQADV 4L06 SER F 415 UNP O75874 EXPRESSION TAG
SEQADV 4L06 LEU F 416 UNP O75874 EXPRESSION TAG
SEQADV 4L06 GLU F 417 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 418 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 419 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 420 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 421 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 422 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 423 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 424 UNP O75874 EXPRESSION TAG
SEQADV 4L06 HIS F 425 UNP O75874 EXPRESSION TAG
SEQRES 1 A 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 A 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 A 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 A 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 A 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 A 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 A 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 A 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 A 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 A 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 A 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 A 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 A 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 A 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 A 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 A 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 A 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 A 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 A 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 A 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 A 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 A 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 A 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 A 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 A 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 A 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 A 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 A 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 A 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 A 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 A 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 A 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 A 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 B 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 B 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 B 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 B 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 B 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 B 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 B 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 B 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 B 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 B 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 B 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 B 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 B 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 B 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 B 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 B 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 B 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 B 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 B 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 B 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 B 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 B 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 B 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 B 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 B 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 B 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 B 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 B 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 B 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 B 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 B 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 B 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 C 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 C 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 C 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 C 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 C 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 C 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 C 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 C 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 C 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 C 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 C 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 C 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 C 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 C 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 C 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 C 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 C 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 C 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 C 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 C 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 C 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 C 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 C 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 C 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 C 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 C 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 C 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 C 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 C 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 C 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 C 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 C 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 D 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 D 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 D 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 D 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 D 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 D 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 D 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 D 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 D 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 D 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 D 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 D 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 D 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 D 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 D 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 D 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 D 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 D 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 D 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 D 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 D 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 D 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 D 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 D 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 D 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 D 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 D 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 D 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 D 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 D 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 D 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 D 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 E 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 E 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 E 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 E 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 E 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 E 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 E 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 E 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 E 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 E 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 E 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 E 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 E 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 E 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 E 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 E 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 E 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 E 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 E 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 E 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 E 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 E 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 E 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 E 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 E 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 E 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 E 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 E 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 E 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 E 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 E 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 E 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 F 425 MET SER LYS LYS ILE SER GLY GLY SER VAL VAL GLU MET
SEQRES 2 F 425 GLN GLY ASP GLU MET THR ARG ILE ILE TRP GLU LEU ILE
SEQRES 3 F 425 LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU LEU ASP LEU
SEQRES 4 F 425 HIS SER TYR ASP LEU GLY ILE GLU ASN ARG ASP ALA THR
SEQRES 5 F 425 ASN ASP GLN VAL THR LYS ASP ALA ALA GLU ALA ILE LYS
SEQRES 6 F 425 LYS HIS ASN VAL GLY VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 F 425 ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU LYS GLN MET
SEQRES 8 F 425 TRP LYS SER PRO ASN GLY THR ILE ARG ASN ILE LEU GLY
SEQRES 9 F 425 GLY THR VAL PHE ARG GLU ALA ILE ILE CYS LYS ASN ILE
SEQRES 10 F 425 PRO ARG LEU VAL SER GLY TRP VAL LYS PRO ILE ILE ILE
SEQRES 11 F 425 GLY ARG HIS ALA TYR GLY ASP GLN ASP ARG ALA THR ASP
SEQRES 12 F 425 PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU ILE THR TYR
SEQRES 13 F 425 THR PRO SER ASP GLY THR GLN LYS VAL THR TYR LEU VAL
SEQRES 14 F 425 HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA MET GLY MET
SEQRES 15 F 425 TYR ASN GLN ASP LYS SER ILE GLU ASP PHE ALA HIS SER
SEQRES 16 F 425 SER PHE GLN MET ALA LEU SER LYS GLY TRP PRO LEU TYR
SEQRES 17 F 425 LEU SER THR LYS ASN THR ILE LEU LYS LYS TYR ASP GLY
SEQRES 18 F 425 ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR ASP LYS GLN
SEQRES 19 F 425 TYR LYS SER GLN PHE GLU ALA GLN LYS ILE TRP TYR GLU
SEQRES 20 F 425 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN ALA MET LYS
SEQRES 21 F 425 SER GLU GLY GLY PHE ILE TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 F 425 GLY ASP VAL GLN SER ASP SER VAL ALA GLN GLY TYR GLY
SEQRES 23 F 425 SER LEU GLY MET MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 F 425 GLY LYS THR VAL GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 F 425 THR ARG HIS TYR ARG MET TYR GLN LYS GLY GLN GLU THR
SEQRES 26 F 425 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 F 425 GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN ASN LYS GLU
SEQRES 28 F 425 LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU VAL SER ILE
SEQRES 29 F 425 GLU THR ILE GLU ALA GLY PHE MET THR LYS ASP LEU ALA
SEQRES 30 F 425 ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN ARG SER ASP
SEQRES 31 F 425 TYR LEU ASN THR PHE GLU PHE MET ASP LYS LEU GLY GLU
SEQRES 32 F 425 ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS LEU SER LEU
SEQRES 33 F 425 GLU HIS HIS HIS HIS HIS HIS HIS HIS
HET CA A 501 1
HET NAP A 502 48
HET AKG A 503 10
HET CA B 501 1
HET NAP B 502 48
HET AKG B 503 10
HET CA C 501 1
HET NAP C 502 48
HET AKG C 503 10
HET CA D 501 1
HET NAP D 502 48
HET AKG D 503 10
HET CA E 501 1
HET NAP E 502 48
HET AKG E 503 10
HET CA F 501 1
HET NAP F 502 48
HET AKG F 503 10
HETNAM CA CALCIUM ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM AKG 2-OXOGLUTARIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 7 CA 6(CA 2+)
FORMUL 8 NAP 6(C21 H28 N7 O17 P3)
FORMUL 9 AKG 6(C5 H6 O5)
FORMUL 25 HOH *129(H2 O)
HELIX 1 1 ASP A 16 ILE A 31 1 16
HELIX 2 2 GLY A 45 THR A 52 1 8
HELIX 3 3 ASP A 54 ASN A 68 1 15
HELIX 4 4 ASP A 79 LYS A 87 1 9
HELIX 5 5 SER A 94 GLY A 104 1 11
HELIX 6 6 GLY A 136 ALA A 141 5 6
HELIX 7 7 ASP A 186 GLY A 204 1 19
HELIX 8 8 LYS A 218 GLN A 234 1 17
HELIX 9 9 TYR A 235 GLN A 242 1 8
HELIX 10 10 ILE A 251 SER A 261 1 11
HELIX 11 11 LYS A 270 TYR A 285 1 16
HELIX 12 12 VAL A 312 LYS A 321 1 10
HELIX 13 13 PRO A 329 ASN A 348 1 20
HELIX 14 14 ASN A 349 ALA A 369 1 21
HELIX 15 15 THR A 373 GLY A 382 1 10
HELIX 16 16 LEU A 383 VAL A 386 5 4
HELIX 17 17 GLN A 387 TYR A 391 5 5
HELIX 18 18 ASN A 393 LEU A 414 1 22
HELIX 19 19 ASP B 16 LEU B 30 1 15
HELIX 20 20 ILE B 31 PRO B 33 5 3
HELIX 21 21 GLY B 45 THR B 52 1 8
HELIX 22 22 ASP B 54 ASN B 68 1 15
HELIX 23 23 ASP B 79 LYS B 87 1 9
HELIX 24 24 SER B 94 GLY B 104 1 11
HELIX 25 25 GLY B 136 ALA B 141 5 6
HELIX 26 26 ASP B 186 GLY B 204 1 19
HELIX 27 27 LYS B 218 GLN B 234 1 17
HELIX 28 28 TYR B 235 GLN B 242 1 8
HELIX 29 29 ILE B 251 SER B 261 1 11
HELIX 30 30 LYS B 270 TYR B 285 1 16
HELIX 31 31 VAL B 312 GLN B 320 1 9
HELIX 32 32 PRO B 329 ASN B 348 1 20
HELIX 33 33 ASN B 349 ALA B 369 1 21
HELIX 34 34 THR B 373 GLY B 382 1 10
HELIX 35 35 LEU B 383 VAL B 386 5 4
HELIX 36 36 GLN B 387 TYR B 391 5 5
HELIX 37 37 ASN B 393 LEU B 414 1 22
HELIX 38 38 ASP C 16 LEU C 30 1 15
HELIX 39 39 GLY C 45 THR C 52 1 8
HELIX 40 40 ASP C 54 ASN C 68 1 15
HELIX 41 41 ASP C 79 LYS C 87 1 9
HELIX 42 42 SER C 94 GLY C 104 1 11
HELIX 43 43 GLY C 136 ALA C 141 5 6
HELIX 44 44 ASP C 186 GLY C 204 1 19
HELIX 45 45 LYS C 218 GLN C 234 1 17
HELIX 46 46 TYR C 235 GLN C 242 1 8
HELIX 47 47 ILE C 251 SER C 261 1 11
HELIX 48 48 LYS C 270 TYR C 285 1 16
HELIX 49 49 VAL C 312 LYS C 321 1 10
HELIX 50 50 PRO C 329 ASN C 348 1 20
HELIX 51 51 ASN C 349 ALA C 369 1 21
HELIX 52 52 THR C 373 GLY C 382 1 10
HELIX 53 53 LEU C 383 VAL C 386 5 4
HELIX 54 54 GLN C 387 TYR C 391 5 5
HELIX 55 55 ASN C 393 ALA C 412 1 20
HELIX 56 56 GLU D 17 LYS D 29 1 13
HELIX 57 57 GLY D 45 ASN D 53 1 9
HELIX 58 58 ASP D 54 ASN D 68 1 15
HELIX 59 59 ASP D 79 LYS D 87 1 9
HELIX 60 60 SER D 94 GLY D 104 1 11
HELIX 61 61 ASP D 186 GLY D 204 1 19
HELIX 62 62 LYS D 218 GLN D 234 1 17
HELIX 63 63 TYR D 235 GLN D 242 1 8
HELIX 64 64 ILE D 251 SER D 261 1 11
HELIX 65 65 LYS D 270 TYR D 285 1 16
HELIX 66 66 SER D 287 GLY D 289 5 3
HELIX 67 67 VAL D 312 LYS D 321 1 10
HELIX 68 68 PRO D 329 ASN D 348 1 20
HELIX 69 69 ASN D 349 ALA D 369 1 21
HELIX 70 70 THR D 373 GLY D 382 1 10
HELIX 71 71 GLN D 387 TYR D 391 5 5
HELIX 72 72 ASN D 393 GLN D 411 1 19
HELIX 73 73 ASP E 16 LEU E 30 1 15
HELIX 74 74 GLY E 45 THR E 52 1 8
HELIX 75 75 ASP E 54 ASN E 68 1 15
HELIX 76 76 ASP E 79 LYS E 87 1 9
HELIX 77 77 SER E 94 GLY E 104 1 11
HELIX 78 78 GLY E 136 ALA E 141 5 6
HELIX 79 79 ASP E 186 GLY E 204 1 19
HELIX 80 80 LYS E 218 GLN E 234 1 17
HELIX 81 81 TYR E 235 GLN E 242 1 8
HELIX 82 82 ILE E 251 SER E 261 1 11
HELIX 83 83 LYS E 270 TYR E 285 1 16
HELIX 84 84 VAL E 312 LYS E 321 1 10
HELIX 85 85 PRO E 329 ASN E 348 1 20
HELIX 86 86 ASN E 349 ALA E 369 1 21
HELIX 87 87 THR E 373 GLY E 382 1 10
HELIX 88 88 LEU E 383 VAL E 386 5 4
HELIX 89 89 GLN E 387 TYR E 391 5 5
HELIX 90 90 ASN E 393 LEU E 414 1 22
HELIX 91 91 ASP F 16 LEU F 30 1 15
HELIX 92 92 GLY F 45 THR F 52 1 8
HELIX 93 93 ASP F 54 ASN F 68 1 15
HELIX 94 94 ASP F 79 LYS F 87 1 9
HELIX 95 95 SER F 94 GLY F 104 1 11
HELIX 96 96 GLY F 136 ALA F 141 5 6
HELIX 97 97 ASP F 186 GLY F 204 1 19
HELIX 98 98 LYS F 218 GLN F 234 1 17
HELIX 99 99 TYR F 235 GLN F 242 1 8
HELIX 100 100 ILE F 251 LYS F 260 1 10
HELIX 101 101 LYS F 270 TYR F 285 1 16
HELIX 102 102 SER F 287 GLY F 289 5 3
HELIX 103 103 VAL F 312 LYS F 321 1 10
HELIX 104 104 PRO F 329 ASN F 348 1 20
HELIX 105 105 ASN F 349 ALA F 369 1 21
HELIX 106 106 THR F 373 GLY F 382 1 10
HELIX 107 107 GLN F 387 TYR F 391 5 5
HELIX 108 108 ASN F 393 LYS F 413 1 21
SHEET 1 A10 VAL A 35 ASP A 43 0
SHEET 2 A10 ILE A 5 GLN A 14 1 N ILE A 5 O GLU A 36
SHEET 3 A10 VAL A 69 LYS A 72 1 O VAL A 71 N VAL A 11
SHEET 4 A10 VAL A 303 GLU A 306 1 O ALA A 305 N GLY A 70
SHEET 5 A10 MET A 291 VAL A 296 -1 N LEU A 295 O GLU A 304
SHEET 6 A10 THR A 106 ALA A 111 -1 N THR A 106 O VAL A 296
SHEET 7 A10 ILE A 128 HIS A 133 -1 O ARG A 132 N VAL A 107
SHEET 8 A10 PHE A 265 CYS A 269 1 O CYS A 269 N GLY A 131
SHEET 9 A10 LEU A 207 THR A 211 1 N TYR A 208 O ALA A 268
SHEET 10 A10 TYR A 246 LEU A 250 1 O ARG A 249 N LEU A 209
SHEET 1 B 4 THR A 142 VAL A 146 0
SHEET 2 B 4 GLY A 177 GLN A 185 -1 O GLY A 181 N THR A 142
SHEET 3 B 4 GLY B 177 GLN B 185 -1 O MET B 180 N MET A 182
SHEET 4 B 4 THR B 142 VAL B 146 -1 N VAL B 146 O GLY B 177
SHEET 1 C 8 VAL B 165 PHE B 172 0
SHEET 2 C 8 GLY B 150 PRO B 158 -1 N ILE B 154 O TYR B 167
SHEET 3 C 8 GLY A 150 PRO A 158 -1 N GLU A 153 O THR B 155
SHEET 4 C 8 GLN A 163 PHE A 172 -1 O PHE A 172 N GLY A 150
SHEET 5 C 8 GLN C 163 PHE C 172 -1 O LYS C 164 N THR A 166
SHEET 6 C 8 GLY C 150 PRO C 158 -1 N GLY C 150 O PHE C 172
SHEET 7 C 8 GLY D 150 PRO D 158 -1 O THR D 155 N GLU C 153
SHEET 8 C 8 VAL D 165 PHE D 172 -1 O PHE D 172 N GLY D 150
SHEET 1 D10 VAL B 35 ASP B 43 0
SHEET 2 D10 ILE B 5 GLN B 14 1 N GLY B 7 O GLU B 36
SHEET 3 D10 VAL B 69 LYS B 72 1 O VAL B 71 N VAL B 11
SHEET 4 D10 VAL B 303 GLU B 306 1 O ALA B 305 N GLY B 70
SHEET 5 D10 MET B 291 VAL B 296 -1 N LEU B 295 O GLU B 304
SHEET 6 D10 THR B 106 ALA B 111 -1 N GLU B 110 O THR B 292
SHEET 7 D10 ILE B 128 HIS B 133 -1 O ARG B 132 N VAL B 107
SHEET 8 D10 PHE B 265 CYS B 269 1 O TRP B 267 N ILE B 129
SHEET 9 D10 LEU B 207 THR B 211 1 N TYR B 208 O ALA B 268
SHEET 10 D10 TYR B 246 LEU B 250 1 O ARG B 249 N LEU B 209
SHEET 1 E10 VAL C 35 ASP C 43 0
SHEET 2 E10 ILE C 5 GLN C 14 1 N ILE C 5 O GLU C 36
SHEET 3 E10 VAL C 69 LYS C 72 1 O VAL C 69 N VAL C 11
SHEET 4 E10 VAL C 303 GLU C 306 1 O ALA C 305 N GLY C 70
SHEET 5 E10 MET C 291 VAL C 296 -1 N LEU C 295 O GLU C 304
SHEET 6 E10 THR C 106 ALA C 111 -1 N THR C 106 O VAL C 296
SHEET 7 E10 ILE C 129 HIS C 133 -1 O ARG C 132 N VAL C 107
SHEET 8 E10 ILE C 266 CYS C 269 1 O TRP C 267 N ILE C 129
SHEET 9 E10 LEU C 207 THR C 211 1 N TYR C 208 O ALA C 268
SHEET 10 E10 TYR C 246 LEU C 250 1 O ARG C 249 N LEU C 209
SHEET 1 F 4 THR C 142 VAL C 146 0
SHEET 2 F 4 GLY C 177 GLN C 185 -1 O GLY C 181 N THR C 142
SHEET 3 F 4 GLY D 177 GLN D 185 -1 O ASN D 184 N VAL C 178
SHEET 4 F 4 THR D 142 VAL D 146 -1 N THR D 142 O GLY D 181
SHEET 1 G10 VAL D 35 ASP D 43 0
SHEET 2 G10 ILE D 5 GLN D 14 1 N GLU D 12 O HIS D 40
SHEET 3 G10 GLY D 70 LYS D 72 1 O VAL D 71 N MET D 13
SHEET 4 G10 VAL D 303 GLU D 306 1 O ALA D 305 N GLY D 70
SHEET 5 G10 MET D 291 VAL D 296 -1 N LEU D 295 O GLU D 304
SHEET 6 G10 THR D 106 ALA D 111 -1 N THR D 106 O VAL D 296
SHEET 7 G10 ILE D 128 HIS D 133 -1 O ARG D 132 N VAL D 107
SHEET 8 G10 PHE D 265 CYS D 269 1 O CYS D 269 N GLY D 131
SHEET 9 G10 LEU D 207 THR D 211 1 N TYR D 208 O ALA D 268
SHEET 10 G10 TYR D 246 LEU D 250 1 O ARG D 249 N LEU D 209
SHEET 1 H10 VAL E 35 ASP E 43 0
SHEET 2 H10 ILE E 5 GLN E 14 1 N GLY E 7 O GLU E 36
SHEET 3 H10 VAL E 69 LYS E 72 1 O VAL E 71 N VAL E 11
SHEET 4 H10 VAL E 303 GLU E 306 1 O ALA E 305 N LYS E 72
SHEET 5 H10 MET E 291 VAL E 296 -1 N LEU E 295 O GLU E 304
SHEET 6 H10 THR E 106 ALA E 111 -1 N THR E 106 O VAL E 296
SHEET 7 H10 ILE E 128 HIS E 133 -1 O ILE E 130 N ARG E 109
SHEET 8 H10 PHE E 265 CYS E 269 1 O TRP E 267 N ILE E 129
SHEET 9 H10 LEU E 207 THR E 211 1 N TYR E 208 O ALA E 268
SHEET 10 H10 TYR E 246 LEU E 250 1 O ARG E 249 N LEU E 209
SHEET 1 I 4 THR E 142 VAL E 146 0
SHEET 2 I 4 GLY E 177 GLN E 185 -1 O GLY E 177 N VAL E 146
SHEET 3 I 4 GLY F 177 GLN F 185 -1 O MET F 182 N MET E 180
SHEET 4 I 4 THR F 142 VAL F 146 -1 N VAL F 146 O GLY F 177
SHEET 1 J 4 VAL E 165 PHE E 172 0
SHEET 2 J 4 GLY E 150 PRO E 158 -1 N ILE E 154 O TYR E 167
SHEET 3 J 4 GLY F 150 PRO F 158 -1 O THR F 155 N GLU E 153
SHEET 4 J 4 VAL F 165 PHE F 172 -1 O TYR F 167 N ILE F 154
SHEET 1 K10 VAL F 35 ASP F 43 0
SHEET 2 K10 ILE F 5 GLN F 14 1 N ILE F 5 O GLU F 36
SHEET 3 K10 VAL F 69 LYS F 72 1 O VAL F 71 N VAL F 11
SHEET 4 K10 VAL F 303 GLU F 306 1 O ALA F 305 N GLY F 70
SHEET 5 K10 MET F 291 VAL F 296 -1 N LEU F 295 O GLU F 304
SHEET 6 K10 THR F 106 ALA F 111 -1 N PHE F 108 O VAL F 294
SHEET 7 K10 ILE F 128 HIS F 133 -1 O ARG F 132 N VAL F 107
SHEET 8 K10 PHE F 265 CYS F 269 1 O TRP F 267 N ILE F 129
SHEET 9 K10 LEU F 207 THR F 211 1 N TYR F 208 O ALA F 268
SHEET 10 K10 TYR F 246 LEU F 250 1 O ARG F 249 N LEU F 209
LINK OD2 ASP A 252 CA CA B 501 1555 1555 2.48
LINK OD1 ASP A 275 CA CA A 501 1555 1555 2.24
LINK O ASP A 275 CA CA A 501 1555 1555 3.04
LINK OD1 ASP A 279 CA CA A 501 1555 1555 2.49
LINK CA CA A 501 O2 AKG A 503 1555 1555 2.36
LINK CA CA A 501 O5 AKG A 503 1555 1555 2.97
LINK CA CA A 501 OD1 ASP B 252 1555 1555 2.21
LINK OD1 ASP B 275 CA CA B 501 1555 1555 2.30
LINK O ASP B 275 CA CA B 501 1555 1555 3.13
LINK OD1 ASP B 279 CA CA B 501 1555 1555 2.24
LINK CA CA B 501 O2 AKG B 503 1555 1555 2.40
LINK CA CA B 501 O5 AKG B 503 1555 1555 2.87
LINK OD2 ASP C 252 CA CA D 501 1555 1555 2.55
LINK OD1 ASP C 275 CA CA C 501 1555 1555 2.29
LINK O ASP C 275 CA CA C 501 1555 1555 3.04
LINK OD2 ASP C 279 CA CA C 501 1555 1555 2.51
LINK CA CA C 501 O2 AKG C 503 1555 1555 2.37
LINK CA CA C 501 O HOH C 610 1555 1555 2.52
LINK CA CA C 501 OD2 ASP D 252 1555 1555 2.63
LINK OD1 ASP D 275 CA CA D 501 1555 1555 2.30
LINK O ASP D 275 CA CA D 501 1555 1555 2.92
LINK OD2 ASP D 279 CA CA D 501 1555 1555 2.26
LINK CA CA D 501 O2 AKG D 503 1555 1555 2.33
LINK OD1 ASP E 252 CA CA F 501 1555 1555 2.34
LINK OD1 ASP E 275 CA CA E 501 1555 1555 2.32
LINK O ASP E 275 CA CA E 501 1555 1555 2.98
LINK OD2 ASP E 279 CA CA E 501 1555 1555 2.41
LINK CA CA E 501 O2 AKG E 503 1555 1555 2.23
LINK CA CA E 501 O5 AKG E 503 1555 1555 2.96
LINK CA CA E 501 O HOH E 624 1555 1555 2.41
LINK CA CA E 501 OD1 ASP F 252 1555 1555 2.28
LINK OD1 ASP F 275 CA CA F 501 1555 1555 2.40
LINK O ASP F 275 CA CA F 501 1555 1555 2.82
LINK OD2 ASP F 279 CA CA F 501 1555 1555 2.92
LINK CA CA F 501 O2 AKG F 503 1555 1555 2.35
SITE 1 AC1 4 ASP A 275 ASP A 279 AKG A 503 ASP B 252
SITE 1 AC2 28 LYS A 72 ALA A 74 THR A 75 ILE A 76
SITE 2 AC2 28 THR A 77 ARG A 82 ASN A 96 LEU A 288
SITE 3 AC2 28 ALA A 307 HIS A 309 GLY A 310 THR A 311
SITE 4 AC2 28 VAL A 312 THR A 313 ARG A 314 HIS A 315
SITE 5 AC2 28 ASN A 328 AKG A 503 HOH A 607 HOH A 608
SITE 6 AC2 28 HOH A 609 HOH A 610 HOH A 640 HOH A 641
SITE 7 AC2 28 LEU B 250 ASP B 253 GLN B 257 LYS B 260
SITE 1 AC3 12 THR A 77 SER A 94 ASN A 96 ARG A 100
SITE 2 AC3 12 ARG A 109 ARG A 132 ASP A 275 CA A 501
SITE 3 AC3 12 NAP A 502 HOH A 607 HOH A 627 ASP B 252
SITE 1 AC4 4 ASP A 252 ASP B 275 ASP B 279 AKG B 503
SITE 1 AC5 23 LEU A 250 ASP A 253 GLN A 257 LYS A 260
SITE 2 AC5 23 LYS B 72 ALA B 74 THR B 75 THR B 77
SITE 3 AC5 23 ARG B 82 ASN B 96 LEU B 288 ALA B 307
SITE 4 AC5 23 HIS B 309 GLY B 310 THR B 311 VAL B 312
SITE 5 AC5 23 ARG B 314 HIS B 315 THR B 327 ASN B 328
SITE 6 AC5 23 AKG B 503 HOH B 613 HOH B 614
SITE 1 AC6 11 ASP A 252 THR B 77 SER B 94 ASN B 96
SITE 2 AC6 11 ARG B 100 ARG B 109 ARG B 132 ASP B 275
SITE 3 AC6 11 ALA B 308 CA B 501 NAP B 502
SITE 1 AC7 5 ASP C 275 ASP C 279 AKG C 503 HOH C 610
SITE 2 AC7 5 ASP D 252
SITE 1 AC8 24 LYS C 72 ALA C 74 THR C 75 ILE C 76
SITE 2 AC8 24 THR C 77 ARG C 82 ASN C 96 ALA C 307
SITE 3 AC8 24 ALA C 308 HIS C 309 GLY C 310 THR C 311
SITE 4 AC8 24 VAL C 312 THR C 313 ARG C 314 HIS C 315
SITE 5 AC8 24 ASN C 328 AKG C 503 HOH C 604 HOH C 614
SITE 6 AC8 24 LEU D 250 ASP D 253 GLN D 257 LYS D 260
SITE 1 AC9 13 THR C 77 SER C 94 ASN C 96 ARG C 100
SITE 2 AC9 13 ARG C 109 ARG C 132 ASP C 275 ALA C 308
SITE 3 AC9 13 CA C 501 NAP C 502 LYS D 212 ILE D 215
SITE 4 AC9 13 ASP D 252
SITE 1 BC1 5 ASP C 252 ARG D 109 ASP D 275 ASP D 279
SITE 2 BC1 5 AKG D 503
SITE 1 BC2 19 ASP C 253 GLN C 257 LYS C 260 LYS D 72
SITE 2 BC2 19 ALA D 74 THR D 75 THR D 77 ARG D 82
SITE 3 BC2 19 ASN D 96 ALA D 307 ALA D 308 HIS D 309
SITE 4 BC2 19 GLY D 310 THR D 311 VAL D 312 ARG D 314
SITE 5 BC2 19 HIS D 315 ASN D 328 AKG D 503
SITE 1 BC3 11 ASP C 252 THR D 77 SER D 94 ASN D 96
SITE 2 BC3 11 ARG D 100 ARG D 109 ARG D 132 ASP D 275
SITE 3 BC3 11 ALA D 308 CA D 501 NAP D 502
SITE 1 BC4 5 ASP E 275 ASP E 279 AKG E 503 HOH E 624
SITE 2 BC4 5 ASP F 252
SITE 1 BC5 25 LYS E 72 ALA E 74 THR E 75 ILE E 76
SITE 2 BC5 25 THR E 77 ARG E 82 ASN E 96 LEU E 288
SITE 3 BC5 25 ALA E 307 HIS E 309 GLY E 310 THR E 311
SITE 4 BC5 25 VAL E 312 THR E 313 ARG E 314 HIS E 315
SITE 5 BC5 25 THR E 327 ASN E 328 AKG E 503 HOH E 610
SITE 6 BC5 25 HOH E 618 LEU F 250 ASP F 253 GLN F 257
SITE 7 BC5 25 LYS F 260
SITE 1 BC6 12 THR E 77 SER E 94 ASN E 96 ARG E 100
SITE 2 BC6 12 ARG E 109 ARG E 132 ASP E 275 ALA E 308
SITE 3 BC6 12 CA E 501 NAP E 502 LYS F 212 ASP F 252
SITE 1 BC7 4 ASP E 252 ASP F 275 ASP F 279 AKG F 503
SITE 1 BC8 23 LEU E 250 ASP E 253 GLN E 257 LYS E 260
SITE 2 BC8 23 LYS F 72 ALA F 74 THR F 75 ILE F 76
SITE 3 BC8 23 THR F 77 ARG F 82 ASN F 96 ALA F 307
SITE 4 BC8 23 HIS F 309 GLY F 310 THR F 311 VAL F 312
SITE 5 BC8 23 THR F 313 ARG F 314 HIS F 315 ASN F 328
SITE 6 BC8 23 AKG F 503 HOH F 602 HOH F 609
SITE 1 BC9 11 ASP E 252 THR F 77 SER F 94 ASN F 96
SITE 2 BC9 11 ARG F 100 ARG F 109 ARG F 132 ASP F 275
SITE 3 BC9 11 ALA F 308 CA F 501 NAP F 502
CRYST1 96.220 116.550 275.710 90.00 90.00 90.00 P 21 21 21 24
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 0.010393 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003627 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
