HEADER TRANSFERASE/PROTEIN BINDING 04-SEP-13 4MJS
TITLE CRYSTAL STRUCTURE OF A PB1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C ZETA TYPE;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W;
COMPND 4 FRAGMENT: PB1 DOMAIN, UNP RESIDUES 15-101;
COMPND 5 SYNONYM: NPKC-ZETA;
COMPND 6 EC: 2.7.11.13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SEQUESTOSOME-1;
COMPND 10 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X;
COMPND 11 FRAGMENT: PB1 DOMAIN, UNP RESIDUES 3-102;
COMPND 12 SYNONYM: EBI3-ASSOCIATED PROTEIN OF 60 KDA, EBIAP, P60,
COMPND 13 PHOSPHOTYROSINE-INDEPENDENT LIGAND FOR THE LCK SH2 DOMAIN OF 62 KDA,
COMPND 14 UBIQUITIN-BINDING PROTEIN P62;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PKCZ, PRKCZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ORCA, OSIL, SQSTM1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PACYCDUET
KEYWDS PB1 DOMAIN, PB1 HETERODIMER AND PROTEIN INTERACTION, TRANSFERASE-
KEYWDS 2 PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.REN,Z.X.WANG,J.W.WU
REVDAT 2 29-OCT-14 4MJS 1 JRNL
REVDAT 1 27-AUG-14 4MJS 0
JRNL AUTH J.REN,J.WANG,Z.X.WANG,J.W.WU
JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO THE HOMOTYPIC
JRNL TITL 2 PB1-PB1 COMPLEX BETWEEN PKC ZETA AND P62
JRNL REF SCI CHINA LIFE SCI V. 57 69 2014
JRNL REFN ISSN 1674-7305
JRNL PMID 24369353
JRNL DOI 10.1007/S11427-013-4592-Z
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 105316
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5264
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 39.5385 - 7.7492 0.98 3540 184 0.2323 0.2770
REMARK 3 2 7.7492 - 6.1583 1.00 3424 189 0.2674 0.2649
REMARK 3 3 6.1583 - 5.3820 1.00 3405 186 0.2721 0.3029
REMARK 3 4 5.3820 - 4.8909 1.00 3395 183 0.2086 0.2392
REMARK 3 5 4.8909 - 4.5409 1.00 3354 187 0.1867 0.2196
REMARK 3 6 4.5409 - 4.2735 1.00 3367 169 0.1871 0.2451
REMARK 3 7 4.2735 - 4.0597 1.00 3352 182 0.2050 0.2546
REMARK 3 8 4.0597 - 3.8832 1.00 3342 173 0.2153 0.2636
REMARK 3 9 3.8832 - 3.7338 1.00 3354 161 0.2171 0.2817
REMARK 3 10 3.7338 - 3.6050 1.00 3348 172 0.2360 0.2533
REMARK 3 11 3.6050 - 3.4924 1.00 3341 189 0.2529 0.3239
REMARK 3 12 3.4924 - 3.3926 1.00 3288 168 0.2437 0.2868
REMARK 3 13 3.3926 - 3.3033 1.00 3341 166 0.2489 0.3222
REMARK 3 14 3.3033 - 3.2228 1.00 3354 164 0.2459 0.2784
REMARK 3 15 3.2228 - 3.1495 1.00 3296 170 0.2572 0.3235
REMARK 3 16 3.1495 - 3.0825 1.00 3320 159 0.2578 0.3449
REMARK 3 17 3.0825 - 3.0209 1.00 3314 187 0.2587 0.3051
REMARK 3 18 3.0209 - 2.9639 1.00 3308 164 0.2493 0.3287
REMARK 3 19 2.9639 - 2.9110 1.00 3347 176 0.2609 0.3119
REMARK 3 20 2.9110 - 2.8617 1.00 3273 187 0.2675 0.3369
REMARK 3 21 2.8617 - 2.8155 1.00 3289 190 0.2703 0.3427
REMARK 3 22 2.8155 - 2.7722 1.00 3297 148 0.2635 0.3007
REMARK 3 23 2.7722 - 2.7315 1.00 3322 192 0.2807 0.3402
REMARK 3 24 2.7315 - 2.6930 1.00 3319 150 0.2827 0.3658
REMARK 3 25 2.6930 - 2.6566 1.00 3282 198 0.2721 0.3309
REMARK 3 26 2.6566 - 2.6221 1.00 3294 181 0.2715 0.3557
REMARK 3 27 2.6221 - 2.5893 1.00 3262 185 0.2621 0.3307
REMARK 3 28 2.5893 - 2.5582 1.00 3334 173 0.2607 0.3489
REMARK 3 29 2.5582 - 2.5284 1.00 3275 166 0.2657 0.3173
REMARK 3 30 2.5284 - 2.5000 1.00 3315 165 0.2741 0.3813
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 30.28
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.450
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) : 1.15690
REMARK 3 B22 (A**2) : -1.51230
REMARK 3 B33 (A**2) : 4.06580
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 16736
REMARK 3 ANGLE : 1.200 22511
REMARK 3 CHIRALITY : 0.078 2499
REMARK 3 PLANARITY : 0.005 2882
REMARK 3 DIHEDRAL : 17.137 6270
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 4MJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB081998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97892
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105401
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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: PDB ENTRY 1WMH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 8% PEG8000, 0.4M MGCL2,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 42.85750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 129.77950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.84050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 129.77950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.85750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.84050
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, 4, 5, 6, 7, 8, 9, 10, 11, 12
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 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 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 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X
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 GLY A 11
REMARK 465 PRO A 33
REMARK 465 GLU A 101
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 HIS B 1
REMARK 465 MET B 2
REMARK 465 SER B 3
REMARK 465 GLY B 12
REMARK 465 LYS B 13
REMARK 465 GLU B 14
REMARK 465 CYS B 27
REMARK 465 SER B 28
REMARK 465 PRO B 29
REMARK 465 GLU B 30
REMARK 465 PRO B 31
REMARK 465 GLU B 32
REMARK 465 ALA B 33
REMARK 465 GLU B 34
REMARK 465 ALA B 35
REMARK 465 GLU B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 ALA B 39
REMARK 465 GLY B 40
REMARK 465 GLY C 11
REMARK 465 PRO C 33
REMARK 465 GLU C 101
REMARK 465 GLY D -1
REMARK 465 PRO D 0
REMARK 465 HIS D 1
REMARK 465 MET D 2
REMARK 465 GLY D 12
REMARK 465 LYS D 13
REMARK 465 GLU D 14
REMARK 465 CYS D 27
REMARK 465 SER D 28
REMARK 465 PRO D 29
REMARK 465 GLU D 30
REMARK 465 PRO D 31
REMARK 465 GLU D 32
REMARK 465 ALA D 33
REMARK 465 GLU D 34
REMARK 465 ALA D 35
REMARK 465 GLU D 36
REMARK 465 ALA D 37
REMARK 465 ALA D 38
REMARK 465 ALA D 39
REMARK 465 GLY D 40
REMARK 465 GLY E 11
REMARK 465 PRO E 33
REMARK 465 GLU E 101
REMARK 465 GLY F -1
REMARK 465 PRO F 0
REMARK 465 HIS F 1
REMARK 465 MET F 2
REMARK 465 GLY F 12
REMARK 465 LYS F 13
REMARK 465 GLU F 14
REMARK 465 CYS F 27
REMARK 465 SER F 28
REMARK 465 PRO F 29
REMARK 465 GLU F 30
REMARK 465 PRO F 31
REMARK 465 GLU F 32
REMARK 465 ALA F 33
REMARK 465 GLU F 34
REMARK 465 ALA F 35
REMARK 465 GLU F 36
REMARK 465 ALA F 37
REMARK 465 ALA F 38
REMARK 465 ALA F 39
REMARK 465 GLY F 40
REMARK 465 GLY G 11
REMARK 465 PRO G 33
REMARK 465 GLU G 101
REMARK 465 GLY H -1
REMARK 465 PRO H 0
REMARK 465 HIS H 1
REMARK 465 MET H 2
REMARK 465 LYS H 13
REMARK 465 GLU H 14
REMARK 465 CYS H 27
REMARK 465 SER H 28
REMARK 465 PRO H 29
REMARK 465 GLU H 30
REMARK 465 PRO H 31
REMARK 465 GLU H 32
REMARK 465 ALA H 33
REMARK 465 GLU H 34
REMARK 465 ALA H 35
REMARK 465 GLU H 36
REMARK 465 ALA H 37
REMARK 465 ALA H 38
REMARK 465 ALA H 39
REMARK 465 GLY H 40
REMARK 465 GLY I 11
REMARK 465 PRO I 33
REMARK 465 GLU I 101
REMARK 465 GLY J -1
REMARK 465 PRO J 0
REMARK 465 HIS J 1
REMARK 465 MET J 2
REMARK 465 SER J 28
REMARK 465 PRO J 29
REMARK 465 GLU J 30
REMARK 465 PRO J 31
REMARK 465 GLU J 32
REMARK 465 ALA J 33
REMARK 465 GLU J 34
REMARK 465 ALA J 35
REMARK 465 GLU J 36
REMARK 465 ALA J 37
REMARK 465 ALA J 38
REMARK 465 ALA J 39
REMARK 465 GLY J 40
REMARK 465 GLY K 11
REMARK 465 PRO K 33
REMARK 465 GLU K 101
REMARK 465 GLY L -1
REMARK 465 PRO L 0
REMARK 465 HIS L 1
REMARK 465 MET L 2
REMARK 465 CYS L 27
REMARK 465 SER L 28
REMARK 465 PRO L 29
REMARK 465 GLU L 30
REMARK 465 PRO L 31
REMARK 465 GLU L 32
REMARK 465 ALA L 33
REMARK 465 GLU L 34
REMARK 465 ALA L 35
REMARK 465 GLU L 36
REMARK 465 ALA L 37
REMARK 465 ALA L 38
REMARK 465 ALA L 39
REMARK 465 GLY L 40
REMARK 465 GLY M 11
REMARK 465 PRO M 33
REMARK 465 GLU M 101
REMARK 465 GLY N -1
REMARK 465 PRO N 0
REMARK 465 HIS N 1
REMARK 465 MET N 2
REMARK 465 GLY N 12
REMARK 465 LYS N 13
REMARK 465 GLU N 14
REMARK 465 CYS N 27
REMARK 465 SER N 28
REMARK 465 PRO N 29
REMARK 465 GLU N 30
REMARK 465 PRO N 31
REMARK 465 GLU N 32
REMARK 465 ALA N 33
REMARK 465 GLU N 34
REMARK 465 ALA N 35
REMARK 465 GLU N 36
REMARK 465 ALA N 37
REMARK 465 ALA N 38
REMARK 465 ALA N 39
REMARK 465 GLY N 40
REMARK 465 GLY O 11
REMARK 465 PRO O 33
REMARK 465 GLU O 101
REMARK 465 GLY P -1
REMARK 465 PRO P 0
REMARK 465 HIS P 1
REMARK 465 MET P 2
REMARK 465 SER P 3
REMARK 465 GLY P 12
REMARK 465 LYS P 13
REMARK 465 GLU P 14
REMARK 465 CYS P 27
REMARK 465 SER P 28
REMARK 465 PRO P 29
REMARK 465 GLU P 30
REMARK 465 PRO P 31
REMARK 465 GLU P 32
REMARK 465 ALA P 33
REMARK 465 GLU P 34
REMARK 465 ALA P 35
REMARK 465 GLU P 36
REMARK 465 ALA P 37
REMARK 465 ALA P 38
REMARK 465 ALA P 39
REMARK 465 GLY P 40
REMARK 465 PRO P 41
REMARK 465 GLY Q 11
REMARK 465 PRO Q 33
REMARK 465 GLU Q 101
REMARK 465 GLY R -1
REMARK 465 PRO R 0
REMARK 465 HIS R 1
REMARK 465 MET R 2
REMARK 465 LYS R 13
REMARK 465 GLU R 14
REMARK 465 CYS R 27
REMARK 465 SER R 28
REMARK 465 PRO R 29
REMARK 465 GLU R 30
REMARK 465 PRO R 31
REMARK 465 GLU R 32
REMARK 465 ALA R 33
REMARK 465 GLU R 34
REMARK 465 ALA R 35
REMARK 465 GLU R 36
REMARK 465 ALA R 37
REMARK 465 ALA R 38
REMARK 465 ALA R 39
REMARK 465 GLY R 40
REMARK 465 GLY S 11
REMARK 465 PRO S 33
REMARK 465 GLU S 101
REMARK 465 GLY T -1
REMARK 465 PRO T 0
REMARK 465 HIS T 1
REMARK 465 MET T 2
REMARK 465 GLY T 12
REMARK 465 LYS T 13
REMARK 465 GLU T 14
REMARK 465 CYS T 27
REMARK 465 SER T 28
REMARK 465 PRO T 29
REMARK 465 GLU T 30
REMARK 465 PRO T 31
REMARK 465 GLU T 32
REMARK 465 ALA T 33
REMARK 465 GLU T 34
REMARK 465 ALA T 35
REMARK 465 GLU T 36
REMARK 465 ALA T 37
REMARK 465 ALA T 38
REMARK 465 ALA T 39
REMARK 465 GLY T 40
REMARK 465 GLY U 11
REMARK 465 PRO U 33
REMARK 465 GLU U 101
REMARK 465 GLY V -1
REMARK 465 PRO V 0
REMARK 465 HIS V 1
REMARK 465 MET V 2
REMARK 465 SER V 3
REMARK 465 GLY V 12
REMARK 465 LYS V 13
REMARK 465 GLU V 14
REMARK 465 CYS V 26
REMARK 465 CYS V 27
REMARK 465 SER V 28
REMARK 465 PRO V 29
REMARK 465 GLU V 30
REMARK 465 PRO V 31
REMARK 465 GLU V 32
REMARK 465 ALA V 33
REMARK 465 GLU V 34
REMARK 465 ALA V 35
REMARK 465 GLU V 36
REMARK 465 ALA V 37
REMARK 465 ALA V 38
REMARK 465 ALA V 39
REMARK 465 GLY V 40
REMARK 465 LYS V 102
REMARK 465 GLY W 11
REMARK 465 PRO W 33
REMARK 465 GLU W 101
REMARK 465 GLY X -1
REMARK 465 PRO X 0
REMARK 465 HIS X 1
REMARK 465 SER X 28
REMARK 465 PRO X 29
REMARK 465 GLU X 30
REMARK 465 PRO X 31
REMARK 465 GLU X 32
REMARK 465 ALA X 33
REMARK 465 GLU X 34
REMARK 465 ALA X 35
REMARK 465 GLU X 36
REMARK 465 ALA X 37
REMARK 465 ALA X 38
REMARK 465 ALA X 39
REMARK 465 GLY X 40
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA B 16 -179.78 -64.22
REMARK 500 PHE B 25 126.35 -170.63
REMARK 500 SER B 78 3.65 -153.93
REMARK 500 ASP B 93 2.63 90.38
REMARK 500 SER D 78 10.58 -142.37
REMARK 500 LYS D 91 -64.84 -98.66
REMARK 500 ASP D 93 7.02 -59.97
REMARK 500 SER H 78 -0.27 -148.58
REMARK 500 GLU J 14 98.53 -69.08
REMARK 500 SER J 78 19.36 -147.78
REMARK 500 TYR J 89 -62.87 -96.93
REMARK 500 ASP J 93 6.57 81.22
REMARK 500 ARG K 87 16.00 58.54
REMARK 500 LYS L 13 -136.77 47.32
REMARK 500 SER L 78 -1.15 -142.23
REMARK 500 SER N 78 -2.19 -152.04
REMARK 500 LYS N 91 51.15 -118.98
REMARK 500 ALA P 16 -164.05 -102.07
REMARK 500 TYR P 67 -156.36 -128.70
REMARK 500 ALA P 69 -162.31 -103.95
REMARK 500 ARG P 71 36.89 -78.65
REMARK 500 MET P 87 11.33 -69.02
REMARK 500 ASP P 93 -1.79 79.20
REMARK 500 SER R 78 23.32 -153.80
REMARK 500 ASP R 92 -9.94 -59.62
REMARK 500 SER S 63 -5.85 -59.51
REMARK 500 ARG S 87 69.06 38.94
REMARK 500 SER U 71 27.78 -140.34
REMARK 500 ARG U 87 71.88 45.25
REMARK 500 SER V 78 -43.94 -149.90
REMARK 500 SER V 88 30.13 -81.08
REMARK 500 TYR V 89 16.71 -148.16
REMARK 500 ASP V 93 44.15 -84.80
REMARK 500 GLU X 14 66.43 61.85
REMARK 500 GLU X 70 138.29 -37.98
REMARK 500 SER X 78 20.37 -151.82
REMARK 500 ILE X 94 115.37 -166.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO X 201
DBREF 4MJS A 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS B 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS C 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS D 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS E 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS F 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS G 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS H 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS I 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS J 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS K 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS L 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS M 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS N 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS O 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS P 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS Q 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS R 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS S 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS T 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS U 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS V 3 102 UNP Q13501 SQSTM_HUMAN 3 102
DBREF 4MJS W 15 101 UNP P09217 KPCZ_RAT 15 101
DBREF 4MJS X 3 102 UNP Q13501 SQSTM_HUMAN 3 102
SEQADV 4MJS GLY A 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO A 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS A 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET A 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY B -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO B 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS B 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET B 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA B 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG B 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY C 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO C 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS C 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET C 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY D -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO D 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS D 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET D 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA D 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG D 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY E 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO E 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS E 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET E 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY F -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO F 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS F 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET F 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA F 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG F 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY G 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO G 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS G 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET G 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY H -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO H 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS H 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET H 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA H 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG H 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY I 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO I 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS I 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET I 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY J -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO J 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS J 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET J 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA J 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG J 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY K 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO K 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS K 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET K 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY L -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO L 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS L 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET L 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA L 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG L 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY M 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO M 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS M 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET M 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY N -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO N 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS N 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET N 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA N 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG N 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY O 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO O 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS O 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET O 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY P -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO P 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS P 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET P 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA P 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG P 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY Q 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO Q 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS Q 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET Q 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY R -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO R 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS R 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET R 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA R 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG R 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY S 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO S 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS S 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET S 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY T -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO T 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS T 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET T 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA T 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG T 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY U 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO U 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS U 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET U 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY V -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO V 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS V 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET V 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA V 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG V 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQADV 4MJS GLY W 11 UNP P09217 EXPRESSION TAG
SEQADV 4MJS PRO W 12 UNP P09217 EXPRESSION TAG
SEQADV 4MJS HIS W 13 UNP P09217 EXPRESSION TAG
SEQADV 4MJS MET W 14 UNP P09217 EXPRESSION TAG
SEQADV 4MJS GLY X -1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS PRO X 0 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS HIS X 1 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS MET X 2 UNP Q13501 EXPRESSION TAG
SEQADV 4MJS ALA X 69 UNP Q13501 ASP 69 ENGINEERED MUTATION
SEQADV 4MJS ARG X 71 UNP Q13501 ASP 71 ENGINEERED MUTATION
SEQRES 1 A 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 A 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 A 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 A 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 A 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 A 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 A 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 B 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 B 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 B 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 B 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 B 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 B 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 B 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 B 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 C 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 C 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 C 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 C 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 C 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 C 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 C 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 D 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 D 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 D 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 D 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 D 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 D 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 D 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 D 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 E 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 E 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 E 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 E 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 E 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 E 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 E 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 F 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 F 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 F 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 F 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 F 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 F 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 F 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 F 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 G 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 G 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 G 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 G 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 G 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 G 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 G 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 H 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 H 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 H 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 H 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 H 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 H 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 H 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 H 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 I 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 I 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 I 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 I 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 I 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 I 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 I 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 J 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 J 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 J 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 J 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 J 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 J 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 J 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 J 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 K 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 K 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 K 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 K 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 K 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 K 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 K 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 L 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 L 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 L 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 L 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 L 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 L 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 L 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 L 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 M 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 M 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 M 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 M 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 M 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 M 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 M 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 N 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 N 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 N 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 N 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 N 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 N 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 N 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 N 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 O 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 O 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 O 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 O 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 O 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 O 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 O 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 P 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 P 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 P 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 P 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 P 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 P 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 P 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 P 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 Q 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 Q 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 Q 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 Q 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 Q 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 Q 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 Q 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 R 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 R 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 R 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 R 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 R 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 R 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 R 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 R 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 S 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 S 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 S 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 S 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 S 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 S 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 S 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 T 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 T 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 T 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 T 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 T 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 T 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 T 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 T 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 U 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 U 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 U 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 U 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 U 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 U 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 U 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 V 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 V 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 V 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 V 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 V 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 V 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 V 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 V 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
SEQRES 1 W 91 GLY PRO HIS MET ARG VAL ARG LEU LYS ALA HIS TYR GLY
SEQRES 2 W 91 GLY ASP ILE LEU ILE THR SER VAL ASP PRO THR THR THR
SEQRES 3 W 91 PHE GLN ASP LEU CYS GLU GLU VAL ARG ASP MET CYS GLY
SEQRES 4 W 91 LEU HIS GLN GLN HIS PRO LEU THR LEU LYS TRP VAL ASP
SEQRES 5 W 91 SER GLU GLY ASP PRO CYS THR VAL SER SER GLN MET GLU
SEQRES 6 W 91 LEU GLU GLU ALA PHE ARG LEU ALA CYS GLN GLY ARG ASP
SEQRES 7 W 91 GLU VAL LEU ILE ILE HIS VAL PHE PRO SER ILE PRO GLU
SEQRES 1 X 104 GLY PRO HIS MET SER LEU THR VAL LYS ALA TYR LEU LEU
SEQRES 2 X 104 GLY LYS GLU ASP ALA ALA ARG GLU ILE ARG ARG PHE SER
SEQRES 3 X 104 PHE CYS CYS SER PRO GLU PRO GLU ALA GLU ALA GLU ALA
SEQRES 4 X 104 ALA ALA GLY PRO GLY PRO CYS GLU ARG LEU LEU SER ARG
SEQRES 5 X 104 VAL ALA ALA LEU PHE PRO ALA LEU ARG PRO GLY GLY PHE
SEQRES 6 X 104 GLN ALA HIS TYR ARG ALA GLU ARG GLY ASP LEU VAL ALA
SEQRES 7 X 104 PHE SER SER ASP GLU GLU LEU THR MET ALA MET SER TYR
SEQRES 8 X 104 VAL LYS ASP ASP ILE PHE ARG ILE TYR ILE LYS GLU LYS
HET EDO H 201 4
HET EDO M 201 4
HET EDO O 201 4
HET EDO X 201 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 25 EDO 4(C2 H6 O2)
FORMUL 29 HOH *397(H2 O)
HELIX 1 1 THR A 36 CYS A 48 1 13
HELIX 2 2 SER A 72 GLY A 86 1 15
HELIX 3 3 GLY B 42 PHE B 55 1 14
HELIX 4 4 SER B 79 TYR B 89 1 11
HELIX 5 5 THR C 36 GLY C 49 1 14
HELIX 6 6 SER C 72 GLY C 86 1 15
HELIX 7 7 GLY D 42 PHE D 55 1 14
HELIX 8 8 SER D 79 SER D 88 1 10
HELIX 9 9 THR E 36 CYS E 48 1 13
HELIX 10 10 SER E 72 GLY E 86 1 15
HELIX 11 11 GLY F 42 PHE F 55 1 14
HELIX 12 12 SER F 79 MET F 87 1 9
HELIX 13 13 SER F 88 VAL F 90 5 3
HELIX 14 14 THR G 36 CYS G 48 1 13
HELIX 15 15 SER G 72 GLY G 86 1 15
HELIX 16 16 GLY H 42 PHE H 55 1 14
HELIX 17 17 SER H 79 TYR H 89 1 11
HELIX 18 18 THR I 36 GLY I 49 1 14
HELIX 19 19 SER I 72 GLY I 86 1 15
HELIX 20 20 GLY J 42 PHE J 55 1 14
HELIX 21 21 SER J 79 VAL J 90 1 12
HELIX 22 22 THR K 36 GLY K 49 1 14
HELIX 23 23 SER K 72 GLY K 86 1 15
HELIX 24 24 GLY L 42 PHE L 55 1 14
HELIX 25 25 SER L 79 TYR L 89 1 11
HELIX 26 26 THR M 36 GLY M 49 1 14
HELIX 27 27 SER M 72 GLY M 86 1 15
HELIX 28 28 GLY N 42 PHE N 55 1 14
HELIX 29 29 SER N 79 TYR N 89 1 11
HELIX 30 30 THR O 36 GLY O 49 1 14
HELIX 31 31 SER O 72 GLY O 86 1 15
HELIX 32 32 PRO P 43 PHE P 55 1 13
HELIX 33 33 GLU P 81 MET P 87 1 7
HELIX 34 34 THR Q 36 GLY Q 49 1 14
HELIX 35 35 SER Q 72 GLY Q 86 1 15
HELIX 36 36 GLY R 42 PHE R 55 1 14
HELIX 37 37 SER R 79 SER R 88 1 10
HELIX 38 38 THR S 36 GLY S 49 1 14
HELIX 39 39 SER S 72 GLN S 85 1 14
HELIX 40 40 GLY T 42 PHE T 55 1 14
HELIX 41 41 SER T 79 SER T 88 1 10
HELIX 42 42 THR U 36 CYS U 48 1 13
HELIX 43 43 SER U 72 GLY U 86 1 15
HELIX 44 44 GLY V 42 PHE V 55 1 14
HELIX 45 45 SER V 79 MET V 87 1 9
HELIX 46 46 THR W 36 GLY W 49 1 14
HELIX 47 47 SER W 72 GLY W 86 1 15
HELIX 48 48 GLY X 42 PHE X 55 1 14
HELIX 49 49 SER X 79 TYR X 89 1 11
SHEET 1 A 5 ASP A 25 VAL A 31 0
SHEET 2 A 5 ARG A 15 TYR A 22 -1 N LEU A 18 O THR A 29
SHEET 3 A 5 VAL A 90 PRO A 97 1 O VAL A 95 N HIS A 21
SHEET 4 A 5 LEU A 56 VAL A 61 -1 N LYS A 59 O HIS A 94
SHEET 5 A 5 PRO A 67 VAL A 70 -1 O VAL A 70 N LEU A 58
SHEET 1 B 4 GLU B 19 SER B 24 0
SHEET 2 B 4 THR B 5 LEU B 10 -1 N LEU B 10 O GLU B 19
SHEET 3 B 4 PHE B 95 GLU B 101 1 O ILE B 97 N TYR B 9
SHEET 4 B 4 PHE B 63 GLN B 64 -1 N GLN B 64 O LYS B 100
SHEET 1 C 2 HIS B 66 ARG B 68 0
SHEET 2 C 2 LEU B 74 ALA B 76 -1 O VAL B 75 N TYR B 67
SHEET 1 D 5 ASP C 25 VAL C 31 0
SHEET 2 D 5 ARG C 15 TYR C 22 -1 N LEU C 18 O THR C 29
SHEET 3 D 5 VAL C 90 PRO C 97 1 O VAL C 95 N HIS C 21
SHEET 4 D 5 LEU C 56 VAL C 61 -1 N THR C 57 O PHE C 96
SHEET 5 D 5 PRO C 67 VAL C 70 -1 O CYS C 68 N TRP C 60
SHEET 1 E 5 GLU D 19 PHE D 25 0
SHEET 2 E 5 LEU D 4 LEU D 10 -1 N LEU D 4 O PHE D 25
SHEET 3 E 5 ILE D 94 GLU D 101 1 O ILE D 99 N TYR D 9
SHEET 4 E 5 PHE D 63 ARG D 68 -1 N GLN D 64 O LYS D 100
SHEET 5 E 5 LEU D 74 ALA D 76 -1 O VAL D 75 N TYR D 67
SHEET 1 F 5 ASP E 25 VAL E 31 0
SHEET 2 F 5 VAL E 16 TYR E 22 -1 N LEU E 18 O THR E 29
SHEET 3 F 5 LEU E 91 PRO E 97 1 O ILE E 93 N LYS E 19
SHEET 4 F 5 LEU E 56 VAL E 61 -1 N LYS E 59 O HIS E 94
SHEET 5 F 5 PRO E 67 THR E 69 -1 O CYS E 68 N TRP E 60
SHEET 1 G 5 GLU F 19 PHE F 25 0
SHEET 2 G 5 LEU F 4 LEU F 10 -1 N LEU F 4 O PHE F 25
SHEET 3 G 5 PHE F 95 GLU F 101 1 O ILE F 99 N TYR F 9
SHEET 4 G 5 PHE F 63 ARG F 68 -1 N GLN F 64 O LYS F 100
SHEET 5 G 5 LEU F 74 ALA F 76 -1 O VAL F 75 N TYR F 67
SHEET 1 H 5 ASP G 25 VAL G 31 0
SHEET 2 H 5 VAL G 16 TYR G 22 -1 N LEU G 18 O THR G 29
SHEET 3 H 5 LEU G 91 PRO G 97 1 O VAL G 95 N HIS G 21
SHEET 4 H 5 LEU G 56 VAL G 61 -1 N THR G 57 O PHE G 96
SHEET 5 H 5 PRO G 67 VAL G 70 -1 O CYS G 68 N TRP G 60
SHEET 1 I 5 ALA H 17 PHE H 25 0
SHEET 2 I 5 LEU H 4 LEU H 11 -1 N LEU H 10 O ARG H 18
SHEET 3 I 5 PHE H 95 GLU H 101 1 O PHE H 95 N THR H 5
SHEET 4 I 5 PHE H 63 ARG H 68 -1 N GLN H 64 O LYS H 100
SHEET 5 I 5 LEU H 74 PHE H 77 -1 O VAL H 75 N TYR H 67
SHEET 1 J 5 ASP I 25 VAL I 31 0
SHEET 2 J 5 ARG I 15 TYR I 22 -1 N ALA I 20 O LEU I 27
SHEET 3 J 5 VAL I 90 PRO I 97 1 O ILE I 93 N LYS I 19
SHEET 4 J 5 LEU I 56 VAL I 61 -1 N THR I 57 O PHE I 96
SHEET 5 J 5 PRO I 67 VAL I 70 -1 O CYS I 68 N TRP I 60
SHEET 1 K 5 ALA J 16 PHE J 25 0
SHEET 2 K 5 LEU J 4 LYS J 13 -1 N LEU J 4 O PHE J 25
SHEET 3 K 5 PHE J 95 GLU J 101 1 O PHE J 95 N THR J 5
SHEET 4 K 5 PHE J 63 ARG J 68 -1 N GLN J 64 O LYS J 100
SHEET 5 K 5 LEU J 74 PHE J 77 -1 O VAL J 75 N TYR J 67
SHEET 1 L 5 ASP K 25 VAL K 31 0
SHEET 2 L 5 ARG K 15 TYR K 22 -1 N ALA K 20 O LEU K 27
SHEET 3 L 5 VAL K 90 PRO K 97 1 O LEU K 91 N ARG K 15
SHEET 4 L 5 LEU K 56 VAL K 61 -1 N THR K 57 O PHE K 96
SHEET 5 L 5 PRO K 67 VAL K 70 -1 O CYS K 68 N TRP K 60
SHEET 1 M 5 ALA L 16 PHE L 25 0
SHEET 2 M 5 LEU L 4 GLY L 12 -1 N GLY L 12 O ALA L 16
SHEET 3 M 5 ILE L 94 GLU L 101 1 O ILE L 99 N TYR L 9
SHEET 4 M 5 PHE L 63 ARG L 68 -1 N HIS L 66 O TYR L 98
SHEET 5 M 5 LEU L 74 PHE L 77 -1 O PHE L 77 N ALA L 65
SHEET 1 N 5 ASP M 25 VAL M 31 0
SHEET 2 N 5 ARG M 15 TYR M 22 -1 N ALA M 20 O LEU M 27
SHEET 3 N 5 VAL M 90 PRO M 97 1 O ILE M 93 N ARG M 17
SHEET 4 N 5 LEU M 56 VAL M 61 -1 N THR M 57 O PHE M 96
SHEET 5 N 5 PRO M 67 THR M 69 -1 O CYS M 68 N TRP M 60
SHEET 1 O 5 GLU N 19 PHE N 25 0
SHEET 2 O 5 LEU N 4 LEU N 10 -1 N LEU N 4 O PHE N 25
SHEET 3 O 5 PHE N 95 GLU N 101 1 O PHE N 95 N THR N 5
SHEET 4 O 5 PHE N 63 ARG N 68 -1 N GLN N 64 O LYS N 100
SHEET 5 O 5 LEU N 74 ALA N 76 -1 O VAL N 75 N TYR N 67
SHEET 1 P 5 ASP O 25 VAL O 31 0
SHEET 2 P 5 VAL O 16 TYR O 22 -1 N VAL O 16 O VAL O 31
SHEET 3 P 5 LEU O 91 PRO O 97 1 O ILE O 93 N ARG O 17
SHEET 4 P 5 LEU O 56 VAL O 61 -1 N LYS O 59 O HIS O 94
SHEET 5 P 5 PRO O 67 THR O 69 -1 O CYS O 68 N TRP O 60
SHEET 1 Q 5 GLU P 19 SER P 24 0
SHEET 2 Q 5 THR P 5 LEU P 10 -1 N LEU P 10 O GLU P 19
SHEET 3 Q 5 PHE P 95 GLU P 101 1 O ILE P 97 N TYR P 9
SHEET 4 Q 5 PHE P 63 HIS P 66 -1 N HIS P 66 O TYR P 98
SHEET 5 Q 5 ALA P 76 PHE P 77 -1 O PHE P 77 N ALA P 65
SHEET 1 R 5 ASP Q 25 VAL Q 31 0
SHEET 2 R 5 ARG Q 15 TYR Q 22 -1 N VAL Q 16 O VAL Q 31
SHEET 3 R 5 VAL Q 90 PRO Q 97 1 O LEU Q 91 N ARG Q 15
SHEET 4 R 5 LEU Q 56 VAL Q 61 -1 N LYS Q 59 O HIS Q 94
SHEET 5 R 5 PRO Q 67 THR Q 69 -1 O CYS Q 68 N TRP Q 60
SHEET 1 S 5 ALA R 17 PHE R 25 0
SHEET 2 S 5 LEU R 4 LEU R 11 -1 N LEU R 10 O ARG R 18
SHEET 3 S 5 ILE R 94 GLU R 101 1 O ILE R 99 N TYR R 9
SHEET 4 S 5 PHE R 63 ARG R 68 -1 N GLN R 64 O LYS R 100
SHEET 5 S 5 LEU R 74 ALA R 76 -1 O VAL R 75 N TYR R 67
SHEET 1 T 5 ASP S 25 VAL S 31 0
SHEET 2 T 5 ARG S 15 TYR S 22 -1 N VAL S 16 O VAL S 31
SHEET 3 T 5 VAL S 90 PRO S 97 1 O LEU S 91 N ARG S 15
SHEET 4 T 5 LEU S 56 VAL S 61 -1 N LYS S 59 O HIS S 94
SHEET 5 T 5 PRO S 67 VAL S 70 -1 O CYS S 68 N TRP S 60
SHEET 1 U 5 GLU T 19 PHE T 25 0
SHEET 2 U 5 LEU T 4 LEU T 10 -1 N LEU T 10 O GLU T 19
SHEET 3 U 5 PHE T 95 GLU T 101 1 O ILE T 99 N TYR T 9
SHEET 4 U 5 PHE T 63 ARG T 68 -1 N GLN T 64 O LYS T 100
SHEET 5 U 5 LEU T 74 ALA T 76 -1 O VAL T 75 N TYR T 67
SHEET 1 V 5 ASP U 25 VAL U 31 0
SHEET 2 V 5 ARG U 15 TYR U 22 -1 N VAL U 16 O VAL U 31
SHEET 3 V 5 VAL U 90 PRO U 97 1 O VAL U 95 N LYS U 19
SHEET 4 V 5 LEU U 56 VAL U 61 -1 N LYS U 59 O HIS U 94
SHEET 5 V 5 PRO U 67 VAL U 70 -1 O CYS U 68 N TRP U 60
SHEET 1 W 5 GLU V 19 SER V 24 0
SHEET 2 W 5 THR V 5 LEU V 10 -1 N ALA V 8 O ARG V 21
SHEET 3 W 5 PHE V 95 LYS V 100 1 O ILE V 97 N TYR V 9
SHEET 4 W 5 GLN V 64 ALA V 69 -1 N GLN V 64 O LYS V 100
SHEET 5 W 5 ASP V 73 ALA V 76 -1 O ASP V 73 N ALA V 69
SHEET 1 X 5 ASP W 25 VAL W 31 0
SHEET 2 X 5 ARG W 15 TYR W 22 -1 N LEU W 18 O THR W 29
SHEET 3 X 5 VAL W 90 PRO W 97 1 O VAL W 95 N HIS W 21
SHEET 4 X 5 LEU W 56 VAL W 61 -1 N LYS W 59 O HIS W 94
SHEET 5 X 5 PRO W 67 THR W 69 -1 O CYS W 68 N TRP W 60
SHEET 1 Y 5 ALA X 16 CYS X 26 0
SHEET 2 Y 5 SER X 3 GLY X 12 -1 N LEU X 4 O PHE X 25
SHEET 3 Y 5 PHE X 95 GLU X 101 1 O ILE X 99 N TYR X 9
SHEET 4 Y 5 PHE X 63 ALA X 69 -1 N GLN X 64 O LYS X 100
SHEET 5 Y 5 ASP X 73 ALA X 76 -1 O ASP X 73 N ALA X 69
SITE 1 AC1 6 TYR H 67 ARG H 68 TYR H 89 ILE H 94
SITE 2 AC1 6 ARG H 96 HOH H 311
SITE 1 AC2 5 TRP M 60 VAL M 61 VAL M 90 LEU M 91
SITE 2 AC2 5 ILE M 92
SITE 1 AC3 3 PHE O 37 GLN O 38 GLN O 73
SITE 1 AC4 4 TYR X 67 ARG X 68 VAL X 90 ARG X 96
CRYST1 85.715 135.681 259.559 90.00 90.00 90.00 P 21 21 21 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 0.011667 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
