HEADER TRANSFERASE 31-JUL-15 5CZO
TITLE STRUCTURE OF S. CEREVISIAE HRR25:MAM1 COMPLEX, FORM 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE I HOMOLOG HRR25;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.11.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: SURFACE LYS RESIDUES METHYLATED (MLY);
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MONOPOLIN COMPLEX SUBUNIT MAM1;
COMPND 10 CHAIN: C, D;
COMPND 11 SYNONYM: MONOPOLAR MICROTUBULE ATTACHMENT DURING MEIOSIS 1 PROTEIN 1;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: SURFACE LYS RESIDUES METHYLATED (MLY)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: HRR25, YPL204W;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 12 S288C);
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 GENE: MAM1, YER106W;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CASEIN KINASE, MONOPOLIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.YE,K.D.CORBETT
REVDAT 5 27-SEP-23 5CZO 1 LINK
REVDAT 4 25-DEC-19 5CZO 1 REMARK
REVDAT 3 20-SEP-17 5CZO 1 JRNL
REVDAT 2 07-DEC-16 5CZO 1 JRNL
REVDAT 1 03-AUG-16 5CZO 0
JRNL AUTH Q.YE,S.N.UR,T.Y.SU,K.D.CORBETT
JRNL TITL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE HRR25:MAM1
JRNL TITL 2 MONOPOLIN SUBCOMPLEX REVEALS A NOVEL KINASE REGULATOR.
JRNL REF EMBO J. V. 35 2139 2016
JRNL REFN ISSN 0261-4189
JRNL PMID 27491543
JRNL DOI 10.15252/EMBJ.201694082
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 50244
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2572
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 49.6993 - 7.5764 0.99 2615 157 0.1804 0.2076
REMARK 3 2 7.5764 - 6.0170 1.00 2695 141 0.2267 0.2473
REMARK 3 3 6.0170 - 5.2573 1.00 2610 156 0.2105 0.2638
REMARK 3 4 5.2573 - 4.7771 1.00 2665 144 0.1865 0.2095
REMARK 3 5 4.7771 - 4.4349 1.00 2664 169 0.1544 0.1888
REMARK 3 6 4.4349 - 4.1736 1.00 2692 135 0.1764 0.1974
REMARK 3 7 4.1736 - 3.9647 1.00 2642 134 0.1841 0.2056
REMARK 3 8 3.9647 - 3.7921 1.00 2648 152 0.2039 0.2451
REMARK 3 9 3.7921 - 3.6462 1.00 2670 152 0.2213 0.3071
REMARK 3 10 3.6462 - 3.5204 1.00 2603 169 0.2325 0.2519
REMARK 3 11 3.5204 - 3.4104 1.00 2721 126 0.2524 0.2868
REMARK 3 12 3.4104 - 3.3129 1.00 2650 113 0.2740 0.3445
REMARK 3 13 3.3129 - 3.2257 1.00 2723 138 0.3037 0.3912
REMARK 3 14 3.2257 - 3.1470 1.00 2640 134 0.3258 0.3850
REMARK 3 15 3.1470 - 3.0755 1.00 2647 146 0.3217 0.3402
REMARK 3 16 3.0755 - 3.0100 1.00 2680 146 0.3419 0.4431
REMARK 3 17 3.0100 - 2.9498 1.00 2675 145 0.3372 0.3917
REMARK 3 18 2.9498 - 2.8942 0.90 2432 115 0.3539 0.4452
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) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 8100
REMARK 3 ANGLE : 0.505 10883
REMARK 3 CHIRALITY : 0.023 1133
REMARK 3 PLANARITY : 0.002 1386
REMARK 3 DIHEDRAL : 12.428 3083
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5127 -0.1637 11.6359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3521 T22: 0.4371
REMARK 3 T33: 0.5389 T12: 0.0535
REMARK 3 T13: 0.0600 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.8182 L22: 2.3594
REMARK 3 L33: 2.7223 L12: -0.1416
REMARK 3 L13: 0.1228 L23: -0.1179
REMARK 3 S TENSOR
REMARK 3 S11: -0.1552 S12: -0.1577 S13: -0.0543
REMARK 3 S21: 0.2254 S22: -0.0155 S23: 0.4067
REMARK 3 S31: 0.0090 S32: -0.3596 S33: 0.1439
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7060 -10.4454 55.6390
REMARK 3 T TENSOR
REMARK 3 T11: 0.3835 T22: 0.4799
REMARK 3 T33: 0.4033 T12: -0.0177
REMARK 3 T13: 0.0267 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.4693 L22: 2.9451
REMARK 3 L33: 3.4739 L12: -0.6329
REMARK 3 L13: 1.1555 L23: -0.8523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: -0.1158 S13: 0.2656
REMARK 3 S21: 0.0349 S22: -0.0714 S23: -0.0561
REMARK 3 S31: 0.0826 S32: -0.2026 S33: 0.1105
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -38.1260 -7.5072 -9.8443
REMARK 3 T TENSOR
REMARK 3 T11: 0.6242 T22: 0.5114
REMARK 3 T33: 0.8167 T12: -0.0342
REMARK 3 T13: -0.1630 T23: -0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 2.4284 L22: 2.6145
REMARK 3 L33: 4.0624 L12: -0.6945
REMARK 3 L13: 0.6776 L23: -1.2660
REMARK 3 S TENSOR
REMARK 3 S11: -0.0438 S12: 0.2487 S13: -0.1767
REMARK 3 S21: -0.5121 S22: 0.0615 S23: 0.5576
REMARK 3 S31: -0.0546 S32: -0.2334 S33: -0.0280
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1413 -4.7711 77.4115
REMARK 3 T TENSOR
REMARK 3 T11: 0.8509 T22: 0.8886
REMARK 3 T33: 0.6251 T12: 0.1521
REMARK 3 T13: -0.0245 T23: -0.2068
REMARK 3 L TENSOR
REMARK 3 L11: 1.4106 L22: 3.4628
REMARK 3 L33: 3.1248 L12: 0.2801
REMARK 3 L13: 0.7752 L23: -1.0989
REMARK 3 S TENSOR
REMARK 3 S11: -0.1449 S12: -0.7077 S13: 0.3560
REMARK 3 S21: 0.9274 S22: 0.1375 S23: 0.3730
REMARK 3 S31: -0.2027 S32: -0.3968 S33: 0.0068
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 5CZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2829
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 132.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.360
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: 4XHL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE PH 8.0, 14% PEG3350, 6%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.92050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 5550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 5410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 THR A 174
REMARK 465 GLY A 175
REMARK 465 ASP A 312
REMARK 465 LEU A 313
REMARK 465 ASN A 314
REMARK 465 ALA A 315
REMARK 465 ASN A 316
REMARK 465 SER A 317
REMARK 465 ASN A 318
REMARK 465 ALA A 319
REMARK 465 ALA A 320
REMARK 465 SER A 321
REMARK 465 ALA A 322
REMARK 465 SER A 323
REMARK 465 ASN A 324
REMARK 465 SER A 325
REMARK 465 MET A 390
REMARK 465 GLU A 391
REMARK 465 ASN A 392
REMARK 465 LEU A 393
REMARK 465 ARG A 394
REMARK 465 GLU C 87
REMARK 465 ALA C 88
REMARK 465 THR C 89
REMARK 465 GLU C 90
REMARK 465 ALA B 218
REMARK 465 THR B 219
REMARK 465 THR B 220
REMARK 465 LYS B 221
REMARK 465 LYS B 222
REMARK 465 GLN B 223
REMARK 465 ASN B 318
REMARK 465 ALA B 319
REMARK 465 ALA B 320
REMARK 465 SER B 321
REMARK 465 ALA B 322
REMARK 465 SER B 323
REMARK 465 ASN B 324
REMARK 465 SER B 325
REMARK 465 LYS B 388
REMARK 465 GLY B 389
REMARK 465 MET B 390
REMARK 465 GLU B 391
REMARK 465 ASN B 392
REMARK 465 LEU B 393
REMARK 465 ARG B 394
REMARK 465 GLU D 87
REMARK 465 ALA D 88
REMARK 465 THR D 89
REMARK 465 GLU D 90
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 PHE A 20 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 173 CG CD1 CD2
REMARK 470 LYS C 128 CG CD CE NZ
REMARK 470 PHE B 20 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 125 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 128 CG CD CE NZ
REMARK 470 TYR D 129 CG CD1 CD2 CE1 CE2 CZ OH
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 ASP A 2 75.69 -118.15
REMARK 500 ARG A 7 18.10 56.24
REMARK 500 ARG A 43 42.45 -89.16
REMARK 500 GLN A 48 -8.73 -143.03
REMARK 500 ASP A 149 84.68 57.57
REMARK 500 CYS A 241 51.56 -113.79
REMARK 500 LYS A 310 67.41 -117.90
REMARK 500 ASN A 373 48.21 -93.86
REMARK 500 PRO A 379 -79.28 -93.45
REMARK 500 ASN C 145 -52.76 -125.43
REMARK 500 ASP B 2 69.41 -119.32
REMARK 500 ASP B 128 76.70 -154.06
REMARK 500 ASP B 149 83.15 57.50
REMARK 500 HIS B 162 58.78 -67.35
REMARK 500 THR B 174 -158.80 -71.92
REMARK 500 CYS B 241 50.86 -99.75
REMARK 500 ASN B 314 176.94 61.31
REMARK 500 ASN B 373 51.83 -101.31
REMARK 500 PRO B 379 -83.42 -86.23
REMARK 500 GLN D 175 99.21 -64.42
REMARK 500 HIS D 178 30.48 -87.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 425 DISTANCE = 5.88 ANGSTROMS
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 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 114 SG
REMARK 620 2 HIS C 116 ND1 112.4
REMARK 620 3 CYS C 119 SG 120.9 121.8
REMARK 620 4 CYS C 152 SG 116.9 75.7 98.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 114 SG
REMARK 620 2 HIS D 116 ND1 89.9
REMARK 620 3 CYS D 119 SG 114.4 133.8
REMARK 620 4 CYS D 152 SG 117.9 100.9 100.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CYZ RELATED DB: PDB
DBREF 5CZO A 1 394 UNP P29295 HRR25_YEAST 1 394
DBREF 5CZO C 87 191 UNP P40065 MAM1_YEAST 87 191
DBREF 5CZO B 1 394 UNP P29295 HRR25_YEAST 1 394
DBREF 5CZO D 87 191 UNP P40065 MAM1_YEAST 87 191
SEQADV 5CZO ALA A 0 UNP P29295 EXPRESSION TAG
SEQADV 5CZO ARG A 38 UNP P29295 LYS 38 ENGINEERED MUTATION
SEQADV 5CZO ALA B 0 UNP P29295 EXPRESSION TAG
SEQADV 5CZO ARG B 38 UNP P29295 LYS 38 ENGINEERED MUTATION
SEQRES 1 A 395 ALA MET ASP LEU ARG VAL GLY ARG MLY PHE ARG ILE GLY
SEQRES 2 A 395 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR HIS
SEQRES 3 A 395 GLY THR ASN LEU ILE SER GLY GLU GLU VAL ALA ILE ARG
SEQRES 4 A 395 LEU GLU SER ILE ARG SER ARG HIS PRO GLN LEU ASP TYR
SEQRES 5 A 395 GLU SER ARG VAL TYR ARG TYR LEU SER GLY GLY VAL GLY
SEQRES 6 A 395 ILE PRO PHE ILE ARG TRP PHE GLY ARG GLU GLY GLU TYR
SEQRES 7 A 395 ASN ALA MET VAL ILE ASP LEU LEU GLY PRO SER LEU GLU
SEQRES 8 A 395 ASP LEU PHE ASN TYR CYS HIS ARG ARG PHE SER PHE LYS
SEQRES 9 A 395 THR VAL ILE MET LEU ALA LEU GLN MET PHE CYS ARG ILE
SEQRES 10 A 395 GLN TYR ILE HIS GLY ARG SER PHE ILE HIS ARG ASP ILE
SEQRES 11 A 395 LYS PRO ASP ASN PHE LEU MET GLY VAL GLY ARG ARG GLY
SEQRES 12 A 395 SER THR VAL HIS VAL ILE ASP PHE GLY LEU SER MLY MLY
SEQRES 13 A 395 TYR ARG ASP PHE ASN THR HIS ARG HIS ILE PRO TYR ARG
SEQRES 14 A 395 GLU ASN LYS SER LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 15 A 395 VAL ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 16 A 395 ASP LEU GLU SER LEU GLY TYR VAL LEU ILE TYR PHE CYS
SEQRES 17 A 395 LYS GLY SER LEU PRO TRP GLN GLY LEU LYS ALA THR THR
SEQRES 18 A 395 LYS LYS GLN LYS TYR ASP ARG ILE MET GLU MLY LYS LEU
SEQRES 19 A 395 ASN VAL SER VAL GLU THR LEU CYS SER GLY LEU PRO LEU
SEQRES 20 A 395 GLU PHE GLN GLU TYR MET ALA TYR CYS MLY ASN LEU LYS
SEQRES 21 A 395 PHE ASP GLU MLY PRO ASP TYR LEU PHE LEU ALA ARG LEU
SEQRES 22 A 395 PHE LYS ASP LEU SER ILE LYS LEU GLU TYR HIS ASN ASP
SEQRES 23 A 395 HIS LEU PHE ASP TRP THR MET LEU ARG TYR THR LYS ALA
SEQRES 24 A 395 MET VAL GLU LYS GLN ARG ASP LEU LEU ILE GLU LYS GLY
SEQRES 25 A 395 ASP LEU ASN ALA ASN SER ASN ALA ALA SER ALA SER ASN
SEQRES 26 A 395 SER THR ASP ASN LYS SER GLU THR PHE ASN LYS ILE MLY
SEQRES 27 A 395 LEU LEU ALA MET LYS LYS PHE PRO THR HIS PHE HIS TYR
SEQRES 28 A 395 TYR MLY ASN GLU ASP LYS HIS ASN PRO SER PRO GLU GLU
SEQRES 29 A 395 ILE MLY GLN GLN THR ILE LEU ASN ASN ASN ALA ALA SER
SEQRES 30 A 395 SER LEU PRO GLU GLU LEU LEU ASN ALA LEU ASP LYS GLY
SEQRES 31 A 395 MET GLU ASN LEU ARG
SEQRES 1 C 105 GLU ALA THR GLU CYS LEU THR ARG SER ASN LEU LYS LYS
SEQRES 2 C 105 LEU GLN GLU LYS ILE PHE ASP ARG GLU LEU ASN ASP ILE
SEQRES 3 C 105 ALA CYS ASP HIS CYS LEU CYS SER THR GLU ASN ARG ARG
SEQRES 4 C 105 ASP ILE LYS TYR SER ARG LEU TRP PHE LEU PHE GLU LEU
SEQRES 5 C 105 GLU MET SER GLU ASN TRP ASN GLU ASN LEU ARG LEU SER
SEQRES 6 C 105 CYS TYR ASN MLY TYR VAL TYR SER ALA ILE ASP GLU SER
SEQRES 7 C 105 TRP MLY MET GLU ASN ILE LEU LEU LYS GLU GLN GLU LYS
SEQRES 8 C 105 HIS TYR GLU TYR PHE PRO ILE GLY GLN LEU LEU ILE PRO
SEQRES 9 C 105 ASN
SEQRES 1 B 395 ALA MET ASP LEU ARG VAL GLY ARG MLY PHE ARG ILE GLY
SEQRES 2 B 395 ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR HIS
SEQRES 3 B 395 GLY THR ASN LEU ILE SER GLY GLU GLU VAL ALA ILE ARG
SEQRES 4 B 395 LEU GLU SER ILE ARG SER ARG HIS PRO GLN LEU ASP TYR
SEQRES 5 B 395 GLU SER ARG VAL TYR ARG TYR LEU SER GLY GLY VAL GLY
SEQRES 6 B 395 ILE PRO PHE ILE ARG TRP PHE GLY ARG GLU GLY GLU TYR
SEQRES 7 B 395 ASN ALA MET VAL ILE ASP LEU LEU GLY PRO SER LEU GLU
SEQRES 8 B 395 ASP LEU PHE ASN TYR CYS HIS ARG ARG PHE SER PHE LYS
SEQRES 9 B 395 THR VAL ILE MET LEU ALA LEU GLN MET PHE CYS ARG ILE
SEQRES 10 B 395 GLN TYR ILE HIS GLY ARG SER PHE ILE HIS ARG ASP ILE
SEQRES 11 B 395 LYS PRO ASP ASN PHE LEU MET GLY VAL GLY ARG ARG GLY
SEQRES 12 B 395 SER THR VAL HIS VAL ILE ASP PHE GLY LEU SER MLY MLY
SEQRES 13 B 395 TYR ARG ASP PHE ASN THR HIS ARG HIS ILE PRO TYR ARG
SEQRES 14 B 395 GLU ASN LYS SER LEU THR GLY THR ALA ARG TYR ALA SER
SEQRES 15 B 395 VAL ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP
SEQRES 16 B 395 ASP LEU GLU SER LEU GLY TYR VAL LEU ILE TYR PHE CYS
SEQRES 17 B 395 LYS GLY SER LEU PRO TRP GLN GLY LEU LYS ALA THR THR
SEQRES 18 B 395 LYS LYS GLN LYS TYR ASP ARG ILE MET GLU MLY LYS LEU
SEQRES 19 B 395 ASN VAL SER VAL GLU THR LEU CYS SER GLY LEU PRO LEU
SEQRES 20 B 395 GLU PHE GLN GLU TYR MET ALA TYR CYS MLY ASN LEU LYS
SEQRES 21 B 395 PHE ASP GLU MLY PRO ASP TYR LEU PHE LEU ALA ARG LEU
SEQRES 22 B 395 PHE LYS ASP LEU SER ILE LYS LEU GLU TYR HIS ASN ASP
SEQRES 23 B 395 HIS LEU PHE ASP TRP THR MET LEU ARG TYR THR LYS ALA
SEQRES 24 B 395 MET VAL GLU LYS GLN ARG ASP LEU LEU ILE GLU LYS GLY
SEQRES 25 B 395 ASP LEU ASN ALA ASN SER ASN ALA ALA SER ALA SER ASN
SEQRES 26 B 395 SER THR ASP ASN LYS SER GLU THR PHE ASN LYS ILE MLY
SEQRES 27 B 395 LEU LEU ALA MET LYS LYS PHE PRO THR HIS PHE HIS TYR
SEQRES 28 B 395 TYR MLY ASN GLU ASP LYS HIS ASN PRO SER PRO GLU GLU
SEQRES 29 B 395 ILE MLY GLN GLN THR ILE LEU ASN ASN ASN ALA ALA SER
SEQRES 30 B 395 SER LEU PRO GLU GLU LEU LEU ASN ALA LEU ASP LYS GLY
SEQRES 31 B 395 MET GLU ASN LEU ARG
SEQRES 1 D 105 GLU ALA THR GLU CYS LEU THR ARG SER ASN LEU LYS LYS
SEQRES 2 D 105 LEU GLN GLU LYS ILE PHE ASP ARG GLU LEU ASN ASP ILE
SEQRES 3 D 105 ALA CYS ASP HIS CYS LEU CYS SER THR GLU ASN ARG ARG
SEQRES 4 D 105 ASP ILE LYS TYR SER ARG LEU TRP PHE LEU PHE GLU LEU
SEQRES 5 D 105 GLU MET SER GLU ASN TRP ASN GLU ASN LEU ARG LEU SER
SEQRES 6 D 105 CYS TYR ASN MLY TYR VAL TYR SER ALA ILE ASP GLU SER
SEQRES 7 D 105 TRP MLY MET GLU ASN ILE LEU LEU LYS GLU GLN GLU LYS
SEQRES 8 D 105 HIS TYR GLU TYR PHE PRO ILE GLY GLN LEU LEU ILE PRO
SEQRES 9 D 105 ASN
MODRES 5CZO MLY A 8 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 154 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 155 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 231 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 256 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 263 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 337 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 352 LYS MODIFIED RESIDUE
MODRES 5CZO MLY A 365 LYS MODIFIED RESIDUE
MODRES 5CZO MLY C 155 LYS MODIFIED RESIDUE
MODRES 5CZO MLY C 166 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 8 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 154 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 155 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 231 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 256 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 263 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 337 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 352 LYS MODIFIED RESIDUE
MODRES 5CZO MLY B 365 LYS MODIFIED RESIDUE
MODRES 5CZO MLY D 155 LYS MODIFIED RESIDUE
MODRES 5CZO MLY D 166 LYS MODIFIED RESIDUE
HET MLY A 8 11
HET MLY A 154 11
HET MLY A 155 11
HET MLY A 231 11
HET MLY A 256 11
HET MLY A 263 11
HET MLY A 337 11
HET MLY A 352 11
HET MLY A 365 11
HET MLY C 155 11
HET MLY C 166 11
HET MLY B 8 11
HET MLY B 154 11
HET MLY B 155 11
HET MLY B 231 11
HET MLY B 256 11
HET MLY B 263 11
HET MLY B 337 11
HET MLY B 352 11
HET MLY B 365 11
HET MLY D 155 11
HET MLY D 166 11
HET ZN C 201 1
HET ZN D 201 1
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM ZN ZINC ION
FORMUL 1 MLY 22(C8 H18 N2 O2)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *39(H2 O)
HELIX 1 AA1 GLN A 48 LEU A 59 1 12
HELIX 2 AA2 LEU A 89 CYS A 96 1 8
HELIX 3 AA3 SER A 101 GLY A 121 1 21
HELIX 4 AA4 LYS A 130 ASP A 132 5 3
HELIX 5 AA5 GLY A 139 GLY A 142 5 4
HELIX 6 AA6 SER A 181 LEU A 186 1 6
HELIX 7 AA7 SER A 191 GLY A 209 1 19
HELIX 8 AA8 THR A 220 VAL A 235 1 16
HELIX 9 AA9 SER A 236 CYS A 241 1 6
HELIX 10 AB1 PRO A 245 ASN A 257 1 13
HELIX 11 AB2 ASP A 265 LEU A 280 1 16
HELIX 12 AB3 PHE A 288 LYS A 310 1 23
HELIX 13 AB4 ASP A 327 PHE A 344 1 18
HELIX 14 AB5 SER A 360 ASN A 373 1 14
HELIX 15 AB6 PRO A 379 LYS A 388 1 10
HELIX 16 AB7 THR C 93 ASP C 111 1 19
HELIX 17 AB8 SER C 120 ASP C 126 1 7
HELIX 18 AB9 TYR C 129 LEU C 135 1 7
HELIX 19 AC1 ASN C 147 CYS C 152 1 6
HELIX 20 AC2 CYS C 152 VAL C 157 1 6
HELIX 21 AC3 VAL C 157 ASP C 162 1 6
HELIX 22 AC4 PRO C 183 LEU C 187 5 5
HELIX 23 AC5 GLN B 48 LEU B 59 1 12
HELIX 24 AC6 LEU B 89 CYS B 96 1 8
HELIX 25 AC7 SER B 101 ARG B 122 1 22
HELIX 26 AC8 GLY B 139 GLY B 142 5 4
HELIX 27 AC9 SER B 181 LEU B 186 1 6
HELIX 28 AD1 SER B 191 GLY B 209 1 19
HELIX 29 AD2 TYR B 225 VAL B 235 1 11
HELIX 30 AD3 SER B 236 CYS B 241 1 6
HELIX 31 AD4 PRO B 245 LEU B 258 1 14
HELIX 32 AD5 ASP B 265 LEU B 280 1 16
HELIX 33 AD6 PHE B 288 GLY B 311 1 24
HELIX 34 AD7 ASP B 327 PHE B 344 1 18
HELIX 35 AD8 SER B 360 MLY B 365 1 6
HELIX 36 AD9 MLY B 365 ASN B 373 1 9
HELIX 37 AE1 PRO B 379 ASP B 387 1 9
HELIX 38 AE2 THR D 93 ASP D 111 1 19
HELIX 39 AE3 SER D 120 ILE D 127 1 8
HELIX 40 AE4 TYR D 129 LEU D 135 1 7
HELIX 41 AE5 PHE D 136 MET D 140 5 5
HELIX 42 AE6 ASN D 147 CYS D 152 1 6
HELIX 43 AE7 CYS D 152 VAL D 157 1 6
HELIX 44 AE8 VAL D 157 ASP D 162 1 6
HELIX 45 AE9 PRO D 183 LEU D 187 5 5
SHEET 1 AA1 6 ARG A 4 VAL A 5 0
SHEET 2 AA1 6 PHE A 9 GLY A 16 -1 O PHE A 9 N VAL A 5
SHEET 3 AA1 6 GLY A 21 ASN A 28 -1 O ILE A 23 N GLY A 16
SHEET 4 AA1 6 GLU A 34 SER A 41 -1 O ILE A 37 N TYR A 24
SHEET 5 AA1 6 TYR A 77 ASP A 83 -1 O ASN A 78 N GLU A 40
SHEET 6 AA1 6 ILE A 68 GLU A 74 -1 N ARG A 69 O VAL A 81
SHEET 1 AA2 3 LEU A 85 SER A 88 0
SHEET 2 AA2 3 PHE A 134 GLY A 137 -1 O MET A 136 N GLY A 86
SHEET 3 AA2 3 VAL A 145 VAL A 147 -1 O HIS A 146 N LEU A 135
SHEET 1 AA3 2 PHE A 124 ILE A 125 0
SHEET 2 AA3 2 MLY A 154 MLY A 155 -1 O MLY A 154 N ILE A 125
SHEET 1 AA4 6 ARG B 4 VAL B 5 0
SHEET 2 AA4 6 PHE B 9 GLY B 18 -1 O PHE B 9 N VAL B 5
SHEET 3 AA4 6 GLY B 21 ASN B 28 -1 O ILE B 23 N GLY B 16
SHEET 4 AA4 6 GLU B 34 SER B 41 -1 O ILE B 37 N TYR B 24
SHEET 5 AA4 6 TYR B 77 ASP B 83 -1 O ASN B 78 N GLU B 40
SHEET 6 AA4 6 ILE B 68 GLU B 74 -1 N TRP B 70 O VAL B 81
SHEET 1 AA5 3 LEU B 85 SER B 88 0
SHEET 2 AA5 3 PHE B 134 GLY B 137 -1 O MET B 136 N GLY B 86
SHEET 3 AA5 3 VAL B 145 VAL B 147 -1 O HIS B 146 N LEU B 135
SHEET 1 AA6 2 PHE B 124 ILE B 125 0
SHEET 2 AA6 2 MLY B 154 MLY B 155 -1 O MLY B 154 N ILE B 125
LINK C ARG A 7 N MLY A 8 1555 1555 1.33
LINK C MLY A 8 N PHE A 9 1555 1555 1.33
LINK C SER A 153 N MLY A 154 1555 1555 1.33
LINK C MLY A 154 N MLY A 155 1555 1555 1.33
LINK C MLY A 155 N TYR A 156 1555 1555 1.33
LINK C GLU A 230 N MLY A 231 1555 1555 1.33
LINK C MLY A 231 N LYS A 232 1555 1555 1.33
LINK C CYS A 255 N MLY A 256 1555 1555 1.33
LINK C MLY A 256 N ASN A 257 1555 1555 1.33
LINK C GLU A 262 N MLY A 263 1555 1555 1.33
LINK C MLY A 263 N PRO A 264 1555 1555 1.34
LINK C ILE A 336 N MLY A 337 1555 1555 1.33
LINK C MLY A 337 N LEU A 338 1555 1555 1.33
LINK C TYR A 351 N MLY A 352 1555 1555 1.33
LINK C MLY A 352 N ASN A 353 1555 1555 1.33
LINK C ILE A 364 N MLY A 365 1555 1555 1.33
LINK C MLY A 365 N GLN A 366 1555 1555 1.33
LINK C ASN C 154 N MLY C 155 1555 1555 1.33
LINK C MLY C 155 N TYR C 156 1555 1555 1.33
LINK C TRP C 165 N MLY C 166 1555 1555 1.33
LINK C MLY C 166 N MET C 167 1555 1555 1.33
LINK C ARG B 7 N MLY B 8 1555 1555 1.33
LINK C MLY B 8 N PHE B 9 1555 1555 1.33
LINK C SER B 153 N MLY B 154 1555 1555 1.33
LINK C MLY B 154 N MLY B 155 1555 1555 1.33
LINK C MLY B 155 N TYR B 156 1555 1555 1.33
LINK C GLU B 230 N MLY B 231 1555 1555 1.33
LINK C MLY B 231 N LYS B 232 1555 1555 1.33
LINK C CYS B 255 N MLY B 256 1555 1555 1.33
LINK C MLY B 256 N ASN B 257 1555 1555 1.33
LINK C GLU B 262 N MLY B 263 1555 1555 1.33
LINK C MLY B 263 N PRO B 264 1555 1555 1.34
LINK C ILE B 336 N MLY B 337 1555 1555 1.33
LINK C MLY B 337 N LEU B 338 1555 1555 1.33
LINK C TYR B 351 N MLY B 352 1555 1555 1.33
LINK C MLY B 352 N ASN B 353 1555 1555 1.33
LINK C ILE B 364 N MLY B 365 1555 1555 1.33
LINK C MLY B 365 N GLN B 366 1555 1555 1.33
LINK C ASN D 154 N MLY D 155 1555 1555 1.33
LINK C MLY D 155 N TYR D 156 1555 1555 1.33
LINK C TRP D 165 N MLY D 166 1555 1555 1.33
LINK C MLY D 166 N MET D 167 1555 1555 1.33
LINK SG CYS C 114 ZN ZN C 201 1555 1555 2.30
LINK ND1 HIS C 116 ZN ZN C 201 1555 1555 2.06
LINK SG CYS C 119 ZN ZN C 201 1555 1555 2.31
LINK SG CYS C 152 ZN ZN C 201 1555 1555 2.32
LINK SG CYS D 114 ZN ZN D 201 1555 1555 2.32
LINK ND1 HIS D 116 ZN ZN D 201 1555 1555 2.03
LINK SG CYS D 119 ZN ZN D 201 1555 1555 2.32
LINK SG CYS D 152 ZN ZN D 201 1555 1555 2.30
SITE 1 AC1 4 CYS C 114 HIS C 116 CYS C 119 CYS C 152
SITE 1 AC2 4 CYS D 114 HIS D 116 CYS D 119 CYS D 152
CRYST1 52.701 83.841 132.508 90.00 92.57 90.00 P 1 21 1 4
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 0.018975 0.000000 0.000852 0.00000
SCALE2 0.000000 0.011927 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007554 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
