HEADER LYASE 10-AUG-13 4M6R
TITLE STRUCTURAL AND BIOCHEMICAL BASIS FOR THE INHIBITION OF CELL DEATH BY
TITLE 2 APIP, A METHIONINE SALVAGE ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 20-242;
COMPND 5 SYNONYM: MTRU-1-P DEHYDRATASE, APAF1-INTERACTING PROTEIN, HAPIP;
COMPND 6 EC: 4.2.1.109;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APIP, CGI-29;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APIP, MTNB, CLASS II ALDOLASE FAMILY, DEHYDRATASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.KANG,S.H.HONG,H.M.LEE,N.Y.KIM,Y.C.LIM,L.T.M.LE,B.LIM,H.C.KIM,
AUTHOR 2 T.Y.KIM,H.ASHIDA,A.YOKOTA,S.S.HAH,K.H.CHUN,Y.K.JUNG,J.K.YANG
REVDAT 2 20-MAR-24 4M6R 1 REMARK SEQADV LINK
REVDAT 1 29-JAN-14 4M6R 0
JRNL AUTH W.KANG,S.H.HONG,H.M.LEE,N.Y.KIM,Y.C.LIM,L.T.M.LE,B.LIM,
JRNL AUTH 2 H.C.KIM,T.Y.KIM,H.ASHIDA,A.YOKOTA,S.S.HAH,K.H.CHUN,Y.K.JUNG,
JRNL AUTH 3 J.K.YANG
JRNL TITL STRUCTURAL AND BIOCHEMICAL BASIS FOR THE INHIBITION OF CELL
JRNL TITL 2 DEATH BY APIP, A METHIONINE SALVAGE ENZYME.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 581 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24367089
JRNL DOI 10.1073/PNAS.1308768111
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 68405
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3616
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4122
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 567
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : -1.40000
REMARK 3 B33 (A**2) : 1.98000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.167
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.302
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7221 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9742 ; 2.049 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 889 ; 6.555 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 304 ;38.744 ;24.211
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1313 ;17.153 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.788 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1036 ; 0.210 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5396 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4438 ; 1.216 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7177 ; 2.168 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2783 ; 3.072 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2565 ; 4.969 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 21 A 182 2
REMARK 3 1 B 21 B 182 2
REMARK 3 1 C 21 C 182 2
REMARK 3 1 D 21 D 182 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 648 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 648 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 648 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 648 ; 0.07 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 628 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 628 ; 0.09 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 628 ; 0.08 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 628 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 648 ; 0.32 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 648 ; 0.50 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 648 ; 0.43 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 648 ; 0.39 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 628 ; 0.34 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 628 ; 0.41 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 628 ; 0.43 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 628 ; 0.36 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 184 A 232 2
REMARK 3 1 B 184 B 232 2
REMARK 3 1 C 184 C 232 2
REMARK 3 1 D 184 D 232 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 196 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 196 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 196 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 196 ; 0.06 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 A (A): 199 ; 0.08 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 199 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 199 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 199 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 196 ; 0.42 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 196 ; 0.47 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 196 ; 0.51 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 196 ; 0.58 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 199 ; 0.38 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 199 ; 0.44 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 199 ; 0.50 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 199 ; 0.48 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 233 A 242 4
REMARK 3 1 B 233 B 242 4
REMARK 3 1 C 233 C 242 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 71 ; 0.24 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 71 ; 0.15 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 C (A): 71 ; 0.24 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 71 ; 3.29 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 71 ; 2.89 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 71 ; 6.06 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4M6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000, 0.91977, 0.91957,
REMARK 200 0.90633
REMARK 200 MONOCHROMATOR : DCM SI (111) 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 : 72069
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 96.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04M CITRIC ACID, 0.06M BIS-TRIS
REMARK 280 PROPANE, 5%(V/V) GLYCEROL, 21%(W/V) PEG 3350, PH 6.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.04950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.04950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.51750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.86750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.51750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.86750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.04950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.51750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.86750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.04950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.51750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.86750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 D 240
REMARK 465 ILE D 241
REMARK 465 VAL D 242
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 CD1 ILE B 58 O HOH B 531 1.83
REMARK 500 O HOH D 463 O HOH D 528 1.91
REMARK 500 O ILE C 48 O HOH C 467 1.95
REMARK 500 OG1 THR D 42 O HOH D 527 1.96
REMARK 500 OE1 GLN D 233 O HOH D 510 1.97
REMARK 500 O HOH D 435 O HOH D 525 1.99
REMARK 500 O HOH B 494 O HOH B 551 2.02
REMARK 500 CG LYS D 226 O HOH D 476 2.05
REMARK 500 OE2 GLU B 22 O HOH B 454 2.06
REMARK 500 O HOH B 495 O HOH B 547 2.07
REMARK 500 OD1 ASP B 72 O HOH B 504 2.08
REMARK 500 SG CYS B 188 O HOH B 512 2.08
REMARK 500 O HOH B 538 O HOH C 432 2.09
REMARK 500 O HOH C 415 O HOH C 475 2.12
REMARK 500 NE ARG D 131 O HOH D 467 2.14
REMARK 500 O GLU A 170 O HOH A 452 2.15
REMARK 500 O HOH C 481 O HOH D 475 2.16
REMARK 500 OD1 ASP A 72 O HOH A 516 2.17
REMARK 500 SG CYS C 188 O HOH C 506 2.18
REMARK 500 O HOH B 482 O HOH B 539 2.19
REMARK 500 O HOH C 401 O HOH C 489 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 133 CE1 PHE A 133 CZ 0.120
REMARK 500 ASP A 156 CB ASP A 156 CG -0.150
REMARK 500 ARG A 193 CD ARG A 193 NE -0.115
REMARK 500 ASP B 156 CB ASP B 156 CG -0.154
REMARK 500 TYR B 214 CE2 TYR B 214 CD2 0.091
REMARK 500 ASP C 156 CB ASP C 156 CG -0.153
REMARK 500 ALA C 178 CA ALA C 178 CB 0.138
REMARK 500 PHE D 128 CZ PHE D 128 CE2 0.149
REMARK 500 ASP D 156 CB ASP D 156 CG -0.215
REMARK 500 ARG D 193 CD ARG D 193 NE -0.108
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 VAL A 41 CG1 - CB - CG2 ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU A 127 CA - CB - CG ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP A 156 CB - CG - OD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG A 193 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 LEU B 31 CB - CG - CD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 VAL B 41 CG1 - CB - CG2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 LEU B 127 CA - CB - CG ANGL. DEV. = -15.1 DEGREES
REMARK 500 ASP B 156 CB - CG - OD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG B 193 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 VAL C 41 CG1 - CB - CG2 ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG C 108 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 156 CB - CG - OD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG C 193 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 VAL D 41 CG1 - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 ASP D 156 OD1 - CG - OD2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASP D 156 CB - CG - OD1 ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG D 193 CD - NE - CZ ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG D 193 NE - CZ - NH1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG D 193 NE - CZ - NH2 ANGL. DEV. = -11.9 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 THR A 44 -1.71 61.57
REMARK 500 ILE A 83 -63.62 -99.53
REMARK 500 HIS A 195 -63.51 -151.94
REMARK 500 VAL B 41 42.46 -140.77
REMARK 500 ILE B 83 -63.78 -99.41
REMARK 500 HIS B 195 -63.90 -149.65
REMARK 500 VAL C 41 43.49 -141.19
REMARK 500 THR C 44 -0.54 61.86
REMARK 500 ILE C 78 -18.96 -48.93
REMARK 500 ILE C 83 -67.69 -98.39
REMARK 500 HIS C 195 -65.82 -145.78
REMARK 500 VAL D 41 43.26 -142.62
REMARK 500 ILE D 83 -60.74 -97.89
REMARK 500 HIS D 195 -63.67 -149.44
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 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 115 NE2
REMARK 620 2 HIS A 117 NE2 98.1
REMARK 620 3 HIS A 195 NE2 91.8 100.3
REMARK 620 4 HOH A 425 O 79.5 176.8 81.9
REMARK 620 5 HOH A 481 O 96.8 98.9 157.7 79.4
REMARK 620 6 HOH D 446 O 167.3 93.2 91.9 89.0 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 486 O
REMARK 620 2 HIS B 115 NE2 160.3
REMARK 620 3 HIS B 117 NE2 98.1 100.6
REMARK 620 4 HIS B 195 NE2 89.2 94.2 98.9
REMARK 620 5 HOH B 492 O 72.3 88.3 167.8 88.6
REMARK 620 6 HOH B 494 O 71.0 98.6 102.2 152.8 68.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 424 O
REMARK 620 2 HIS C 115 NE2 163.3
REMARK 620 3 HIS C 117 NE2 94.2 99.8
REMARK 620 4 HIS C 195 NE2 92.9 94.1 98.1
REMARK 620 5 HOH C 443 O 78.4 91.9 92.2 167.0
REMARK 620 6 HOH C 448 O 82.6 82.8 174.9 86.1 83.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 418 O
REMARK 620 2 HIS D 115 NE2 159.7
REMARK 620 3 HIS D 117 NE2 99.0 98.4
REMARK 620 4 HIS D 195 NE2 93.5 93.9 99.7
REMARK 620 5 HOH D 415 O 75.8 91.9 96.3 162.0
REMARK 620 6 HOH D 462 O 72.2 88.8 167.0 90.6 72.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 301
DBREF 4M6R A 20 242 UNP Q96GX9 MTNB_HUMAN 20 242
DBREF 4M6R B 20 242 UNP Q96GX9 MTNB_HUMAN 20 242
DBREF 4M6R C 20 242 UNP Q96GX9 MTNB_HUMAN 20 242
DBREF 4M6R D 20 242 UNP Q96GX9 MTNB_HUMAN 20 242
SEQADV 4M6R MET A 19 UNP Q96GX9 EXPRESSION TAG
SEQADV 4M6R MET B 19 UNP Q96GX9 EXPRESSION TAG
SEQADV 4M6R MET C 19 UNP Q96GX9 EXPRESSION TAG
SEQADV 4M6R MET D 19 UNP Q96GX9 EXPRESSION TAG
SEQRES 1 A 224 MET ASP LYS GLU HIS PRO ARG TYR LEU ILE PRO GLU LEU
SEQRES 2 A 224 CYS LYS GLN PHE TYR HIS LEU GLY TRP VAL THR GLY THR
SEQRES 3 A 224 GLY GLY GLY ILE SER LEU LYS HIS GLY ASP GLU ILE TYR
SEQRES 4 A 224 ILE ALA PRO SER GLY VAL GLN LYS GLU ARG ILE GLN PRO
SEQRES 5 A 224 GLU ASP MET PHE VAL CYS ASP ILE ASN GLU LYS ASP ILE
SEQRES 6 A 224 SER GLY PRO SER PRO SER LYS LYS LEU LYS LYS SER GLN
SEQRES 7 A 224 CYS THR PRO LEU PHE MET ASN ALA TYR THR MET ARG GLY
SEQRES 8 A 224 ALA GLY ALA VAL ILE HIS THR HIS SER LYS ALA ALA VAL
SEQRES 9 A 224 MET ALA THR LEU LEU PHE PRO GLY ARG GLU PHE LYS ILE
SEQRES 10 A 224 THR HIS GLN GLU MET ILE LYS GLY ILE LYS LYS CYS THR
SEQRES 11 A 224 SER GLY GLY TYR TYR ARG TYR ASP ASP MET LEU VAL VAL
SEQRES 12 A 224 PRO ILE ILE GLU ASN THR PRO GLU GLU LYS ASP LEU LYS
SEQRES 13 A 224 ASP ARG MET ALA HIS ALA MET ASN GLU TYR PRO ASP SER
SEQRES 14 A 224 CYS ALA VAL LEU VAL ARG ARG HIS GLY VAL TYR VAL TRP
SEQRES 15 A 224 GLY GLU THR TRP GLU LYS ALA LYS THR MET CYS GLU CYS
SEQRES 16 A 224 TYR ASP TYR LEU PHE ASP ILE ALA VAL SER MET LYS LYS
SEQRES 17 A 224 VAL GLY LEU ASP PRO SER GLN LEU PRO VAL GLY GLU ASN
SEQRES 18 A 224 GLY ILE VAL
SEQRES 1 B 224 MET ASP LYS GLU HIS PRO ARG TYR LEU ILE PRO GLU LEU
SEQRES 2 B 224 CYS LYS GLN PHE TYR HIS LEU GLY TRP VAL THR GLY THR
SEQRES 3 B 224 GLY GLY GLY ILE SER LEU LYS HIS GLY ASP GLU ILE TYR
SEQRES 4 B 224 ILE ALA PRO SER GLY VAL GLN LYS GLU ARG ILE GLN PRO
SEQRES 5 B 224 GLU ASP MET PHE VAL CYS ASP ILE ASN GLU LYS ASP ILE
SEQRES 6 B 224 SER GLY PRO SER PRO SER LYS LYS LEU LYS LYS SER GLN
SEQRES 7 B 224 CYS THR PRO LEU PHE MET ASN ALA TYR THR MET ARG GLY
SEQRES 8 B 224 ALA GLY ALA VAL ILE HIS THR HIS SER LYS ALA ALA VAL
SEQRES 9 B 224 MET ALA THR LEU LEU PHE PRO GLY ARG GLU PHE LYS ILE
SEQRES 10 B 224 THR HIS GLN GLU MET ILE LYS GLY ILE LYS LYS CYS THR
SEQRES 11 B 224 SER GLY GLY TYR TYR ARG TYR ASP ASP MET LEU VAL VAL
SEQRES 12 B 224 PRO ILE ILE GLU ASN THR PRO GLU GLU LYS ASP LEU LYS
SEQRES 13 B 224 ASP ARG MET ALA HIS ALA MET ASN GLU TYR PRO ASP SER
SEQRES 14 B 224 CYS ALA VAL LEU VAL ARG ARG HIS GLY VAL TYR VAL TRP
SEQRES 15 B 224 GLY GLU THR TRP GLU LYS ALA LYS THR MET CYS GLU CYS
SEQRES 16 B 224 TYR ASP TYR LEU PHE ASP ILE ALA VAL SER MET LYS LYS
SEQRES 17 B 224 VAL GLY LEU ASP PRO SER GLN LEU PRO VAL GLY GLU ASN
SEQRES 18 B 224 GLY ILE VAL
SEQRES 1 C 224 MET ASP LYS GLU HIS PRO ARG TYR LEU ILE PRO GLU LEU
SEQRES 2 C 224 CYS LYS GLN PHE TYR HIS LEU GLY TRP VAL THR GLY THR
SEQRES 3 C 224 GLY GLY GLY ILE SER LEU LYS HIS GLY ASP GLU ILE TYR
SEQRES 4 C 224 ILE ALA PRO SER GLY VAL GLN LYS GLU ARG ILE GLN PRO
SEQRES 5 C 224 GLU ASP MET PHE VAL CYS ASP ILE ASN GLU LYS ASP ILE
SEQRES 6 C 224 SER GLY PRO SER PRO SER LYS LYS LEU LYS LYS SER GLN
SEQRES 7 C 224 CYS THR PRO LEU PHE MET ASN ALA TYR THR MET ARG GLY
SEQRES 8 C 224 ALA GLY ALA VAL ILE HIS THR HIS SER LYS ALA ALA VAL
SEQRES 9 C 224 MET ALA THR LEU LEU PHE PRO GLY ARG GLU PHE LYS ILE
SEQRES 10 C 224 THR HIS GLN GLU MET ILE LYS GLY ILE LYS LYS CYS THR
SEQRES 11 C 224 SER GLY GLY TYR TYR ARG TYR ASP ASP MET LEU VAL VAL
SEQRES 12 C 224 PRO ILE ILE GLU ASN THR PRO GLU GLU LYS ASP LEU LYS
SEQRES 13 C 224 ASP ARG MET ALA HIS ALA MET ASN GLU TYR PRO ASP SER
SEQRES 14 C 224 CYS ALA VAL LEU VAL ARG ARG HIS GLY VAL TYR VAL TRP
SEQRES 15 C 224 GLY GLU THR TRP GLU LYS ALA LYS THR MET CYS GLU CYS
SEQRES 16 C 224 TYR ASP TYR LEU PHE ASP ILE ALA VAL SER MET LYS LYS
SEQRES 17 C 224 VAL GLY LEU ASP PRO SER GLN LEU PRO VAL GLY GLU ASN
SEQRES 18 C 224 GLY ILE VAL
SEQRES 1 D 224 MET ASP LYS GLU HIS PRO ARG TYR LEU ILE PRO GLU LEU
SEQRES 2 D 224 CYS LYS GLN PHE TYR HIS LEU GLY TRP VAL THR GLY THR
SEQRES 3 D 224 GLY GLY GLY ILE SER LEU LYS HIS GLY ASP GLU ILE TYR
SEQRES 4 D 224 ILE ALA PRO SER GLY VAL GLN LYS GLU ARG ILE GLN PRO
SEQRES 5 D 224 GLU ASP MET PHE VAL CYS ASP ILE ASN GLU LYS ASP ILE
SEQRES 6 D 224 SER GLY PRO SER PRO SER LYS LYS LEU LYS LYS SER GLN
SEQRES 7 D 224 CYS THR PRO LEU PHE MET ASN ALA TYR THR MET ARG GLY
SEQRES 8 D 224 ALA GLY ALA VAL ILE HIS THR HIS SER LYS ALA ALA VAL
SEQRES 9 D 224 MET ALA THR LEU LEU PHE PRO GLY ARG GLU PHE LYS ILE
SEQRES 10 D 224 THR HIS GLN GLU MET ILE LYS GLY ILE LYS LYS CYS THR
SEQRES 11 D 224 SER GLY GLY TYR TYR ARG TYR ASP ASP MET LEU VAL VAL
SEQRES 12 D 224 PRO ILE ILE GLU ASN THR PRO GLU GLU LYS ASP LEU LYS
SEQRES 13 D 224 ASP ARG MET ALA HIS ALA MET ASN GLU TYR PRO ASP SER
SEQRES 14 D 224 CYS ALA VAL LEU VAL ARG ARG HIS GLY VAL TYR VAL TRP
SEQRES 15 D 224 GLY GLU THR TRP GLU LYS ALA LYS THR MET CYS GLU CYS
SEQRES 16 D 224 TYR ASP TYR LEU PHE ASP ILE ALA VAL SER MET LYS LYS
SEQRES 17 D 224 VAL GLY LEU ASP PRO SER GLN LEU PRO VAL GLY GLU ASN
SEQRES 18 D 224 GLY ILE VAL
HET ZN A 301 1
HET ZN B 301 1
HET ZN C 301 1
HET ZN D 301 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 HOH *567(H2 O)
HELIX 1 1 HIS A 23 LEU A 38 1 16
HELIX 2 2 VAL A 41 GLY A 45 5 5
HELIX 3 3 GLN A 64 ILE A 68 5 5
HELIX 4 4 GLN A 69 MET A 73 5 5
HELIX 5 5 SER A 87 LYS A 91 5 5
HELIX 6 6 CYS A 97 GLY A 109 1 13
HELIX 7 7 SER A 118 PHE A 128 1 11
HELIX 8 8 GLN A 138 ILE A 144 5 7
HELIX 9 9 GLU A 169 TYR A 184 1 16
HELIX 10 10 THR A 203 VAL A 227 1 25
HELIX 11 11 HIS B 23 LEU B 38 1 16
HELIX 12 12 VAL B 41 GLY B 45 5 5
HELIX 13 13 GLN B 64 ILE B 68 5 5
HELIX 14 14 GLN B 69 MET B 73 5 5
HELIX 15 15 SER B 87 LYS B 91 5 5
HELIX 16 16 CYS B 97 ARG B 108 1 12
HELIX 17 17 SER B 118 PHE B 128 1 11
HELIX 18 18 GLN B 138 ILE B 144 5 7
HELIX 19 19 GLU B 169 TYR B 184 1 16
HELIX 20 20 THR B 203 VAL B 227 1 25
HELIX 21 21 HIS C 23 LEU C 38 1 16
HELIX 22 22 VAL C 41 GLY C 45 5 5
HELIX 23 23 GLN C 64 ILE C 68 5 5
HELIX 24 24 GLN C 69 MET C 73 5 5
HELIX 25 25 SER C 87 LYS C 91 5 5
HELIX 26 26 CYS C 97 GLY C 109 1 13
HELIX 27 27 SER C 118 PHE C 128 1 11
HELIX 28 28 GLN C 138 ILE C 144 5 7
HELIX 29 29 GLU C 169 TYR C 184 1 16
HELIX 30 30 THR C 203 VAL C 227 1 25
HELIX 31 31 HIS D 23 LEU D 38 1 16
HELIX 32 32 VAL D 41 GLY D 45 5 5
HELIX 33 33 GLN D 64 ILE D 68 5 5
HELIX 34 34 GLN D 69 MET D 73 5 5
HELIX 35 35 SER D 87 LYS D 91 5 5
HELIX 36 36 CYS D 97 GLY D 109 1 13
HELIX 37 37 SER D 118 PHE D 128 1 11
HELIX 38 38 GLN D 138 ILE D 144 5 7
HELIX 39 39 GLU D 169 TYR D 184 1 16
HELIX 40 40 THR D 203 VAL D 227 1 25
SHEET 1 A 9 ASP A 82 SER A 84 0
SHEET 2 A 9 PHE A 74 CYS A 76 -1 N VAL A 75 O ILE A 83
SHEET 3 A 9 GLU A 55 ILE A 58 -1 N ILE A 56 O CYS A 76
SHEET 4 A 9 GLY A 47 HIS A 52 -1 N HIS A 52 O GLU A 55
SHEET 5 A 9 ALA A 112 THR A 116 -1 O HIS A 115 N GLY A 47
SHEET 6 A 9 GLY A 196 GLY A 201 -1 O VAL A 199 N ILE A 114
SHEET 7 A 9 ALA A 189 VAL A 192 -1 N VAL A 192 O GLY A 196
SHEET 8 A 9 MET A 158 ILE A 164 1 N ILE A 164 O LEU A 191
SHEET 9 A 9 GLU A 132 THR A 136 -1 N PHE A 133 O VAL A 161
SHEET 1 B 9 ASP B 82 SER B 84 0
SHEET 2 B 9 PHE B 74 CYS B 76 -1 N VAL B 75 O SER B 84
SHEET 3 B 9 GLU B 55 ILE B 58 -1 N ILE B 56 O CYS B 76
SHEET 4 B 9 GLY B 47 HIS B 52 -1 N HIS B 52 O GLU B 55
SHEET 5 B 9 ALA B 112 THR B 116 -1 O HIS B 115 N GLY B 47
SHEET 6 B 9 GLY B 196 GLY B 201 -1 O VAL B 199 N ILE B 114
SHEET 7 B 9 ALA B 189 VAL B 192 -1 N VAL B 192 O GLY B 196
SHEET 8 B 9 MET B 158 ILE B 164 1 N ILE B 164 O LEU B 191
SHEET 9 B 9 GLU B 132 THR B 136 -1 N ILE B 135 O LEU B 159
SHEET 1 C 9 ASP C 82 SER C 84 0
SHEET 2 C 9 PHE C 74 CYS C 76 -1 N VAL C 75 O ILE C 83
SHEET 3 C 9 GLU C 55 ILE C 58 -1 N ILE C 56 O CYS C 76
SHEET 4 C 9 GLY C 47 HIS C 52 -1 N HIS C 52 O GLU C 55
SHEET 5 C 9 ALA C 112 THR C 116 -1 O HIS C 115 N GLY C 47
SHEET 6 C 9 GLY C 196 GLY C 201 -1 O VAL C 199 N ILE C 114
SHEET 7 C 9 ALA C 189 VAL C 192 -1 N VAL C 192 O GLY C 196
SHEET 8 C 9 MET C 158 ILE C 164 1 N ILE C 164 O LEU C 191
SHEET 9 C 9 GLU C 132 THR C 136 -1 N PHE C 133 O VAL C 161
SHEET 1 D 9 ASP D 82 SER D 84 0
SHEET 2 D 9 PHE D 74 ASP D 77 -1 N VAL D 75 O SER D 84
SHEET 3 D 9 GLU D 55 ILE D 58 -1 N ILE D 56 O CYS D 76
SHEET 4 D 9 GLY D 47 HIS D 52 -1 N HIS D 52 O GLU D 55
SHEET 5 D 9 ALA D 112 THR D 116 -1 O HIS D 115 N GLY D 47
SHEET 6 D 9 GLY D 196 GLY D 201 -1 O VAL D 199 N ILE D 114
SHEET 7 D 9 ALA D 189 VAL D 192 -1 N VAL D 192 O GLY D 196
SHEET 8 D 9 MET D 158 ILE D 164 1 N ILE D 164 O LEU D 191
SHEET 9 D 9 GLU D 132 THR D 136 -1 N ILE D 135 O LEU D 159
LINK NE2 HIS A 115 ZN ZN A 301 1555 1555 2.10
LINK NE2 HIS A 117 ZN ZN A 301 1555 1555 2.13
LINK NE2 HIS A 195 ZN ZN A 301 1555 1555 2.25
LINK ZN ZN A 301 O HOH A 425 1555 1555 2.69
LINK ZN ZN A 301 O HOH A 481 1555 1555 2.40
LINK ZN ZN A 301 O HOH D 446 1555 1555 2.10
LINK O HOH A 486 ZN ZN B 301 1555 1555 2.22
LINK NE2 HIS B 115 ZN ZN B 301 1555 1555 2.08
LINK NE2 HIS B 117 ZN ZN B 301 1555 1555 2.08
LINK NE2 HIS B 195 ZN ZN B 301 1555 1555 2.13
LINK ZN ZN B 301 O HOH B 492 1555 1555 2.49
LINK ZN ZN B 301 O HOH B 494 1555 1555 2.16
LINK O HOH B 424 ZN ZN C 301 1555 1555 2.08
LINK NE2 HIS C 115 ZN ZN C 301 1555 1555 2.15
LINK NE2 HIS C 117 ZN ZN C 301 1555 1555 2.16
LINK NE2 HIS C 195 ZN ZN C 301 1555 1555 2.20
LINK ZN ZN C 301 O HOH C 443 1555 1555 2.18
LINK ZN ZN C 301 O HOH C 448 1555 1555 2.40
LINK O HOH C 418 ZN ZN D 301 1555 1555 2.15
LINK NE2 HIS D 115 ZN ZN D 301 1555 1555 2.12
LINK NE2 HIS D 117 ZN ZN D 301 1555 1555 2.10
LINK NE2 HIS D 195 ZN ZN D 301 1555 1555 2.14
LINK ZN ZN D 301 O HOH D 415 1555 1555 2.17
LINK ZN ZN D 301 O HOH D 462 1555 1555 2.30
SITE 1 AC1 6 HIS A 115 HIS A 117 HIS A 195 HOH A 425
SITE 2 AC1 6 HOH A 481 HOH D 446
SITE 1 AC2 6 HOH A 486 HIS B 115 HIS B 117 HIS B 195
SITE 2 AC2 6 HOH B 492 HOH B 494
SITE 1 AC3 6 HOH B 424 HIS C 115 HIS C 117 HIS C 195
SITE 2 AC3 6 HOH C 443 HOH C 448
SITE 1 AC4 6 HOH C 418 HIS D 115 HIS D 117 HIS D 195
SITE 2 AC4 6 HOH D 415 HOH D 462
CRYST1 107.035 107.735 192.099 90.00 90.00 90.00 C 2 2 21 32
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 0.009343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005206 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
