HEADER PEPTIDE BINDING PROTEIN 21-JUN-17 5W8F
TITLE CRYSTAL STRUCTURE OF HUMAN MCL-1 IN COMPLEX WITH MODIFIED BIM BH3
TITLE 2 PEPTIDE SAH-MS1-14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL-
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 172-320;
COMPND 6 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN
COMPND 7 EAT/MCL1,MCL1/EAT;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MODIFIED BIM BH3 PEPTIDE SAH-MS1-14;
COMPND 11 CHAIN: B;
COMPND 12 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: MCL1, BCL2L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS STAPLED PEPTIDE, BCL-2 FAMILY, BH3 DOMAIN, APOPTOSIS, PEPTIDE BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.REZAEI ARAGHI,J.M.JENSON,R.A.GRANT,A.E.KEATING
REVDAT 3 14-FEB-18 5W8F 1 JRNL
REVDAT 2 31-JAN-18 5W8F 1 JRNL
REVDAT 1 17-JAN-18 5W8F 0
JRNL AUTH R.REZAEI ARAGHI,G.H.BIRD,J.A.RYAN,J.M.JENSON,M.GODES,
JRNL AUTH 2 J.R.PRITZ,R.A.GRANT,A.LETAI,L.D.WALENSKY,A.E.KEATING
JRNL TITL ITERATIVE OPTIMIZATION YIELDS MCL-1-TARGETING STAPLED
JRNL TITL 2 PEPTIDES WITH SELECTIVE CYTOTOXICITY TO MCL-1-DEPENDENT
JRNL TITL 3 CANCER CELLS.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E886 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29339518
JRNL DOI 10.1073/PNAS.1712952115
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 16785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 840
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 19.6165 - 3.3570 1.00 2844 150 0.2123 0.2518
REMARK 3 2 3.3570 - 2.6667 1.00 2681 142 0.2620 0.3329
REMARK 3 3 2.6667 - 2.3302 1.00 2632 138 0.2683 0.3068
REMARK 3 4 2.3302 - 2.1174 1.00 2603 138 0.2773 0.3077
REMARK 3 5 2.1174 - 1.9658 1.00 2597 136 0.2990 0.3494
REMARK 3 6 1.9658 - 1.8500 1.00 2588 136 0.3378 0.3853
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.510
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 : 0.007 1405
REMARK 3 ANGLE : 0.719 1897
REMARK 3 CHIRALITY : 0.040 206
REMARK 3 PLANARITY : 0.005 243
REMARK 3 DIHEDRAL : 15.940 846
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 5W8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228597.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16798
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 19.615
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.84
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 11.85
REMARK 200 R MERGE FOR SHELL (I) : 1.85000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 3MK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVIOR : 25% PEG 3350, 50MM TRIS PH
REMARK 280 9.0, 0.2 M AMMONIUM ACETATE; PROTEIN: 408 UM IN 20 MM TRIS , 10
REMARK 280 MM TCEP, 5MM ZN2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.72000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 23.42500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 23.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.86000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 23.42500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 23.42500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 125.58000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 23.42500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 23.42500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.86000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 23.42500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 23.42500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 125.58000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.72000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 171
REMARK 465 ILE B 1
REMARK 465 ARG B 21
REMARK 465 NH2 B 22
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2
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 HH12 ARG A 300 O HOH A 504 1.50
REMARK 500 O HOH A 511 O HOH A 514 1.95
REMARK 500 O HOH A 527 O HOH A 545 2.02
REMARK 500 OG1 THR A 259 O HOH A 501 2.10
REMARK 500 OD2 ASP A 296 O HOH A 502 2.11
REMARK 500 OG SER A 285 O HOH A 503 2.13
REMARK 500 NH1 ARG A 300 O HOH A 504 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HE2 HIS A 252 ZN ZN A 401 5555 1.29
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 MET A 199 -70.04 -68.87
REMARK 500 ASP A 236 77.08 45.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 224 NE2
REMARK 620 2 HOH A 552 O 108.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 240 OE2
REMARK 620 2 CYS A 286 SG 113.2
REMARK 620 3 HIS A 252 NE2 91.2 93.3
REMARK 620 4 HOH A 551 O 114.3 112.8 42.6
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5W89 RELATED DB: PDB
DBREF 5W8F A 172 320 UNP Q07820 MCL1_HUMAN 172 320
DBREF 5W8F B 1 22 PDB 5W8F 5W8F 1 22
SEQADV 5W8F GLY A 171 UNP Q07820 EXPRESSION TAG
SEQRES 1 A 150 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 A 150 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 A 150 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 A 150 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 A 150 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 A 150 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 A 150 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 A 150 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 A 150 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 A 150 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 A 150 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 A 150 GLY PHE VAL GLU PHE PHE HIS
SEQRES 1 B 22 ILE TRP NLE MK8 GLN SER LEU MK8 ARG LEU GLY ASP GLU
SEQRES 2 B 22 ILE ASN ALA TYR TYR ALA ARG ARG NH2
HET NLE B 3 18
HET MK8 B 4 22
HET MK8 B 8 22
HET ZN A 401 1
HET ZN A 402 1
HETNAM NLE NORLEUCINE
HETNAM MK8 2-METHYL-L-NORLEUCINE
HETNAM ZN ZINC ION
FORMUL 2 NLE C6 H13 N O2
FORMUL 2 MK8 2(C7 H15 N O2)
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *66(H2 O)
HELIX 1 AA1 ASP A 172 GLY A 192 1 21
HELIX 2 AA2 SER A 202 HIS A 224 1 23
HELIX 3 AA3 HIS A 224 ASP A 236 1 13
HELIX 4 AA4 ASP A 241 SER A 255 1 15
HELIX 5 AA5 ASN A 260 ILE A 281 1 22
HELIX 6 AA6 GLN A 283 SER A 285 5 3
HELIX 7 AA7 CYS A 286 GLN A 309 1 24
HELIX 8 AA8 ARG A 310 PHE A 319 1 10
HELIX 9 AA9 NLE B 3 ARG B 20 1 18
LINK NE2 HIS A 224 ZN ZN A 402 1555 1555 2.28
LINK OE2 GLU A 240 ZN ZN A 401 1555 1555 2.09
LINK SG CYS A 286 ZN ZN A 401 1555 1555 2.19
LINK C TRP B 2 N NLE B 3 1555 1555 1.32
LINK C NLE B 3 N MK8 B 4 1555 1555 1.43
LINK C MK8 B 4 N GLN B 5 1555 1555 1.35
LINK CE MK8 B 4 CE MK8 B 8 1555 1555 1.39
LINK C LEU B 7 N MK8 B 8 1555 1555 1.44
LINK C MK8 B 8 N ARG B 9 1555 1555 1.33
LINK ZN ZN A 402 O HOH A 552 1555 1555 2.08
LINK NE2 HIS A 252 ZN ZN A 401 1555 5555 2.08
LINK ZN ZN A 401 O HOH A 551 1555 5545 2.30
SITE 1 AC1 4 GLU A 240 HIS A 252 CYS A 286 HOH A 551
SITE 1 AC2 2 HIS A 224 HOH A 552
CRYST1 46.850 46.850 167.440 90.00 90.00 90.00 P 41 21 2 8
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 0.021345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005972 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
