HEADER TRANSFERASE 20-MAY-15 4ZXT
TITLE COMPLEX OF ERK2 WITH CATECHOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED KINASE 2, ERK-
COMPND 5 2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED PROTEIN KINASE
COMPND 6 2, MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 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: MAPK1, ERK2, PRKM1, PRKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CATECHOL COMPLEX, MITOGEN-ACTIVATED PROTEIN KINASE, SIGNAL-REGULATED
KEYWDS 2 KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.KURINOV,M.MALAKHOVA
REVDAT 2 05-OCT-16 4ZXT 1 JRNL
REVDAT 1 25-MAY-16 4ZXT 0
JRNL AUTH Y.LIM DO,S.H.SHIN,M.H.LEE,M.MALAKHOVA,I.KURINOV,Q.WU,J.XU,
JRNL AUTH 2 Y.JIANG,Z.DONG,K.LIU,K.Y.LEE,K.B.BAE,B.Y.CHOI,Y.DENG,A.BODE,
JRNL AUTH 3 Z.DONG
JRNL TITL A NATURAL SMALL MOLECULE, CATECHOL, INDUCES C-MYC
JRNL TITL 2 DEGRADATION BY DIRECTLY TARGETING ERK2 IN LUNG CANCER.
JRNL REF ONCOTARGET V. 7 35001 2016
JRNL REFN ESSN 1949-2553
JRNL PMID 27167001
JRNL DOI 10.18632/ONCOTARGET.9223
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 25363
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1269
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 43.7760 - 4.1592 1.00 2735 145 0.1693 0.1659
REMARK 3 2 4.1592 - 3.3016 1.00 2691 141 0.1420 0.1641
REMARK 3 3 3.3016 - 2.8844 1.00 2672 141 0.1546 0.2079
REMARK 3 4 2.8844 - 2.6207 1.00 2705 142 0.1499 0.1864
REMARK 3 5 2.6207 - 2.4329 1.00 2657 141 0.1433 0.1783
REMARK 3 6 2.4329 - 2.2894 1.00 2645 139 0.1392 0.1966
REMARK 3 7 2.2894 - 2.1748 1.00 2706 141 0.1466 0.2054
REMARK 3 8 2.1748 - 2.0801 1.00 2673 141 0.1560 0.1992
REMARK 3 9 2.0801 - 2.0000 0.98 2610 138 0.1651 0.2308
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.920
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 : 0.012 2975
REMARK 3 ANGLE : 1.329 4037
REMARK 3 CHIRALITY : 0.080 438
REMARK 3 PLANARITY : 0.007 519
REMARK 3 DIHEDRAL : 14.530 1131
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 7:109)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5686 12.2244 31.8880
REMARK 3 T TENSOR
REMARK 3 T11: 0.3473 T22: 0.3512
REMARK 3 T33: 0.2570 T12: 0.0529
REMARK 3 T13: -0.0124 T23: 0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 3.0633 L22: 1.1162
REMARK 3 L33: 4.8175 L12: -1.1041
REMARK 3 L13: -0.2490 L23: -1.5091
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: 0.0923 S13: 0.5949
REMARK 3 S21: 0.2115 S22: 0.1705 S23: -0.0208
REMARK 3 S31: -0.8269 S32: -0.6144 S33: -0.1017
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 110:336)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2663 6.8649 55.7652
REMARK 3 T TENSOR
REMARK 3 T11: 0.1289 T22: 0.0892
REMARK 3 T33: 0.1482 T12: 0.0371
REMARK 3 T13: 0.0301 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 2.8753 L22: 0.7419
REMARK 3 L33: 1.0558 L12: 1.0536
REMARK 3 L13: 0.7666 L23: 0.0715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: 0.0670 S13: 0.1252
REMARK 3 S21: -0.0223 S22: 0.0127 S23: -0.0249
REMARK 3 S31: -0.0101 S32: 0.0485 S33: -0.0358
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 337:357)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9752 6.4494 23.4623
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2420
REMARK 3 T33: 0.1260 T12: 0.0383
REMARK 3 T13: 0.0001 T23: 0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 7.8312 L22: 8.0713
REMARK 3 L33: 6.7103 L12: 2.9920
REMARK 3 L13: -0.0597 L23: -0.5496
REMARK 3 S TENSOR
REMARK 3 S11: 0.2279 S12: 0.7161 S13: -0.2672
REMARK 3 S21: -0.2276 S22: -0.0402 S23: -0.3202
REMARK 3 S31: 0.1234 S32: 0.5430 S33: -0.1838
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 4ZXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1-1.3 M AMMONIUM SULFATE, 2% PEG500
REMARK 280 MME, 0.1 M HEPES/NAOH, CRYSTALS SOAKED IN PRECIPITANT SOLUTION
REMARK 280 CONTAINING 2.5 MM CATECHOL IN 2.5% DMSO FOR ONE WEEK, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING 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 34.67050
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 TYR A 358
REMARK 465 ARG A 359
REMARK 465 SER A 360
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 GLU A 12 CG CD OE1 OE2
REMARK 470 MET A 13 CG SD CE
REMARK 470 VAL A 14 CG1 CG2
REMARK 470 ARG A 15 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 OD2 ASP A 167 O HOH A 501 1.94
REMARK 500 O HOH A 755 O HOH A 770 1.99
REMARK 500 O3 SO4 A 404 O HOH A 502 2.07
REMARK 500 O HOH A 502 O HOH A 762 2.09
REMARK 500 O1 SO4 A 403 O HOH A 503 2.14
REMARK 500 O HOH A 697 O HOH A 734 2.16
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 PRO A 11 C - N - CA ANGL. DEV. = 9.8 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 PRO A 11 -132.40 -35.78
REMARK 500 GLU A 12 -121.20 73.66
REMARK 500 VAL A 14 36.08 86.67
REMARK 500 ARG A 15 83.35 45.51
REMARK 500 ASN A 27 152.20 87.77
REMARK 500 ARG A 148 -0.36 74.80
REMARK 500 ASP A 149 43.70 -144.68
REMARK 500 ASP A 167 81.00 68.13
REMARK 500 ASP A 175 71.31 -150.73
REMARK 500 ASN A 201 15.77 -157.55
REMARK 500 LEU A 294 48.74 -98.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 27 LEU A 28 -142.40
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 CAQ A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N0S RELATED DB: PDB
DBREF 4ZXT A 1 360 UNP P28482 MK01_HUMAN 1 360
SEQRES 1 A 360 MET ALA ALA ALA ALA ALA ALA GLY ALA GLY PRO GLU MET
SEQRES 2 A 360 VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR THR
SEQRES 3 A 360 ASN LEU SER TYR ILE GLY GLU GLY ALA TYR GLY MET VAL
SEQRES 4 A 360 CYS SER ALA TYR ASP ASN VAL ASN LYS VAL ARG VAL ALA
SEQRES 5 A 360 ILE LYS LYS ILE SER PRO PHE GLU HIS GLN THR TYR CYS
SEQRES 6 A 360 GLN ARG THR LEU ARG GLU ILE LYS ILE LEU LEU ARG PHE
SEQRES 7 A 360 ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE ARG
SEQRES 8 A 360 ALA PRO THR ILE GLU GLN MET LYS ASP VAL TYR ILE VAL
SEQRES 9 A 360 GLN ASP LEU MET GLU THR ASP LEU TYR LYS LEU LEU LYS
SEQRES 10 A 360 THR GLN HIS LEU SER ASN ASP HIS ILE CYS TYR PHE LEU
SEQRES 11 A 360 TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA
SEQRES 12 A 360 ASN VAL LEU HIS ARG ASP LEU LYS PRO SER ASN LEU LEU
SEQRES 13 A 360 LEU ASN THR THR CME ASP LEU LYS ILE CME ASP PHE GLY
SEQRES 14 A 360 LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP HIS THR GLY
SEQRES 15 A 360 PHE LEU THR GLU TYR VAL ALA THR ARG TRP TYR ARG ALA
SEQRES 16 A 360 PRO GLU ILE MET LEU ASN SER LYS GLY TYR THR LYS SER
SEQRES 17 A 360 ILE ASP ILE TRP SER VAL GLY CYS ILE LEU ALA GLU MET
SEQRES 18 A 360 LEU SER ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR LEU
SEQRES 19 A 360 ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU GLY SER PRO
SEQRES 20 A 360 SER GLN GLU ASP LEU ASN CME ILE ILE ASN LEU LYS ALA
SEQRES 21 A 360 ARG ASN TYR LEU LEU SER LEU PRO HIS LYS ASN LYS VAL
SEQRES 22 A 360 PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP SER LYS ALA
SEQRES 23 A 360 LEU ASP LEU LEU ASP LYS MET LEU THR PHE ASN PRO HIS
SEQRES 24 A 360 LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO TYR
SEQRES 25 A 360 LEU GLU GLN TYR TYR ASP PRO SER ASP GLU PRO ILE ALA
SEQRES 26 A 360 GLU ALA PRO PHE LYS PHE ASP MET GLU LEU ASP ASP LEU
SEQRES 27 A 360 PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU THR
SEQRES 28 A 360 ALA ARG PHE GLN PRO GLY TYR ARG SER
MODRES 4ZXT CME A 161 CYS MODIFIED RESIDUE
MODRES 4ZXT CME A 166 CYS MODIFIED RESIDUE
MODRES 4ZXT CME A 254 CYS MODIFIED RESIDUE
HET CME A 161 18
HET CME A 166 18
HET CME A 254 19
HET CAQ A 401 14
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET NH4 A 405 1
HET NH4 A 406 1
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM CAQ CATECHOL
HETNAM SO4 SULFATE ION
HETNAM NH4 AMMONIUM ION
HETSYN CAQ 1,2-DIHYDROXYBENZENE
FORMUL 1 CME 3(C5 H11 N O3 S2)
FORMUL 2 CAQ C6 H6 O2
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 NH4 2(H4 N 1+)
FORMUL 8 HOH *299(H2 O)
HELIX 1 AA1 HIS A 61 PHE A 78 1 18
HELIX 2 AA2 THR A 94 MET A 98 5 5
HELIX 3 AA3 LEU A 112 GLN A 119 1 8
HELIX 4 AA4 SER A 122 ALA A 143 1 22
HELIX 5 AA5 LYS A 151 SER A 153 5 3
HELIX 6 AA6 ASP A 175 ASP A 179 5 5
HELIX 7 AA7 THR A 190 ARG A 194 5 5
HELIX 8 AA8 ALA A 195 ASN A 201 1 7
HELIX 9 AA9 LYS A 207 ASN A 224 1 18
HELIX 10 AB1 HIS A 232 GLY A 245 1 14
HELIX 11 AB2 SER A 248 CME A 254 1 7
HELIX 12 AB3 ASN A 257 LEU A 267 1 11
HELIX 13 AB4 PRO A 274 PHE A 279 1 6
HELIX 14 AB5 ASP A 283 LEU A 294 1 12
HELIX 15 AB6 GLU A 303 ALA A 309 1 7
HELIX 16 AB7 HIS A 310 GLU A 314 5 5
HELIX 17 AB8 ASP A 318 GLU A 322 5 5
HELIX 18 AB9 PRO A 339 THR A 351 1 13
HELIX 19 AC1 ALA A 352 GLN A 355 5 4
SHEET 1 AA1 5 TYR A 25 GLU A 33 0
SHEET 2 AA1 5 MET A 38 ASP A 44 -1 O TYR A 43 N THR A 26
SHEET 3 AA1 5 VAL A 49 ILE A 56 -1 O VAL A 51 N ALA A 42
SHEET 4 AA1 5 VAL A 101 ASP A 106 -1 O VAL A 101 N ILE A 56
SHEET 5 AA1 5 ASP A 88 ILE A 90 -1 N ILE A 90 O TYR A 102
SHEET 1 AA2 3 THR A 110 ASP A 111 0
SHEET 2 AA2 3 LEU A 155 LEU A 157 -1 O LEU A 157 N THR A 110
SHEET 3 AA2 3 LEU A 163 ILE A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 AA3 2 VAL A 145 LEU A 146 0
SHEET 2 AA3 2 ARG A 172 VAL A 173 -1 O ARG A 172 N LEU A 146
LINK C THR A 160 N CME A 161 1555 1555 1.33
LINK C CME A 161 N ASP A 162 1555 1555 1.33
LINK C ILE A 165 N CME A 166 1555 1555 1.33
LINK C CME A 166 N ASP A 167 1555 1555 1.32
LINK C ASN A 253 N CME A 254 1555 1555 1.34
LINK C CME A 254 N ILE A 255 1555 1555 1.32
SITE 1 AC1 4 ALA A 52 GLN A 105 ASP A 106 MET A 108
SITE 1 AC2 6 ARG A 191 ARG A 194 TYR A 233 HOH A 522
SITE 2 AC2 6 HOH A 535 HOH A 578
SITE 1 AC3 2 LYS A 207 HOH A 503
SITE 1 AC4 6 ASP A 124 TYR A 128 ILE A 256 ARG A 261
SITE 2 AC4 6 TYR A 316 HOH A 502
SITE 1 AC5 5 PRO A 247 SER A 248 ASP A 251 HOH A 579
SITE 2 AC5 5 HOH A 702
SITE 1 AC6 6 ASP A 179 SER A 202 GLY A 204 TYR A 205
SITE 2 AC6 6 THR A 206 HOH A 582
CRYST1 48.588 69.341 59.589 90.00 108.76 90.00 P 1 21 1 2
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 0.020581 0.000000 0.006989 0.00000
SCALE2 0.000000 0.014421 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017723 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
