HEADER TRANSFERASE 26-JAN-17 5MYC
TITLE CRYSTAL STRUCTURE OF HUMAN 14-3-3 SIGMA IN COMPLEX WITH LRRK2 PEPTIDE
TITLE 2 PS910
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN SIGMA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EPITHELIAL CELL MARKER PROTEIN 1,STRATIFIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LEUCINE-RICH REPEAT SERINE/THREONINE-PROTEIN KINASE 2;
COMPND 8 CHAIN: P;
COMPND 9 SYNONYM: DARDARIN;
COMPND 10 EC: 2.7.11.1;
COMPND 11 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: SFN, HME1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
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 14-3-3 LRRK2 PHOSPHORYLATION PPI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.STEVERS,R.M.J.M.DE VRIES,C.OTTMANN
REVDAT 3 17-JAN-24 5MYC 1 LINK ATOM
REVDAT 2 05-APR-17 5MYC 1 JRNL
REVDAT 1 01-MAR-17 5MYC 0
JRNL AUTH L.M.STEVERS,R.M.DE VRIES,R.G.DOVESTON,L.G.MILROY,
JRNL AUTH 2 L.BRUNSVELD,C.OTTMANN
JRNL TITL STRUCTURAL INTERFACE BETWEEN LRRK2 AND 14-3-3 PROTEIN.
JRNL REF BIOCHEM. J. V. 474 1273 2017
JRNL REFN ESSN 1470-8728
JRNL PMID 28202711
JRNL DOI 10.1042/BCJ20161078
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11_2567: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 97760
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4897
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 41.8656 - 4.5325 1.00 3113 163 0.1682 0.1793
REMARK 3 2 4.5325 - 3.5982 1.00 3105 161 0.1324 0.1631
REMARK 3 3 3.5982 - 3.1436 1.00 3097 164 0.1377 0.1539
REMARK 3 4 3.1436 - 2.8562 1.00 3101 163 0.1498 0.1889
REMARK 3 5 2.8562 - 2.6515 1.00 3116 164 0.1599 0.1565
REMARK 3 6 2.6515 - 2.4952 1.00 3074 166 0.1460 0.1659
REMARK 3 7 2.4952 - 2.3703 1.00 3147 164 0.1501 0.1714
REMARK 3 8 2.3703 - 2.2671 1.00 3092 166 0.1488 0.1801
REMARK 3 9 2.2671 - 2.1798 1.00 3043 163 0.1443 0.1720
REMARK 3 10 2.1798 - 2.1046 1.00 3148 165 0.1501 0.1975
REMARK 3 11 2.1046 - 2.0388 1.00 3104 166 0.1536 0.1854
REMARK 3 12 2.0388 - 1.9805 1.00 3095 162 0.1648 0.1933
REMARK 3 13 1.9805 - 1.9284 1.00 3127 167 0.1719 0.2192
REMARK 3 14 1.9284 - 1.8813 1.00 3073 159 0.1703 0.1748
REMARK 3 15 1.8813 - 1.8386 1.00 3086 158 0.1738 0.1721
REMARK 3 16 1.8386 - 1.7994 1.00 3116 167 0.1753 0.2013
REMARK 3 17 1.7994 - 1.7635 1.00 3127 165 0.1850 0.2056
REMARK 3 18 1.7635 - 1.7302 1.00 3081 163 0.1900 0.1697
REMARK 3 19 1.7302 - 1.6993 1.00 3054 161 0.1930 0.1989
REMARK 3 20 1.6993 - 1.6705 1.00 3131 164 0.1872 0.2181
REMARK 3 21 1.6705 - 1.6435 1.00 3137 163 0.2041 0.2045
REMARK 3 22 1.6435 - 1.6182 1.00 3051 163 0.2179 0.2696
REMARK 3 23 1.6182 - 1.5944 1.00 3149 166 0.2330 0.2529
REMARK 3 24 1.5944 - 1.5720 1.00 3133 163 0.2449 0.2557
REMARK 3 25 1.5720 - 1.5507 1.00 3074 161 0.2411 0.2772
REMARK 3 26 1.5507 - 1.5306 1.00 3095 167 0.2482 0.2478
REMARK 3 27 1.5306 - 1.5115 1.00 3083 161 0.2529 0.2877
REMARK 3 28 1.5115 - 1.4932 1.00 3122 167 0.2615 0.2754
REMARK 3 29 1.4932 - 1.4759 1.00 3100 165 0.2682 0.3382
REMARK 3 30 1.4759 - 1.4593 0.93 2889 150 0.3014 0.3383
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.550
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 : 0.006 2120
REMARK 3 ANGLE : 0.750 2882
REMARK 3 CHIRALITY : 0.060 314
REMARK 3 PLANARITY : 0.004 377
REMARK 3 DIHEDRAL : 19.178 853
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 5MYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200003241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978620
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116840
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.088
REMARK 200 RESOLUTION RANGE LOW (A) : 45.618
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 11.80
REMARK 200 R MERGE FOR SHELL (I) : 1.08600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5BTV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, NACL2, PEG400, GLYCEROL, PH
REMARK 280 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 31.34450
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 31.34450
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 41.25850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.20550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.25850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.20550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.34450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.25850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.20550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.34450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.25850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.20550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 224.82200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 125.37800
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 301 LIES ON A SPECIAL POSITION.
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 VAL P 367
REMARK 465 LYS P 368
REMARK 465 LYS P 369
REMARK 465 ASP P 382
REMARK 465 ALA P 383
REMARK 465 VAL P 384
REMARK 465 LEU P 385
REMARK 465 GLN P 386
REMARK 465 ARG P 387
REMARK 465 CYS P 388
REMARK 465 SER P 389
REMARK 465 PRO P 390
REMARK 465 ASN P 391
REMARK 465 LEU P 392
REMARK 465 GLN P 393
REMARK 465 ARG P 394
REMARK 465 HIS P 395
REMARK 465 SER P 396
REMARK 465 ASN P 397
REMARK 465 SEP P 398
REMARK 465 LEU P 399
REMARK 465 GLY P 400
REMARK 465 PRO P 401
REMARK 465 ILE P 402
REMARK 465 PHE P 403
REMARK 465 ASP P 404
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 72 CG CD OE1 OE2
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 O HOH A 490 O HOH A 749 1.67
REMARK 500 O HOH A 495 O HOH A 583 1.81
REMARK 500 O HOH A 676 O HOH A 750 1.84
REMARK 500 O HOH A 620 O HOH A 685 1.95
REMARK 500 O HOH A 414 O HOH A 672 1.96
REMARK 500 O HOH A 607 O HOH A 655 1.98
REMARK 500 O HOH A 490 O HOH A 656 1.99
REMARK 500 O HOH A 651 O HOH A 692 2.01
REMARK 500 O HOH A 664 O HOH A 673 2.07
REMARK 500 O HOH A 526 O HOH A 736 2.07
REMARK 500 O HOH A 413 O HOH A 443 2.14
REMARK 500 O HOH A 656 O HOH A 749 2.14
REMARK 500 O HOH A 565 O HOH A 616 2.17
REMARK 500 O HOH A 646 O HOH A 662 2.17
REMARK 500 O HOH A 425 O HOH A 454 2.18
REMARK 500 O HOH A 591 O HOH A 689 2.19
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 O HOH A 451 O HOH A 694 4577 1.75
REMARK 500 O HOH A 683 O HOH A 751 8577 2.11
REMARK 500 O HOH A 747 O HOH A 761 2874 2.15
REMARK 500 O HOH A 698 O HOH A 727 6775 2.15
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 ARG A 18 77.50 -104.45
REMARK 500 HIS A 106 40.11 -144.34
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 795 DISTANCE = 6.07 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 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE2
REMARK 620 2 GLU A 2 OE2 0.0
REMARK 620 3 HOH A 491 O 76.1 76.1
REMARK 620 4 HOH A 491 O 82.1 82.1 150.8
REMARK 620 5 HOH A 651 O 82.4 82.4 131.8 62.4
REMARK 620 6 HOH A 651 O 137.5 137.5 62.4 131.9 132.4
REMARK 620 7 HOH A 692 O 87.6 87.6 88.6 109.9 47.5 99.7
REMARK 620 8 HOH A 692 O 168.3 168.3 109.9 88.6 99.7 47.5 102.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 35 OE1
REMARK 620 2 GLU A 35 OE2 50.4
REMARK 620 3 GLU A 110 O 86.5 87.8
REMARK 620 4 GLU A 188 OE2 88.5 121.7 44.7
REMARK 620 5 HOH A 436 O 85.9 122.1 48.6 4.8
REMARK 620 6 HOH A 570 O 85.7 119.5 44.6 2.9 3.9
REMARK 620 7 HOH A 665 O 84.4 120.4 47.7 5.2 1.7 3.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 416 O
REMARK 620 2 HOH A 453 O 116.9
REMARK 620 3 HOH A 677 O 158.8 70.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304
DBREF 5MYC A 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5MYC P 367 404 UNP Q5S007 LRRK2_HUMAN 904 941
SEQADV 5MYC GLY A -4 UNP P31947 EXPRESSION TAG
SEQADV 5MYC ALA A -3 UNP P31947 EXPRESSION TAG
SEQADV 5MYC MET A -2 UNP P31947 EXPRESSION TAG
SEQADV 5MYC GLY A -1 UNP P31947 EXPRESSION TAG
SEQADV 5MYC SER A 0 UNP P31947 EXPRESSION TAG
SEQRES 1 A 236 GLY ALA MET GLY SER MET GLU ARG ALA SER LEU ILE GLN
SEQRES 2 A 236 LYS ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP
SEQRES 3 A 236 MET ALA ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU
SEQRES 4 A 236 GLU LEU SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA
SEQRES 5 A 236 TYR LYS ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG
SEQRES 6 A 236 VAL LEU SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY
SEQRES 7 A 236 SER GLU GLU LYS GLY PRO GLU VAL ARG GLU TYR ARG GLU
SEQRES 8 A 236 LYS VAL GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL
SEQRES 9 A 236 LEU GLY LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY
SEQRES 10 A 236 ASP ALA GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY
SEQRES 11 A 236 ASP TYR TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP
SEQRES 12 A 236 ASP LYS LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR
SEQRES 13 A 236 GLN GLU ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO
SEQRES 14 A 236 THR ASN PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER
SEQRES 15 A 236 VAL PHE HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA
SEQRES 16 A 236 ILE SER LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA
SEQRES 17 A 236 ASP LEU HIS THR LEU SER GLU ASP SER TYR LYS ASP SER
SEQRES 18 A 236 THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU
SEQRES 19 A 236 TRP THR
SEQRES 1 P 38 VAL LYS LYS LYS SER ASN SEP ILE SER VAL GLY GLU PHE
SEQRES 2 P 38 TYR ARG ASP ALA VAL LEU GLN ARG CYS SER PRO ASN LEU
SEQRES 3 P 38 GLN ARG HIS SER ASN SEP LEU GLY PRO ILE PHE ASP
MODRES 5MYC SEP P 373 SER MODIFIED RESIDUE
HET SEP P 373 10
HET CA A 301 1
HET CA A 302 1
HET CL A 303 1
HET NA A 304 1
HETNAM SEP PHOSPHOSERINE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 3 CA 2(CA 2+)
FORMUL 5 CL CL 1-
FORMUL 6 NA NA 1+
FORMUL 7 HOH *413(H2 O)
HELIX 1 AA1 GLU A 2 ALA A 16 1 15
HELIX 2 AA2 ARG A 18 LYS A 32 1 15
HELIX 3 AA3 SER A 37 ASN A 70 1 34
HELIX 4 AA4 PRO A 79 SER A 105 1 27
HELIX 5 AA5 HIS A 106 ALA A 111 1 6
HELIX 6 AA6 ASP A 113 ALA A 135 1 23
HELIX 7 AA7 ASP A 139 MET A 162 1 24
HELIX 8 AA8 ASN A 166 ILE A 183 1 18
HELIX 9 AA9 SER A 186 ALA A 203 1 18
HELIX 10 AB1 ASP A 204 LEU A 208 5 5
HELIX 11 AB2 SER A 209 THR A 231 1 23
HELIX 12 AB3 SER P 375 ARG P 381 1 7
LINK C ASN P 372 N SEP P 373 1555 1555 1.33
LINK C SEP P 373 N ILE P 374 1555 1555 1.33
LINK OE2 GLU A 2 CA CA A 301 1555 1555 2.42
LINK OE2 GLU A 2 CA CA A 301 1555 3856 2.42
LINK OE1 GLU A 35 CA CA A 302 1555 6774 2.69
LINK OE2 GLU A 35 CA CA A 302 1555 6774 2.43
LINK O GLU A 110 CA CA A 302 1555 6774 2.31
LINK OE2 GLU A 188 CA CA A 302 1555 1555 2.42
LINK CA CA A 301 O HOH A 491 1555 1555 2.43
LINK CA CA A 301 O HOH A 491 1555 3856 2.43
LINK CA CA A 301 O HOH A 651 1555 1555 2.32
LINK CA CA A 301 O HOH A 651 1555 3856 2.32
LINK CA CA A 301 O HOH A 692 1555 1555 2.63
LINK CA CA A 301 O HOH A 692 1555 3856 2.63
LINK CA CA A 302 O HOH A 436 1555 6775 2.42
LINK CA CA A 302 O HOH A 570 1555 1555 2.35
LINK CA CA A 302 O HOH A 665 1555 6775 2.39
LINK NA NA A 304 O HOH A 416 1555 1555 2.35
LINK NA NA A 304 O HOH A 453 1555 1555 2.90
LINK NA NA A 304 O HOH A 677 1555 1555 2.21
CISPEP 1 SER A 105 HIS A 106 0 6.09
SITE 1 AC1 4 GLU A 2 HOH A 491 HOH A 651 HOH A 692
SITE 1 AC2 6 GLU A 35 GLU A 110 GLU A 188 HOH A 436
SITE 2 AC2 6 HOH A 570 HOH A 665
SITE 1 AC3 4 LYS A 9 LYS A 87 HOH A 652 HOH A 735
SITE 1 AC4 6 LEU A 121 LYS A 124 GLU A 153 HOH A 416
SITE 2 AC4 6 HOH A 453 HOH A 677
CRYST1 82.517 112.411 62.689 90.00 90.00 90.00 C 2 2 21 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 0.012119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008896 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015952 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
