HEADER HYDROLASE 16-JUN-11 3SHQ
TITLE CRYSTAL STRUCTURE OF UBLCP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBLCP1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.3.16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CG6697, DMEL_CG6697, UBLCP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.XIAO,J.L.ENGEL
REVDAT 3 28-FEB-24 3SHQ 1 REMARK SEQADV LINK
REVDAT 2 30-NOV-11 3SHQ 1 JRNL
REVDAT 1 12-OCT-11 3SHQ 0
JRNL AUTH X.GUO,J.L.ENGEL,J.XIAO,V.S.TAGLIABRACCI,X.WANG,L.HUANG,
JRNL AUTH 2 J.E.DIXON
JRNL TITL UBLCP1 IS A 26S PROTEASOME PHOSPHATASE THAT REGULATES
JRNL TITL 2 NUCLEAR PROTEASOME ACTIVITY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 18649 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21949367
JRNL DOI 10.1073/PNAS.1113170108
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34919
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1753
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 36.0024 - 4.6025 1.00 2747 148 0.1803 0.2026
REMARK 3 2 4.6025 - 3.6543 1.00 2609 139 0.1580 0.1791
REMARK 3 3 3.6543 - 3.1927 1.00 2601 121 0.1808 0.2254
REMARK 3 4 3.1927 - 2.9009 1.00 2544 151 0.1900 0.1988
REMARK 3 5 2.9009 - 2.6930 1.00 2534 145 0.1944 0.2269
REMARK 3 6 2.6930 - 2.5343 1.00 2522 140 0.1891 0.2227
REMARK 3 7 2.5343 - 2.4074 1.00 2532 142 0.1860 0.2190
REMARK 3 8 2.4074 - 2.3026 1.00 2553 110 0.1771 0.1961
REMARK 3 9 2.3026 - 2.2140 1.00 2497 141 0.1743 0.1953
REMARK 3 10 2.2140 - 2.1376 1.00 2526 136 0.1715 0.1977
REMARK 3 11 2.1376 - 2.0708 1.00 2522 114 0.1729 0.1988
REMARK 3 12 2.0708 - 2.0116 1.00 2514 132 0.1687 0.2104
REMARK 3 13 2.0116 - 1.9600 0.99 2465 134 0.1895 0.1992
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 : 0.33
REMARK 3 B_SOL : 38.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.76110
REMARK 3 B22 (A**2) : -4.76110
REMARK 3 B33 (A**2) : 9.52220
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 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 2515
REMARK 3 ANGLE : 0.948 3395
REMARK 3 CHIRALITY : 0.070 373
REMARK 3 PLANARITY : 0.003 430
REMARK 3 DIHEDRAL : 12.439 953
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2340 1.5725 7.9876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1604 T22: 0.1586
REMARK 3 T33: 0.1862 T12: -0.0056
REMARK 3 T13: -0.0017 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.7663 L22: 2.5912
REMARK 3 L33: 1.1901 L12: 0.3056
REMARK 3 L13: 0.1769 L23: 0.5555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0760 S12: -0.0312 S13: 0.1550
REMARK 3 S21: -0.2343 S22: 0.1382 S23: 0.0241
REMARK 3 S31: -0.1274 S32: 0.0651 S33: -0.0505
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 3SHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-10; 13-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; ALS
REMARK 200 BEAMLINE : 8.2.1; 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 0.979485
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; ADSC QUANTUM
REMARK 200 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34990
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 61.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NA-FORMATE, PH 6.5, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 45.46800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.90650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.90650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.73400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.90650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.90650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.20200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.90650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.90650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.73400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.90650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.90650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.20200
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 45.46800
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 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 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 HOH A 395 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 VAL A 3
REMARK 465 PRO A 70
REMARK 465 ASN A 71
REMARK 465 ALA A 82
REMARK 465 ASP A 83
REMARK 465 ILE A 84
REMARK 465 GLU A 85
REMARK 465 ASP A 86
REMARK 465 ALA A 87
REMARK 465 CYS A 88
REMARK 465 SER A 89
REMARK 465 LEU A 90
REMARK 465 PRO A 91
REMARK 465 ARG A 107
REMARK 465 GLU A 108
REMARK 465 LYS A 317
REMARK 465 LYS A 318
REMARK 465 ASN A 319
REMARK 465 SER A 320
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 530 O HOH A 537 2.02
REMARK 500 O HOH A 383 O HOH A 488 2.03
REMARK 500 O HOH A 440 O HOH A 478 2.07
REMARK 500 OE2 GLU A 312 O HOH A 514 2.10
REMARK 500 ND1 HIS A 113 O HOH A 437 2.14
REMARK 500 O HOH A 487 O HOH A 495 2.16
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 LEU A 21 -166.06 -161.86
REMARK 500 LEU A 66 -91.93 -175.59
REMARK 500 GLU A 67 -169.08 -101.87
REMARK 500 ASN A 93 84.35 -67.40
REMARK 500 ILE A 147 -61.20 -104.68
REMARK 500 TYR A 149 -0.97 66.39
REMARK 500 ASP A 215 -166.66 -121.02
REMARK 500 GLU A 226 -11.25 79.51
REMARK 500 ASN A 263 61.34 -154.89
REMARK 500 GLN A 275 73.78 32.96
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 MG A 321 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 146 OD2
REMARK 620 2 ASP A 148 OD1 99.8
REMARK 620 3 ASP A 148 O 87.0 85.8
REMARK 620 4 ASP A 255 OD2 85.5 169.4 85.3
REMARK 620 5 HOH A 322 O 92.5 97.6 176.6 91.3
REMARK 620 6 HOH A 344 O 167.6 92.1 90.2 82.2 89.6
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 MG A 321
DBREF 3SHQ A 1 320 UNP Q9XZ16 Q9XZ16_DROME 1 320
SEQADV 3SHQ ALA A 112 UNP Q9XZ16 GLU 112 ENGINEERED MUTATION
SEQRES 1 A 320 MET GLU VAL LYS GLU VAL VAL VAL ILE VAL LYS TRP SER
SEQRES 2 A 320 GLY LYS GLU TYR PRO VAL ASP LEU THR ASP GLN ASP THR
SEQRES 3 A 320 VAL GLU VAL LEU ARG HIS GLU ILE PHE ARG LYS THR GLN
SEQRES 4 A 320 VAL ARG PRO GLU ARG GLN LYS LEU LEU ASN LEU LYS TYR
SEQRES 5 A 320 LYS GLY LYS THR ALA ALA ASP ASN VAL LYS ILE SER ALA
SEQRES 6 A 320 LEU GLU LEU LYS PRO ASN PHE LYS LEU MET MET VAL GLY
SEQRES 7 A 320 SER THR GLU ALA ASP ILE GLU ASP ALA CYS SER LEU PRO
SEQRES 8 A 320 ASP ASN ILE GLY GLU VAL VAL ASP ASP PHE ASP ASP ALA
SEQRES 9 A 320 ASP GLU ARG GLU GLU SER VAL ALA HIS SER ALA VAL TYR
SEQRES 10 A 320 LEU ALA LYS VAL GLN ARG ARG VAL ARG ASP TYR LYS ILE
SEQRES 11 A 320 LYS GLU LEU ALA PRO PRO ARG GLU GLY LYS LYS LEU LEU
SEQRES 12 A 320 VAL LEU ASP ILE ASP TYR THR LEU PHE ASP HIS ARG SER
SEQRES 13 A 320 PRO ALA GLU THR GLY THR GLU LEU MET ARG PRO TYR LEU
SEQRES 14 A 320 HIS GLU PHE LEU THR SER ALA TYR GLU ASP TYR ASP ILE
SEQRES 15 A 320 VAL ILE TRP SER ALA THR SER MET ARG TRP ILE GLU GLU
SEQRES 16 A 320 LYS MET ARG LEU LEU GLY VAL ALA SER ASN ASP ASN TYR
SEQRES 17 A 320 LYS VAL MET PHE TYR LEU ASP SER THR ALA MET ILE SER
SEQRES 18 A 320 VAL HIS VAL PRO GLU ARG GLY VAL VAL ASP VAL LYS PRO
SEQRES 19 A 320 LEU GLY VAL ILE TRP ALA LEU TYR LYS GLN TYR ASN SER
SEQRES 20 A 320 SER ASN THR ILE MET PHE ASP ASP ILE ARG ARG ASN PHE
SEQRES 21 A 320 LEU MET ASN PRO LYS SER GLY LEU LYS ILE ARG PRO PHE
SEQRES 22 A 320 ARG GLN ALA HIS LEU ASN ARG GLY THR ASP THR GLU LEU
SEQRES 23 A 320 LEU LYS LEU SER ASP TYR LEU ARG LYS ILE ALA HIS HIS
SEQRES 24 A 320 CYS PRO ASP PHE ASN SER LEU ASN HIS ARG LYS TRP GLU
SEQRES 25 A 320 HIS TYR HIS PRO LYS LYS ASN SER
HET MG A 321 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 HOH *216(H2 O)
HELIX 1 1 THR A 26 GLN A 39 1 14
HELIX 2 2 ARG A 41 GLN A 45 5 5
HELIX 3 3 SER A 114 TYR A 128 1 15
HELIX 4 4 THR A 160 MET A 165 1 6
HELIX 5 5 TYR A 168 ASP A 179 1 12
HELIX 6 6 SER A 189 LEU A 200 1 12
HELIX 7 7 ASP A 215 MET A 219 5 5
HELIX 8 8 PRO A 234 TYR A 242 1 9
HELIX 9 9 ASN A 246 SER A 248 5 3
HELIX 10 10 ILE A 256 LEU A 261 5 6
HELIX 11 11 ASN A 263 LYS A 265 5 3
HELIX 12 12 GLN A 275 ARG A 280 1 6
HELIX 13 13 THR A 284 CYS A 300 1 17
HELIX 14 14 ASP A 302 LEU A 306 5 5
HELIX 15 15 ASN A 307 TYR A 314 5 8
SHEET 1 A 4 LYS A 15 THR A 22 0
SHEET 2 A 4 GLU A 5 TRP A 12 -1 N VAL A 6 O LEU A 21
SHEET 3 A 4 LYS A 73 VAL A 77 1 O LEU A 74 N LYS A 11
SHEET 4 A 4 LYS A 46 LEU A 47 -1 N LYS A 46 O VAL A 77
SHEET 1 B 5 PHE A 212 LEU A 214 0
SHEET 2 B 5 TYR A 180 TRP A 185 1 N ILE A 184 O LEU A 214
SHEET 3 B 5 LYS A 141 LEU A 145 1 N LYS A 141 O ASP A 181
SHEET 4 B 5 THR A 250 ASP A 254 1 O PHE A 253 N VAL A 144
SHEET 5 B 5 GLY A 267 LYS A 269 1 O LEU A 268 N MET A 252
SHEET 1 C 2 ILE A 220 VAL A 224 0
SHEET 2 C 2 GLY A 228 VAL A 232 -1 O VAL A 230 N VAL A 222
LINK OD2 ASP A 146 MG MG A 321 1555 1555 2.14
LINK OD1 ASP A 148 MG MG A 321 1555 1555 2.12
LINK O ASP A 148 MG MG A 321 1555 1555 2.13
LINK OD2 ASP A 255 MG MG A 321 1555 1555 2.16
LINK MG MG A 321 O HOH A 322 1555 1555 1.98
LINK MG MG A 321 O HOH A 344 1555 1555 2.13
CISPEP 1 GLU A 109 SER A 110 0 3.46
SITE 1 AC1 5 ASP A 146 ASP A 148 ASP A 255 HOH A 322
SITE 2 AC1 5 HOH A 344
CRYST1 101.813 101.813 90.936 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 0.009822 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009822 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010997 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
