HEADER ENDOCYTOSIS 29-JUN-09 3I2W
TITLE CRYSTAL STRUCTURE OF EFC/F-BAR DOMAIN OF DROSOPHILA
TITLE 2 SYNDAPIN/PACSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNDAPIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EFC/F-BAR DOMAIN, UNP RESIDUES 14-303 OUT OF 494;
COMPND 5 SYNONYM: LD46328P;
COMPND 6 ENGINEERED: 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: CG33094, DMEL_CG33094, SYND, SYNDAPIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS EFC, FBAR, SH3 DOMAIN, ENDOCYTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.EDELING,D.J.OWEN,L.M.TRAUB
REVDAT 1 02-MAR-10 3I2W 0
JRNL AUTH M.A.EDELING,S.SANKER,T.SHIMA,P.K.UMASANKAR,
JRNL AUTH 2 S.HONING,H.Y.KIM,L.A.DAVIDSON,S.C.WATKINS,M.TSANG,
JRNL AUTH 3 D.J.OWEN,L.M.TRAUB
JRNL TITL STRUCTURAL REQUIREMENTS FOR PACSIN/SYNDAPIN
JRNL TITL 2 OPERATION DURING ZEBRAFISH EMBRYONIC NOTOCHORD
JRNL TITL 3 DEVELOPMENT.
JRNL REF PLOS ONE V. 4 E8150 2009
JRNL REFN ESSN 1932-6203
JRNL PMID 19997509
JRNL DOI 10.1371/JOURNAL.PONE.0008150
REMARK 2
REMARK 2 RESOLUTION. 2.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28462
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1522
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) : 2.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2010
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.73000
REMARK 3 B22 (A**2) : -4.54000
REMARK 3 B33 (A**2) : 0.81000
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): 0.449
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.286
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.876
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4720 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6345 ; 2.108 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 552 ; 6.881 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;35.891 ;25.328
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 923 ;20.734 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;13.461 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 663 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3524 ; 0.008 ; 0.020
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): 2767 ; 1.024 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4471 ; 2.048 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1953 ; 3.464 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1874 ; 5.877 ; 4.500
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 : NULL
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 : 1.20
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
REMARK 3 RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3I2W COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB053895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.670
REMARK 200 RESOLUTION RANGE LOW (A) : 78.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.600
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 3350, 0.1M DISODIUM
REMARK 280 PHOSPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 31.29750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.43000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.76250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.43000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.29750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.76250
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 ASN A 169
REMARK 465 GLN A 170
REMARK 465 GLU A 171
REMARK 465 ARG A 172
REMARK 465 ASN A 173
REMARK 465 ALA A 174
REMARK 465 ASN A 175
REMARK 465 ALA A 176
REMARK 465 ASP A 177
REMARK 465 SER A 178
REMARK 465 SER A 179
REMARK 465 LEU A 180
REMARK 465 SER A 181
REMARK 465 PRO A 182
REMARK 465 ASP A 183
REMARK 465 GLN A 184
REMARK 465 VAL A 185
REMARK 465 LYS A 186
REMARK 465 LYS A 187
REMARK 465 MSE A 188
REMARK 465 PHE B 299
REMARK 465 VAL B 300
REMARK 465 GLU B 301
REMARK 465 TYR B 302
REMARK 465 THR B 303
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 B 325 O HOH B 327 2.16
REMARK 500 CG2 THR A 27 OE2 GLU A 133 2.17
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 CYS A 37 CB CYS A 37 SG -0.097
REMARK 500 SER A 159 CB SER A 159 OG 0.106
REMARK 500 CYS A 252 CB CYS A 252 SG -0.144
REMARK 500 GLU B 244 CG GLU B 244 CD 0.105
REMARK 500 GLU B 244 CD GLU B 244 OE1 0.073
REMARK 500 GLU B 244 CD GLU B 244 OE2 0.101
REMARK 500 CYS B 252 CB CYS B 252 SG -0.110
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 ASP B 254 CB - CG - OD1 ANGL. DEV. = 6.1 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 ASP A 106 -66.02 -133.95
REMARK 500 LEU A 123 -127.51 45.51
REMARK 500 SER A 260 -3.69 -56.29
REMARK 500 GLU A 301 -175.85 -65.26
REMARK 500 ASN B 291 38.65 -86.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LYS A 141 24.0 L L OUTSIDE RANGE
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 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 69 O
REMARK 620 2 GLU A 70 O 65.0
REMARK 620 3 GLY A 72 O 77.7 77.7
REMARK 620 4 GLU A 74 O 117.6 175.5 106.2
REMARK 620 5 GLU A 79 OE2 80.4 95.0 158.0 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 69 O
REMARK 620 2 GLU B 70 O 67.3
REMARK 620 3 GLY B 72 O 80.7 77.9
REMARK 620 4 GLU B 74 O 112.8 174.9 97.0
REMARK 620 5 GLU B 79 OE2 81.6 95.2 162.3 89.9
REMARK 620 6 HOH B 322 O 129.0 65.3 72.3 112.7 119.9
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 GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 304
DBREF 3I2W A 14 303 UNP Q9VDI1 Q9VDI1_DROME 14 303
DBREF 3I2W B 14 303 UNP Q9VDI1 Q9VDI1_DROME 14 303
SEQRES 1 A 290 SER ASP SER PHE TRP GLU PRO GLY ASN TYR LYS ARG THR
SEQRES 2 A 290 THR LYS ARG ILE GLU ASP GLY TYR LYS LEU CYS ASN ASP
SEQRES 3 A 290 LEU GLN GLN LEU ILE GLN GLU ARG ALA ASP ILE GLU LYS
SEQRES 4 A 290 GLY TYR ALA LYS SER LEU ARG THR TRP SER LYS LYS TRP
SEQRES 5 A 290 GLY GLU LEU ILE GLU LYS GLY PRO GLU TYR GLY THR THR
SEQRES 6 A 290 GLU ALA ALA TRP LYS GLY VAL LEU THR GLU SER GLU ARG
SEQRES 7 A 290 ILE SER ASP VAL HIS MSE LYS ILE LYS ASP ASN LEU CYS
SEQRES 8 A 290 ASN ASP VAL ASN SER GLN ILE LYS THR TRP GLN LYS GLU
SEQRES 9 A 290 ASN TYR HIS HIS THR LEU MSE GLN ILE LYS GLU ARG LYS
SEQRES 10 A 290 ASP LEU GLU ASP LEU PHE LYS LYS ALA GLN LYS PRO TRP
SEQRES 11 A 290 ALA LYS LEU LEU ALA LYS VAL GLU LYS ALA LYS ALA ASP
SEQRES 12 A 290 TYR HIS SER ALA CYS LYS THR GLU ARG SER ALA THR ASN
SEQRES 13 A 290 GLN GLU ARG ASN ALA ASN ALA ASP SER SER LEU SER PRO
SEQRES 14 A 290 ASP GLN VAL LYS LYS MSE HIS ASP ARG VAL GLN LYS THR
SEQRES 15 A 290 LYS ASP GLN VAL GLN LYS CYS ARG GLU LYS TYR GLU GLN
SEQRES 16 A 290 ALA ILE ALA GLU ILE THR LYS TYR ASN SER VAL TYR ILE
SEQRES 17 A 290 GLU ASP MSE THR SER VAL PHE GLU LYS CYS GLN THR PHE
SEQRES 18 A 290 GLU LYS THR ARG LEU GLN PHE PHE LYS GLU ILE LEU PHE
SEQRES 19 A 290 ASN VAL HIS SER CYS LEU ASP LEU THR LYS VAL GLN SER
SEQRES 20 A 290 LEU PRO GLN ILE TYR GLU GLU PHE SER HIS THR ILE ASN
SEQRES 21 A 290 ASN ALA ASP GLN GLN LYS ASP LEU LYS TRP TRP SER ASN
SEQRES 22 A 290 ASN HIS GLY ILE ASN MSE ALA MSE ASN TRP PRO SER PHE
SEQRES 23 A 290 VAL GLU TYR THR
SEQRES 1 B 290 SER ASP SER PHE TRP GLU PRO GLY ASN TYR LYS ARG THR
SEQRES 2 B 290 THR LYS ARG ILE GLU ASP GLY TYR LYS LEU CYS ASN ASP
SEQRES 3 B 290 LEU GLN GLN LEU ILE GLN GLU ARG ALA ASP ILE GLU LYS
SEQRES 4 B 290 GLY TYR ALA LYS SER LEU ARG THR TRP SER LYS LYS TRP
SEQRES 5 B 290 GLY GLU LEU ILE GLU LYS GLY PRO GLU TYR GLY THR THR
SEQRES 6 B 290 GLU ALA ALA TRP LYS GLY VAL LEU THR GLU SER GLU ARG
SEQRES 7 B 290 ILE SER ASP VAL HIS MSE LYS ILE LYS ASP ASN LEU CYS
SEQRES 8 B 290 ASN ASP VAL ASN SER GLN ILE LYS THR TRP GLN LYS GLU
SEQRES 9 B 290 ASN TYR HIS HIS THR LEU MSE GLN ILE LYS GLU ARG LYS
SEQRES 10 B 290 ASP LEU GLU ASP LEU PHE LYS LYS ALA GLN LYS PRO TRP
SEQRES 11 B 290 ALA LYS LEU LEU ALA LYS VAL GLU LYS ALA LYS ALA ASP
SEQRES 12 B 290 TYR HIS SER ALA CYS LYS THR GLU ARG SER ALA THR ASN
SEQRES 13 B 290 GLN GLU ARG ASN ALA ASN ALA ASP SER SER LEU SER PRO
SEQRES 14 B 290 ASP GLN VAL LYS LYS MSE HIS ASP ARG VAL GLN LYS THR
SEQRES 15 B 290 LYS ASP GLN VAL GLN LYS CYS ARG GLU LYS TYR GLU GLN
SEQRES 16 B 290 ALA ILE ALA GLU ILE THR LYS TYR ASN SER VAL TYR ILE
SEQRES 17 B 290 GLU ASP MSE THR SER VAL PHE GLU LYS CYS GLN THR PHE
SEQRES 18 B 290 GLU LYS THR ARG LEU GLN PHE PHE LYS GLU ILE LEU PHE
SEQRES 19 B 290 ASN VAL HIS SER CYS LEU ASP LEU THR LYS VAL GLN SER
SEQRES 20 B 290 LEU PRO GLN ILE TYR GLU GLU PHE SER HIS THR ILE ASN
SEQRES 21 B 290 ASN ALA ASP GLN GLN LYS ASP LEU LYS TRP TRP SER ASN
SEQRES 22 B 290 ASN HIS GLY ILE ASN MSE ALA MSE ASN TRP PRO SER PHE
SEQRES 23 B 290 VAL GLU TYR THR
MODRES 3I2W MSE A 97 MET SELENOMETHIONINE
MODRES 3I2W MSE A 124 MET SELENOMETHIONINE
MODRES 3I2W MSE A 224 MET SELENOMETHIONINE
MODRES 3I2W MSE A 292 MET SELENOMETHIONINE
MODRES 3I2W MSE A 294 MET SELENOMETHIONINE
MODRES 3I2W MSE B 97 MET SELENOMETHIONINE
MODRES 3I2W MSE B 124 MET SELENOMETHIONINE
MODRES 3I2W MSE B 188 MET SELENOMETHIONINE
MODRES 3I2W MSE B 224 MET SELENOMETHIONINE
MODRES 3I2W MSE B 292 MET SELENOMETHIONINE
MODRES 3I2W MSE B 294 MET SELENOMETHIONINE
HET MSE A 97 8
HET MSE A 124 8
HET MSE A 224 8
HET MSE A 292 8
HET MSE A 294 8
HET MSE B 97 8
HET MSE B 124 8
HET MSE B 188 8
HET MSE B 224 8
HET MSE B 292 8
HET MSE B 294 8
HET GOL A 1 6
HET NA A 304 1
HET NA A 3 1
HET GOL B 2 6
HET NA B 304 1
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 NA 3(NA 1+)
FORMUL 8 HOH *104(H2 O)
HELIX 1 1 TYR A 23 GLY A 72 1 50
HELIX 2 2 TYR A 75 ASP A 106 1 32
HELIX 3 3 ASP A 106 TYR A 119 1 14
HELIX 4 4 LYS A 127 THR A 163 1 37
HELIX 5 5 ASP A 197 ASP A 254 1 58
HELIX 6 6 LEU A 255 VAL A 258 5 4
HELIX 7 7 SER A 260 ASN A 274 1 15
HELIX 8 8 ASP A 276 HIS A 288 1 13
HELIX 9 9 TYR B 23 GLY B 72 1 50
HELIX 10 10 TYR B 75 ASP B 106 1 32
HELIX 11 11 ASP B 106 TYR B 119 1 14
HELIX 12 12 LYS B 127 ASN B 173 1 47
HELIX 13 13 SER B 181 ASP B 254 1 74
HELIX 14 14 LEU B 255 VAL B 258 5 4
HELIX 15 15 GLN B 259 ASN B 274 1 16
HELIX 16 16 ASP B 276 GLY B 289 1 14
SHEET 1 A 2 HIS A 121 THR A 122 0
SHEET 2 A 2 GLN A 125 ILE A 126 -1 O GLN A 125 N THR A 122
SHEET 1 B 2 HIS B 121 THR B 122 0
SHEET 2 B 2 GLN B 125 ILE B 126 -1 O GLN B 125 N THR B 122
LINK C HIS A 96 N MSE A 97 1555 1555 1.31
LINK C MSE A 97 N LYS A 98 1555 1555 1.32
LINK C LEU A 123 N MSE A 124 1555 1555 1.32
LINK C MSE A 124 N GLN A 125 1555 1555 1.34
LINK C ASP A 223 N MSE A 224 1555 1555 1.32
LINK C MSE A 224 N THR A 225 1555 1555 1.33
LINK C ASN A 291 N MSE A 292 1555 1555 1.33
LINK C MSE A 292 N ALA A 293 1555 1555 1.34
LINK C ALA A 293 N MSE A 294 1555 1555 1.33
LINK C MSE A 294 N ASN A 295 1555 1555 1.34
LINK C HIS B 96 N MSE B 97 1555 1555 1.34
LINK C MSE B 97 N LYS B 98 1555 1555 1.32
LINK C LEU B 123 N MSE B 124 1555 1555 1.34
LINK C MSE B 124 N GLN B 125 1555 1555 1.32
LINK C LYS B 187 N MSE B 188 1555 1555 1.32
LINK C MSE B 188 N HIS B 189 1555 1555 1.32
LINK C ASP B 223 N MSE B 224 1555 1555 1.32
LINK C MSE B 224 N THR B 225 1555 1555 1.34
LINK C ASN B 291 N MSE B 292 1555 1555 1.32
LINK C MSE B 292 N ALA B 293 1555 1555 1.33
LINK C ALA B 293 N MSE B 294 1555 1555 1.32
LINK C MSE B 294 N ASN B 295 1555 1555 1.33
LINK O ILE A 69 NA NA A 304 1555 1555 2.89
LINK O GLU A 70 NA NA A 304 1555 1555 2.81
LINK O GLY A 72 NA NA A 304 1555 1555 2.41
LINK O GLU A 74 NA NA A 304 1555 1555 2.36
LINK OE2 GLU A 79 NA NA A 304 1555 1555 2.66
LINK O ILE B 69 NA NA B 304 1555 1555 2.77
LINK O GLU B 70 NA NA B 304 1555 1555 2.81
LINK O GLY B 72 NA NA B 304 1555 1555 2.73
LINK O GLU B 74 NA NA B 304 1555 1555 2.43
LINK OE2 GLU B 79 NA NA B 304 1555 1555 2.53
LINK NA NA B 304 O HOH B 322 1555 1555 2.55
SITE 1 AC1 7 ILE A 50 GLY A 53 SER A 57 ILE B 50
SITE 2 AC1 7 GLY B 53 TYR B 54 SER B 57
SITE 1 AC2 5 ILE A 69 GLU A 70 GLY A 72 GLU A 74
SITE 2 AC2 5 GLU A 79
SITE 1 AC3 1 ASN A 273
SITE 1 AC4 9 HIS B 121 ASP B 177 SER B 178 LEU B 180
SITE 2 AC4 9 PRO B 182 ASN B 286 ASN B 291 HOH B 339
SITE 3 AC4 9 HOH B 341
SITE 1 AC5 6 ILE B 69 GLU B 70 GLY B 72 GLU B 74
SITE 2 AC5 6 GLU B 79 HOH B 322
CRYST1 62.595 85.525 192.860 90.00 90.00 90.00 P 21 21 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 0.015976 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005185 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
