REMARK 2 REMARK 2 RESOLUTION. 3.23 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.3 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.23 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 3 NUMBER OF REFLECTIONS : 39891 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) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1986 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.23 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.31 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.87 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2475 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2920 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2355 REMARK 3 BIN R VALUE (WORKING SET) : 0.2919 REMARK 3 BIN FREE R VALUE : 0.2939 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.85 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 120 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12286 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 76.54 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.52 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.08420 REMARK 3 B22 (A**2) : 10.79600 REMARK 3 B33 (A**2) : -7.71170 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -18.30730 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.77 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.43 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.854 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.843 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 12589 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 17094 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 4255 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 275 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1822 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 12589 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1680 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 12525 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.90 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.34 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.76 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3UAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-11. REMARK 100 THE RCSB ID CODE IS RCSB068511. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-MAY-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 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) : 1 REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111) REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39891 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.232 REMARK 200 RESOLUTION RANGE LOW (A) : 47.738 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.10200 REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.23 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.41 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.46500 REMARK 200 R SYM FOR SHELL (I) : 0.46500 REMARK 200 FOR SHELL : 1.700 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: PDB ENTRY 1OKE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG8000, 8% MPD, 0.1 M HEPES, PH REMARK 280 7.5, VAPOR DIFFUSION, TEMPERATURE 292K 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 67.37500 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, L, A, C, D 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 B 146 REMARK 465 ASP B 147 REMARK 465 THR B 148 REMARK 465 HIS B 149 REMARK 465 ALA B 150 REMARK 465 VAL B 151 REMARK 465 GLY B 152 REMARK 465 ASN B 153 REMARK 465 ASP B 154 REMARK 465 THR B 155 REMARK 465 SER B 156 REMARK 465 ASN B 157 REMARK 465 GLY B 223 REMARK 465 ALA B 224 REMARK 465 ASP B 225 REMARK 465 THR B 226 REMARK 465 SER B 227 REMARK 465 GLU B 228 REMARK 465 VAL B 229 REMARK 465 HIS B 244 REMARK 465 ALA B 245 REMARK 465 LYS B 246 REMARK 465 ARG B 247 REMARK 465 GLN B 248 REMARK 465 PRO B 396 REMARK 465 PHE B 397 REMARK 465 GLU B 398 REMARK 465 ASP B 399 REMARK 465 ASP B 400 REMARK 465 ASP B 401 REMARK 465 ASP B 402 REMARK 465 LYS B 403 REMARK 465 ALA B 404 REMARK 465 GLY B 405 REMARK 465 TRP B 406 REMARK 465 SER B 407 REMARK 465 HIS B 408 REMARK 465 PRO B 409 REMARK 465 GLN B 410 REMARK 465 PHE B 411 REMARK 465 GLU B 412 REMARK 465 LYS B 413 REMARK 465 GLY B 414 REMARK 465 GLY B 415 REMARK 465 GLY B 416 REMARK 465 SER B 417 REMARK 465 GLY B 418 REMARK 465 GLY B 419 REMARK 465 GLY B 420 REMARK 465 SER B 421 REMARK 465 GLY B 422 REMARK 465 GLY B 423 REMARK 465 GLY B 424 REMARK 465 SER B 425 REMARK 465 TRP B 426 REMARK 465 SER B 427 REMARK 465 HIS B 428 REMARK 465 PRO B 429 REMARK 465 GLN B 430 REMARK 465 PHE B 431 REMARK 465 GLU B 432 REMARK 465 LYS B 433 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 LYS H 224 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 THR H 228 REMARK 465 THR H 229 REMARK 465 SER H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 ALA L 1 REMARK 465 CYS L 215 REMARK 465 GLY A 146 REMARK 465 ASP A 147 REMARK 465 THR A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 VAL A 151 REMARK 465 GLY A 152 REMARK 465 ASN A 153 REMARK 465 ASP A 154 REMARK 465 THR A 155 REMARK 465 SER A 156 REMARK 465 ASN A 157 REMARK 465 SER A 227 REMARK 465 GLU A 228 REMARK 465 VAL A 229 REMARK 465 PRO A 243 REMARK 465 HIS A 244 REMARK 465 ALA A 245 REMARK 465 LYS A 246 REMARK 465 ARG A 247 REMARK 465 PRO A 396 REMARK 465 PHE A 397 REMARK 465 GLU A 398 REMARK 465 ASP A 399 REMARK 465 ASP A 400 REMARK 465 ASP A 401 REMARK 465 ASP A 402 REMARK 465 LYS A 403 REMARK 465 ALA A 404 REMARK 465 GLY A 405 REMARK 465 TRP A 406 REMARK 465 SER A 407 REMARK 465 HIS A 408 REMARK 465 PRO A 409 REMARK 465 GLN A 410 REMARK 465 PHE A 411 REMARK 465 GLU A 412 REMARK 465 LYS A 413 REMARK 465 GLY A 414 REMARK 465 GLY A 415 REMARK 465 GLY A 416 REMARK 465 SER A 417 REMARK 465 GLY A 418 REMARK 465 GLY A 419 REMARK 465 GLY A 420 REMARK 465 SER A 421 REMARK 465 GLY A 422 REMARK 465 GLY A 423 REMARK 465 GLY A 424 REMARK 465 SER A 425 REMARK 465 TRP A 426 REMARK 465 SER A 427 REMARK 465 HIS A 428 REMARK 465 PRO A 429 REMARK 465 GLN A 430 REMARK 465 PHE A 431 REMARK 465 GLU A 432 REMARK 465 LYS A 433 REMARK 465 LYS C 139 REMARK 465 SER C 140 REMARK 465 THR C 141 REMARK 465 SER C 142 REMARK 465 SER C 225 REMARK 465 CYS C 226 REMARK 465 ASP C 227 REMARK 465 THR C 228 REMARK 465 THR C 229 REMARK 465 SER C 230 REMARK 465 HIS C 231 REMARK 465 HIS C 232 REMARK 465 HIS C 233 REMARK 465 HIS C 234 REMARK 465 HIS C 235 REMARK 465 HIS C 236 REMARK 465 ALA D 1 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 ALA B 19 -39.86 61.25 REMARK 500 ASN B 67 80.46 38.49 REMARK 500 THR B 76 -26.74 67.43 REMARK 500 ASN B 134 75.09 -101.03 REMARK 500 ASP B 177 -15.37 72.03 REMARK 500 LYS B 202 -84.11 57.36 REMARK 500 TYR B 233 67.26 62.19 REMARK 500 VAL B 270 -82.95 -75.26 REMARK 500 GLU B 345 -69.40 -107.77 REMARK 500 THR B 355 79.91 50.02 REMARK 500 SER H 15 -22.96 82.40 REMARK 500 THR H 90 96.94 -67.47 REMARK 500 VAL H 105 -80.34 59.53 REMARK 500 ASP H 154 85.61 54.02 REMARK 500 SER L 31 -135.10 55.00 REMARK 500 ALA L 52 -23.42 60.33 REMARK 500 PHE L 92 18.87 -140.21 REMARK 500 ASN L 139 98.25 48.79 REMARK 500 ASP L 152 63.01 -168.74 REMARK 500 ASN L 153 -4.51 71.95 REMARK 500 LYS L 191 -75.11 -104.03 REMARK 500 ALA A 19 -40.03 61.36 REMARK 500 ASN A 67 79.69 38.70 REMARK 500 THR A 76 -26.64 67.59 REMARK 500 ASN A 134 80.00 -102.94 REMARK 500 ASP A 177 -15.40 72.15 REMARK 500 LYS A 202 -87.92 60.20 REMARK 500 ALA A 224 36.33 -152.35 REMARK 500 TYR A 233 67.24 62.11 REMARK 500 GLU A 345 -69.33 -105.35 REMARK 500 THR A 355 79.91 50.08 REMARK 500 SER C 15 -22.93 82.26 REMARK 500 THR C 90 97.11 -67.51 REMARK 500 ASP C 154 85.60 53.93 REMARK 500 SER D 31 -129.89 53.31 REMARK 500 ALA D 52 -22.68 60.10 REMARK 500 PHE D 92 19.14 -141.13 REMARK 500 ASN D 139 98.36 48.74 REMARK 500 ASP D 152 63.31 -168.79 REMARK 500 ASN D 153 -4.45 71.10 REMARK 500 LYS D 191 -75.12 -104.06 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 VAL H 105 25.0 L L OUTSIDE RANGE REMARK 500 THR A 76 24.6 L L OUTSIDE RANGE 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 NAG B 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1001 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3UC0 RELATED DB: PDB