REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.12 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.85 REMARK 3 NUMBER OF REFLECTIONS : 151525 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) : 0.1887 REMARK 3 R VALUE (WORKING SET) : 0.1878 REMARK 3 FREE R VALUE : 0.2046 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.02 REMARK 3 FREE R VALUE TEST SET COUNT : 7603 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) : 2.05 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.10 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.85 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5136 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2501 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4878 REMARK 3 BIN R VALUE (WORKING SET) : 0.2483 REMARK 3 BIN FREE R VALUE : 0.2859 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.02 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 258 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 : 13633 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 154 REMARK 3 SOLVENT ATOMS : 952 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.49 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.46 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.8034 REMARK 3 B22 (A**2) : -0.4650 REMARK 3 B33 (A**2) : 6.2684 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : 9.3841 REMARK 3 B23 (A**2) : 0.0000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.318 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.158 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.133 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.158 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.134 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 : 0.9521 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9470 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 14122 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES : 19265 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES : 4594 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 288 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES : 2218 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 14122 ; 20.00 ; 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 : 1899 ; 5.00 ; 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 : 15695 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.02 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.43 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.13 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A) REMARK 3 ORIGIN FOR THE GROUP (A): -29.5883 15.4618 -59.3063 REMARK 3 T TENSOR REMARK 3 T11: -0.1650 T22: 0.0056 REMARK 3 T33: -0.2200 T12: 0.0128 REMARK 3 T13: -0.0928 T23: 0.0527 REMARK 3 L TENSOR REMARK 3 L11: 1.7111 L22: 0.3811 REMARK 3 L33: 2.2888 L12: -0.3663 REMARK 3 L13: -0.7450 L23: 0.3715 REMARK 3 S TENSOR REMARK 3 S11: 0.0109 S12: 0.2990 S13: 0.1843 REMARK 3 S21: -0.0198 S22: -0.0319 S23: -0.0499 REMARK 3 S31: -0.0306 S32: -0.4186 S33: 0.0210 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN E) REMARK 3 ORIGIN FOR THE GROUP (A): -18.4464 65.4495 -60.9675 REMARK 3 T TENSOR REMARK 3 T11: -0.1061 T22: -0.0259 REMARK 3 T33: -0.2161 T12: 0.0010 REMARK 3 T13: -0.0963 T23: -0.0343 REMARK 3 L TENSOR REMARK 3 L11: 1.6298 L22: 0.5453 REMARK 3 L33: 1.9184 L12: -0.3198 REMARK 3 L13: -0.8600 L23: 0.5753 REMARK 3 S TENSOR REMARK 3 S11: 0.0098 S12: 0.3051 S13: 0.1004 REMARK 3 S21: -0.0074 S22: -0.0240 S23: -0.0345 REMARK 3 S31: 0.0741 S32: -0.2423 S33: 0.0142 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN G) REMARK 3 ORIGIN FOR THE GROUP (A): -12.5878 23.6448 -23.3323 REMARK 3 T TENSOR REMARK 3 T11: 0.1144 T22: -0.2524 REMARK 3 T33: -0.1145 T12: -0.0467 REMARK 3 T13: -0.0746 T23: 0.0301 REMARK 3 L TENSOR REMARK 3 L11: 1.2129 L22: 1.2845 REMARK 3 L33: 1.8033 L12: -0.4572 REMARK 3 L13: 0.5564 L23: -0.3429 REMARK 3 S TENSOR REMARK 3 S11: -0.1114 S12: 0.1095 S13: 0.2463 REMARK 3 S21: 0.1126 S22: -0.0485 S23: -0.1218 REMARK 3 S31: -0.3197 S32: 0.0193 S33: 0.1598 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN J) REMARK 3 ORIGIN FOR THE GROUP (A): -1.1582 71.6415 -25.0165 REMARK 3 T TENSOR REMARK 3 T11: 0.0786 T22: -0.1711 REMARK 3 T33: -0.1048 T12: -0.0329 REMARK 3 T13: -0.0365 T23: 0.0154 REMARK 3 L TENSOR REMARK 3 L11: 1.3596 L22: 0.8405 REMARK 3 L33: 1.6621 L12: -0.5157 REMARK 3 L13: 0.6700 L23: -0.2609 REMARK 3 S TENSOR REMARK 3 S11: -0.1149 S12: 0.1675 S13: 0.1653 REMARK 3 S21: -0.0532 S22: -0.0325 S23: -0.1227 REMARK 3 S31: -0.0309 S32: 0.2691 S33: 0.1475 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN K) REMARK 3 ORIGIN FOR THE GROUP (A): -0.9975 55.7525 -16.0628 REMARK 3 T TENSOR REMARK 3 T11: 0.0781 T22: -0.2249 REMARK 3 T33: -0.1229 T12: -0.0455 REMARK 3 T13: -0.0489 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 2.1241 L22: 0.9270 REMARK 3 L33: 1.7829 L12: -0.4004 REMARK 3 L13: 1.3279 L23: -0.3878 REMARK 3 S TENSOR REMARK 3 S11: 0.1694 S12: -0.0035 S13: -0.1616 REMARK 3 S21: 0.0221 S22: -0.0540 S23: -0.0585 REMARK 3 S31: 0.2484 S32: 0.1529 S33: -0.1153 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN L) REMARK 3 ORIGIN FOR THE GROUP (A): -11.4141 7.7452 -14.3430 REMARK 3 T TENSOR REMARK 3 T11: 0.0382 T22: -0.2116 REMARK 3 T33: -0.1039 T12: -0.0209 REMARK 3 T13: -0.0554 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 1.9490 L22: 0.9174 REMARK 3 L33: 1.8074 L12: -0.1966 REMARK 3 L13: 1.0815 L23: -0.1537 REMARK 3 S TENSOR REMARK 3 S11: -0.0142 S12: 0.0213 S13: 0.1414 REMARK 3 S21: 0.1621 S22: 0.0069 S23: -0.0365 REMARK 3 S31: -0.0104 S32: -0.0144 S33: 0.0072 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2XQY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-10. REMARK 100 THE PDBE ID CODE IS EBI-44959. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 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) : 1.1399 REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC, XDS REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151575 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.05 REMARK 200 RESOLUTION RANGE LOW (A) : 58.13 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 6.1 REMARK 200 R MERGE (I) : 0.04 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.30 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 55.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.5 REMARK 200 R MERGE FOR SHELL (I) : 0.49 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.30 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 1BBD REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.4 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE PH 8, 0.7M REMARK 280 SODIUM FORMATE, 10.5% PEG 4,000 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 50.31500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 AUTHR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, L 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J, K 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 ARG A 105 REMARK 465 SER A 106 REMARK 465 GLN A 107 REMARK 465 ARG A 108 REMARK 465 PRO A 109 REMARK 465 ARG A 110 REMARK 465 GLU A 111 REMARK 465 ARG A 112 REMARK 465 PRO A 113 REMARK 465 ARG A 114 REMARK 465 LEU A 115 REMARK 465 SER A 116 REMARK 465 GLY A 117 REMARK 465 PRO A 118 REMARK 465 PRO A 119 REMARK 465 SER A 120 REMARK 465 GLY A 121 REMARK 465 ALA A 122 REMARK 465 GLU A 123 REMARK 465 LEU A 124 REMARK 465 VAL A 125 REMARK 465 ALA A 126 REMARK 465 PHE A 127 REMARK 465 ASP A 128 REMARK 465 ALA A 129 REMARK 465 PRO A 130 REMARK 465 ALA A 198 REMARK 465 LEU A 199 REMARK 465 GLY A 200 REMARK 465 SER A 201 REMARK 465 ASP A 202 REMARK 465 LEU A 203 REMARK 465 GLU A 204 REMARK 465 PRO A 205 REMARK 465 PRO A 206 REMARK 465 GLY A 207 REMARK 465 PRO A 208 REMARK 465 PRO A 209 REMARK 465 ALA A 210 REMARK 465 GLY A 448 REMARK 465 GLY A 449 REMARK 465 ASP A 450 REMARK 465 ALA A 469 REMARK 465 PRO A 470 REMARK 465 GLY A 471 REMARK 465 ALA A 472 REMARK 465 ALA A 473 REMARK 465 ALA A 474 REMARK 465 ALA A 475 REMARK 465 THR A 476 REMARK 465 ASP A 477 REMARK 465 GLU A 478 REMARK 465 GLY A 479 REMARK 465 ALA A 480 REMARK 465 GLU A 481 REMARK 465 GLU A 482 REMARK 465 ASP A 543 REMARK 465 SER A 544 REMARK 465 ALA A 545 REMARK 465 ALA A 546 REMARK 465 ALA A 603 REMARK 465 ASN A 604 REMARK 465 SER A 605 REMARK 465 THR A 606 REMARK 465 ILE A 607 REMARK 465 LEU A 634 REMARK 465 SER A 635 REMARK 465 PHE A 636 REMARK 465 THR A 637 REMARK 465 SER A 638 REMARK 465 THR A 639 REMARK 465 PHE A 640 REMARK 465 GLU A 641 REMARK 465 ASP A 642 REMARK 465 ASP A 643 REMARK 465 ASP A 644 REMARK 465 ASP A 645 REMARK 465 LYS A 646 REMARK 465 ALA A 647 REMARK 465 GLY A 648 REMARK 465 TRP A 649 REMARK 465 SER A 650 REMARK 465 HIS A 651 REMARK 465 PRO A 652 REMARK 465 GLN A 653 REMARK 465 PHE A 654 REMARK 465 GLU A 655 REMARK 465 LYS A 656 REMARK 465 GLY A 657 REMARK 465 GLY A 658 REMARK 465 GLY A 659 REMARK 465 SER A 660 REMARK 465 GLY A 661 REMARK 465 GLY A 662 REMARK 465 GLY A 663 REMARK 465 SER A 664 REMARK 465 GLY A 665 REMARK 465 GLY A 666 REMARK 465 GLY A 667 REMARK 465 SER A 668 REMARK 465 TRP A 669 REMARK 465 SER A 670 REMARK 465 HIS A 671 REMARK 465 PRO A 672 REMARK 465 GLN A 673 REMARK 465 PHE A 674 REMARK 465 GLU A 675 REMARK 465 LYS A 676 REMARK 465 ARG E 105 REMARK 465 SER E 106 REMARK 465 GLN E 107 REMARK 465 ARG E 108 REMARK 465 PRO E 109 REMARK 465 ARG E 110 REMARK 465 GLU E 111 REMARK 465 ARG E 112 REMARK 465 PRO E 113 REMARK 465 ARG E 114 REMARK 465 LEU E 115 REMARK 465 SER E 116 REMARK 465 GLY E 117 REMARK 465 PRO E 118 REMARK 465 PRO E 119 REMARK 465 SER E 120 REMARK 465 GLY E 121 REMARK 465 ALA E 122 REMARK 465 GLU E 123 REMARK 465 LEU E 124 REMARK 465 VAL E 125 REMARK 465 ALA E 126 REMARK 465 PHE E 127 REMARK 465 ASP E 128 REMARK 465 ALA E 129 REMARK 465 PRO E 130 REMARK 465 ALA E 198 REMARK 465 LEU E 199 REMARK 465 GLY E 200 REMARK 465 SER E 201 REMARK 465 ASP E 202 REMARK 465 LEU E 203 REMARK 465 GLU E 204 REMARK 465 PRO E 205 REMARK 465 PRO E 206 REMARK 465 GLY E 207 REMARK 465 PRO E 208 REMARK 465 PRO E 209 REMARK 465 ALA E 210 REMARK 465 GLY E 448 REMARK 465 GLY E 449 REMARK 465 ASP E 450 REMARK 465 ALA E 469 REMARK 465 PRO E 470 REMARK 465 GLY E 471 REMARK 465 ALA E 472 REMARK 465 ALA E 473 REMARK 465 ALA E 474 REMARK 465 ALA E 475 REMARK 465 THR E 476 REMARK 465 ASP E 477 REMARK 465 GLU E 478 REMARK 465 GLY E 479 REMARK 465 ALA E 480 REMARK 465 GLU E 481 REMARK 465 GLU E 482 REMARK 465 ASP E 543 REMARK 465 SER E 544 REMARK 465 ALA E 545 REMARK 465 ALA E 546 REMARK 465 ALA E 603 REMARK 465 ASN E 604 REMARK 465 SER E 605 REMARK 465 THR E 606 REMARK 465 ILE E 607 REMARK 465 LEU E 634 REMARK 465 SER E 635 REMARK 465 PHE E 636 REMARK 465 THR E 637 REMARK 465 SER E 638 REMARK 465 THR E 639 REMARK 465 PHE E 640 REMARK 465 GLU E 641 REMARK 465 ASP E 642 REMARK 465 ASP E 643 REMARK 465 ASP E 644 REMARK 465 ASP E 645 REMARK 465 LYS E 646 REMARK 465 ALA E 647 REMARK 465 GLY E 648 REMARK 465 TRP E 649 REMARK 465 SER E 650 REMARK 465 HIS E 651 REMARK 465 PRO E 652 REMARK 465 GLN E 653 REMARK 465 PHE E 654 REMARK 465 GLU E 655 REMARK 465 LYS E 656 REMARK 465 GLY E 657 REMARK 465 GLY E 658 REMARK 465 GLY E 659 REMARK 465 SER E 660 REMARK 465 GLY E 661 REMARK 465 GLY E 662 REMARK 465 GLY E 663 REMARK 465 SER E 664 REMARK 465 GLY E 665 REMARK 465 GLY E 666 REMARK 465 GLY E 667 REMARK 465 SER E 668 REMARK 465 TRP E 669 REMARK 465 SER E 670 REMARK 465 HIS E 671 REMARK 465 PRO E 672 REMARK 465 GLN E 673 REMARK 465 PHE E 674 REMARK 465 GLU E 675 REMARK 465 LYS E 676 REMARK 465 ARG G -5 REMARK 465 SER G -4 REMARK 465 LYS G -3 REMARK 465 LEU G -2 REMARK 465 LEU G -1 REMARK 465 ASP G 0 REMARK 465 ASP G 130 REMARK 465 THR G 131 REMARK 465 ALA G 214 REMARK 465 SER G 215 REMARK 465 ASP G 216 REMARK 465 ASP G 217 REMARK 465 ASP G 218 REMARK 465 ASP G 219 REMARK 465 LYS G 220 REMARK 465 ALA G 221 REMARK 465 GLY G 222 REMARK 465 TRP G 223 REMARK 465 SER G 224 REMARK 465 HIS G 225 REMARK 465 PRO G 226 REMARK 465 GLN G 227 REMARK 465 PHE G 228 REMARK 465 GLU G 229 REMARK 465 LYS G 230 REMARK 465 GLY G 231 REMARK 465 GLY G 232 REMARK 465 GLY G 233 REMARK 465 SER G 234 REMARK 465 GLY G 235 REMARK 465 GLY G 236 REMARK 465 GLY G 237 REMARK 465 SER G 238 REMARK 465 GLY G 239 REMARK 465 GLY G 240 REMARK 465 GLY G 241 REMARK 465 SER G 242 REMARK 465 TRP G 243 REMARK 465 SER G 244 REMARK 465 HIS G 245 REMARK 465 PRO G 246 REMARK 465 GLN G 247 REMARK 465 PHE G 248 REMARK 465 GLU G 249 REMARK 465 LYS G 250 REMARK 465 ARG J -5 REMARK 465 SER J -4 REMARK 465 LYS J -3 REMARK 465 LEU J -2 REMARK 465 LEU J -1 REMARK 465 ASP J 0 REMARK 465 ASP J 130 REMARK 465 THR J 131 REMARK 465 ALA J 214 REMARK 465 SER J 215 REMARK 465 ASP J 216 REMARK 465 ASP J 217 REMARK 465 ASP J 218 REMARK 465 ASP J 219 REMARK 465 LYS J 220 REMARK 465 ALA J 221 REMARK 465 GLY J 222 REMARK 465 TRP J 223 REMARK 465 SER J 224 REMARK 465 HIS J 225 REMARK 465 PRO J 226 REMARK 465 GLN J 227 REMARK 465 PHE J 228 REMARK 465 GLU J 229 REMARK 465 LYS J 230 REMARK 465 GLY J 231 REMARK 465 GLY J 232 REMARK 465 GLY J 233 REMARK 465 SER J 234 REMARK 465 GLY J 235 REMARK 465 GLY J 236 REMARK 465 GLY J 237 REMARK 465 SER J 238 REMARK 465 GLY J 239 REMARK 465 GLY J 240 REMARK 465 GLY J 241 REMARK 465 SER J 242 REMARK 465 TRP J 243 REMARK 465 SER J 244 REMARK 465 HIS J 245 REMARK 465 PRO J 246 REMARK 465 GLN J 247 REMARK 465 PHE J 248 REMARK 465 GLU J 249 REMARK 465 LYS J 250 REMARK 465 ARG K -1 REMARK 465 SER K 0 REMARK 465 ARG L -1 REMARK 465 SER L 0 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 PHE A 610 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE E 610 CG CD1 CD2 CE1 CE2 CZ 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 OE2 GLU J 148 O HOH J 3133 2.18 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 PHE A 220 39.15 -98.63 REMARK 500 ALA A 387 37.59 -152.51 REMARK 500 LEU A 453 44.51 -146.64 REMARK 500 ALA A 561 96.44 53.86 REMARK 500 ASP A 563 -24.91 -151.98 REMARK 500 ASN A 564 72.81 48.01 REMARK 500 PRO A 565 32.54 -95.54 REMARK 500 SER A 566 15.88 57.02 REMARK 500 SER A 609 -50.58 60.93 REMARK 500 LEU A 614 -22.69 -159.91 REMARK 500 PRO A 626 40.69 -63.88 REMARK 500 ASN A 627 -77.54 -158.88 REMARK 500 PHE E 220 39.85 -98.70 REMARK 500 ALA E 387 38.84 -152.90 REMARK 500 LEU E 453 42.14 -151.88 REMARK 500 ALA E 561 96.41 54.06 REMARK 500 ASP E 563 -24.95 -151.90 REMARK 500 ASN E 564 72.72 48.02 REMARK 500 PRO E 565 32.63 -95.68 REMARK 500 SER E 566 15.89 56.98 REMARK 500 SER E 609 -53.59 61.28 REMARK 500 PRO E 612 -144.62 -105.96 REMARK 500 LEU E 614 -6.37 -166.24 REMARK 500 PRO E 626 48.89 -64.21 REMARK 500 ASN E 627 -84.62 -171.89 REMARK 500 PRO G 41 123.16 -39.86 REMARK 500 SER G 82B 60.95 37.86 REMARK 500 SER J 82B 62.14 37.49 REMARK 500 ALA K 51 -37.76 70.44 REMARK 500 ALA L 51 -37.99 70.30 REMARK 500 ASN L 212 -78.58 -71.77 REMARK 500 GLU L 213 42.88 -70.92 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 A 275 21.1 L L OUTSIDE RANGE REMARK 500 THR A 562 25.0 L L OUTSIDE RANGE REMARK 500 ASN A 564 24.5 L L OUTSIDE RANGE REMARK 500 ASN A 611 23.8 L L OUTSIDE RANGE REMARK 500 VAL E 275 21.0 L L OUTSIDE RANGE REMARK 500 THR E 562 24.9 L L OUTSIDE RANGE REMARK 500 ASN E 564 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 E2101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A REMARK 800 162 RESIDUES 1101 TO 1102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A REMARK 800 627 RESIDUES 2101 TO 2102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF SUGAR BOUND TO ASN E REMARK 800 162 RESIDUES 1101 TO 1102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF SUGAR BOUND TO ASN G REMARK 800 55 RESIDUES 1101 TO 1102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN J OF SUGAR BOUND TO ASN J REMARK 800 55 RESIDUES 1101 TO 1102 REMARK 999 REMARK 999 SEQUENCE REMARK 999 PHE610 IS MODELED WITHOUT SIDE CHAIN. REMARK 999 THE SEQUENCE DEPOSITED UNDER GB CBI70317.1 (CHAINS G AND J) REMARK 999 CONTAINS THE WHOLE HEAVY CHAIN OF THE MONOCLONAL ANTIBODY REMARK 999 THAT THE FAB D6.3 FRAGMENT IS DERIVED FROM. THE SEQUENCE COPIED REMARK 999 HERE CORRESPONDS TO THE HEAVY CHAIN FRAGMENT THAT CONTRIBUTES REMARK 999 TO THE FAB, I.E. IT DOES NOT CONTAIN THE FC C-TERMINAL REGION. REMARK 999 CHAINS K AND L ARE GB CBI70318.1. THE CHAINS A AND E HAS C-TERMINAL REMARK 999 DOUBLE STREP-TAG.