REMARK 2 REMARK 2 RESOLUTION. 4.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 10491 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) : 0.291 REMARK 3 R VALUE (WORKING SET) : 0.289 REMARK 3 FREE R VALUE : 0.335 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 530 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) : 4.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.41 REMARK 3 REFLECTION IN BIN (WORKING SET) : 736 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.15 REMARK 3 BIN R VALUE (WORKING SET) : 0.3790 REMARK 3 BIN FREE R VALUE SET COUNT : 39 REMARK 3 BIN FREE R VALUE : 0.4540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4454 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 117 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 226.59 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.974 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.868 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 160.517 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.892 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4698 ; 0.010 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6387 ; 1.617 ; 1.985 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 557 ; 7.048 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;36.617 ;24.300 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 768 ;19.182 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;18.903 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 719 ; 0.103 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3497 ; 0.005 ; 0.021 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 5 E 310 REMARK 3 RESIDUE RANGE : E 401 E 409 REMARK 3 ORIGIN FOR THE GROUP (A): -20.4744 -28.9416 -69.8635 REMARK 3 T TENSOR REMARK 3 T11: 0.5265 T22: 0.8880 REMARK 3 T33: 0.7541 T12: 0.0647 REMARK 3 T13: 0.2141 T23: 0.2411 REMARK 3 L TENSOR REMARK 3 L11: 4.6951 L22: 3.0733 REMARK 3 L33: 4.7588 L12: -0.7219 REMARK 3 L13: -1.5069 L23: 0.5124 REMARK 3 S TENSOR REMARK 3 S11: -0.1691 S12: 0.1597 S13: -0.4484 REMARK 3 S21: 0.2224 S22: 0.1154 S23: 0.2925 REMARK 3 S31: 0.1516 S32: 0.2265 S33: 0.0537 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 116 REMARK 3 ORIGIN FOR THE GROUP (A): -24.5855 -23.7708-110.0858 REMARK 3 T TENSOR REMARK 3 T11: 1.3701 T22: 1.8043 REMARK 3 T33: 0.8952 T12: 0.5155 REMARK 3 T13: -0.3455 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 7.7240 L22: 2.9572 REMARK 3 L33: 6.9404 L12: -2.6125 REMARK 3 L13: 1.1166 L23: -2.9644 REMARK 3 S TENSOR REMARK 3 S11: 0.9529 S12: 1.3024 S13: -0.5774 REMARK 3 S21: -1.1883 S22: -0.1597 S23: 1.0910 REMARK 3 S31: -0.0358 S32: -1.7587 S33: -0.7932 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 114 REMARK 3 ORIGIN FOR THE GROUP (A): -9.4985 -9.6414-103.6780 REMARK 3 T TENSOR REMARK 3 T11: 1.7742 T22: 0.9726 REMARK 3 T33: 0.2923 T12: 0.0133 REMARK 3 T13: 0.6911 T23: -0.0965 REMARK 3 L TENSOR REMARK 3 L11: 7.6041 L22: 8.9105 REMARK 3 L33: 1.4376 L12: -1.1262 REMARK 3 L13: 1.5026 L23: -2.7617 REMARK 3 S TENSOR REMARK 3 S11: 0.4687 S12: 0.9392 S13: 0.2950 REMARK 3 S21: -0.0002 S22: -0.0967 S23: 0.2096 REMARK 3 S31: -0.7191 S32: 0.3726 S33: -0.3720 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 21 REMARK 3 ORIGIN FOR THE GROUP (A): -36.5703 -22.1691 -42.8161 REMARK 3 T TENSOR REMARK 3 T11: 0.6662 T22: 0.6336 REMARK 3 T33: 0.6445 T12: 0.3850 REMARK 3 T13: 0.1472 T23: 0.3771 REMARK 3 L TENSOR REMARK 3 L11: 9.8957 L22: 33.3564 REMARK 3 L33: 11.3482 L12: -6.2265 REMARK 3 L13: -10.0509 L23: 0.5932 REMARK 3 S TENSOR REMARK 3 S11: 0.6417 S12: 0.2209 S13: 0.0784 REMARK 3 S21: 0.1361 S22: -0.2342 S23: 1.7204 REMARK 3 S31: -0.7532 S32: -0.1180 S33: -0.4075 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 7 B 21 REMARK 3 ORIGIN FOR THE GROUP (A): -32.2561 -31.7512 -43.3386 REMARK 3 T TENSOR REMARK 3 T11: 0.9818 T22: 0.7755 REMARK 3 T33: 0.6463 T12: 0.3014 REMARK 3 T13: 0.1540 T23: 0.1882 REMARK 3 L TENSOR REMARK 3 L11: 40.5191 L22: 13.4613 REMARK 3 L33: 17.3558 L12: 16.0583 REMARK 3 L13: 21.8130 L23: 14.9303 REMARK 3 S TENSOR REMARK 3 S11: 0.1980 S12: -2.2609 S13: -0.5046 REMARK 3 S21: 0.8156 S22: 0.3357 S23: -0.3880 REMARK 3 S31: 0.5934 S32: -0.2341 S33: -0.5337 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : F 705 F 715 REMARK 3 ORIGIN FOR THE GROUP (A): -27.3789 -22.6840 -51.5387 REMARK 3 T TENSOR REMARK 3 T11: 0.4765 T22: 1.5840 REMARK 3 T33: 0.5553 T12: 0.4863 REMARK 3 T13: 0.2757 T23: -0.0505 REMARK 3 L TENSOR REMARK 3 L11: 16.5334 L22: 25.7766 REMARK 3 L33: 43.8126 L12: 11.7469 REMARK 3 L13: 17.2102 L23: -9.0157 REMARK 3 S TENSOR REMARK 3 S11: 0.1831 S12: -1.2312 S13: -0.9935 REMARK 3 S21: -0.7291 S22: 0.5290 S23: -0.9950 REMARK 3 S31: 1.1949 S32: -2.9063 S33: -0.7120 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: U VALUES: WITH TLS ADDED REMARK 4 REMARK 4 3W13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-12. REMARK 100 THE RCSB ID CODE IS RCSB095752. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAR-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11033 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.303 REMARK 200 RESOLUTION RANGE LOW (A) : 169.228 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.10100 REMARK 200 FOR THE DATA SET : 8.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.30 REMARK 200 R MERGE FOR SHELL (I) : 1.09000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 3LOH,2WRW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 79.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.97 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9-1.1M TRI-SODIUM CITRATE, 0.1M REMARK 280 IMIDAZOLE-HCL, 0.02% SOIDUM AZIDE, PH 8.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z,-X,-Y REMARK 290 7555 -Z,-X,Y REMARK 290 8555 -Z,X,-Y REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z,-X REMARK 290 11555 Y,-Z,-X REMARK 290 12555 -Y,-Z,X 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 0.00000 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 0.00000 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 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 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: E, C, D, A, B, F 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 HIS E 1 REMARK 465 LEU E 2 REMARK 465 TYR E 3 REMARK 465 PRO E 4 REMARK 465 PRO E 160 REMARK 465 GLY E 161 REMARK 465 THR E 162 REMARK 465 ALA E 163 REMARK 465 LYS E 164 REMARK 465 GLY E 165 REMARK 465 LYS E 166 REMARK 465 THR E 167 REMARK 465 CYS E 266 REMARK 465 LYS E 267 REMARK 465 ASN E 268 REMARK 465 SER E 269 REMARK 465 ARG E 270 REMARK 465 ARG E 271 REMARK 465 GLN E 272 REMARK 465 GLY E 273 REMARK 465 CYS E 274 REMARK 465 HIS E 275 REMARK 465 PHE B 1 REMARK 465 VAL B 2 REMARK 465 ASN B 3 REMARK 465 GLN B 4 REMARK 465 HIS B 5 REMARK 465 LEU B 6 REMARK 465 ARG B 22 REMARK 465 GLY B 23 REMARK 465 PHE B 24 REMARK 465 PHE B 25 REMARK 465 PR9 B 26 REMARK 465 GLU F 697 REMARK 465 GLU F 698 REMARK 465 SER F 699 REMARK 465 SER F 700 REMARK 465 PHE F 701 REMARK 465 ARG F 702 REMARK 465 LYS F 703 REMARK 465 THR F 704 REMARK 465 PRO F 716 REMARK 465 ARG F 717 REMARK 465 PRO F 718 REMARK 465 SER F 719 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 SER E 198 O LEU E 213 2.09 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 VAL F 715 N VAL F 715 CA 0.147 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 CYS E 188 CA - CB - SG ANGL. DEV. = 6.8 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 ASN E 15 -84.36 72.99 REMARK 500 PRO E 43 -39.78 -38.78 REMARK 500 ASP E 59 -97.09 -98.75 REMARK 500 PHE E 89 -105.38 56.95 REMARK 500 GLU E 97 50.14 37.33 REMARK 500 HIS E 100 -22.64 103.51 REMARK 500 ARG E 114 -96.83 62.17 REMARK 500 ASN E 122 77.91 -115.30 REMARK 500 GLU E 124 -31.28 91.85 REMARK 500 CYS E 126 -160.68 -119.09 REMARK 500 GLU E 153 7.96 49.06 REMARK 500 GLU E 154 62.84 -119.88 REMARK 500 ASN E 175 -121.12 -101.59 REMARK 500 LYS E 197 -133.74 50.07 REMARK 500 LEU E 213 -81.81 -99.39 REMARK 500 ASN E 230 -96.06 -96.87 REMARK 500 GLN E 249 17.58 57.82 REMARK 500 TRP E 251 -21.28 -159.34 REMARK 500 LEU E 299 -1.49 61.49 REMARK 500 PRO C 14 155.08 -46.89 REMARK 500 SER C 15 -5.71 72.51 REMARK 500 LYS C 43 -161.84 -108.03 REMARK 500 LYS C 64 74.40 -69.18 REMARK 500 SER C 65 7.23 56.84 REMARK 500 SER C 84 72.57 40.72 REMARK 500 PRO C 99 49.14 -84.55 REMARK 500 TYR C 100 -56.92 -24.56 REMARK 500 PRO C 104 -97.13 -88.62 REMARK 500 TYR C 107 110.89 73.92 REMARK 500 ASN D 34 -5.25 -147.26 REMARK 500 ALA D 57 -2.84 54.07 REMARK 500 SER D 58 -11.93 -143.91 REMARK 500 SER D 83 97.39 66.10 REMARK 500 ALA D 86 -66.17 -25.44 REMARK 500 TYR D 100 -139.12 59.78 REMARK 500 CYS A 7 -66.84 -109.49 REMARK 500 LEU A 13 -89.00 34.78 REMARK 500 ASN F 711 -19.78 -47.86 REMARK 500 VAL F 713 59.54 -98.64 REMARK 500 PHE F 714 94.91 -161.51 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 ALA D 114 22.9 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 E 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES E 402 to 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES E 407 to 409 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2DTG RELATED DB: PDB REMARK 900 RELATED ID: 3LOH RELATED DB: PDB REMARK 900 RELATED ID: 2WRW RELATED DB: PDB REMARK 900 RELATED ID: 3W11 RELATED DB: PDB REMARK 900 RELATED ID: 3W12 RELATED DB: PDB REMARK 900 RELATED ID: 3W14 RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 HIS E 144 IS NATURAL VARIANT RS1051692. THE SEQUENCE OF CHIAN F IS REMARK 999 ISOFORM SHORT OF INSULIN RECEPTOR, P06213-2. B26 TYR MUTATED TO D- REMARK 999 PRO; B27-B30 ARE DELETED; B26 C-TERMINUS IS FINISHED WITH CONH2 REMARK 999 (CARBOXYAMIDE) NOT A COOH GROUP.