REMARK 2 REMARK 2 RESOLUTION. 2.6 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 85.6 REMARK 3 NUMBER OF REFLECTIONS : 30508 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) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1607 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) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2109 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2450 REMARK 3 BIN FREE R VALUE SET COUNT : 117 REMARK 3 BIN FREE R VALUE : 0.3080 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5025 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 63 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.68000 REMARK 3 B22 (A**2) : -0.30000 REMARK 3 B33 (A**2) : 3.93000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.85000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.416 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.798 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5181 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4466 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7042 ; 1.136 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10307 ; 0.756 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 644 ; 6.256 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 229 ;31.203 ;23.493 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 777 ;16.185 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;19.790 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 750 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5839 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1120 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 982 ; 0.192 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4290 ; 0.176 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2439 ; 0.182 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 2892 ; 0.082 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 123 ; 0.151 ; 0.200 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): 6 ; 0.192 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.148 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.262 ; 0.200 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): 4130 ; 1.020 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5150 ; 1.279 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2409 ; 2.257 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1892 ; 3.236 ; 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 : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 10 A 330 REMARK 3 ORIGIN FOR THE GROUP (A): -0.0840 64.1710 46.4940 REMARK 3 T TENSOR REMARK 3 T11: -0.0789 T22: -0.2690 REMARK 3 T33: -0.1028 T12: 0.0452 REMARK 3 T13: -0.0725 T23: -0.0320 REMARK 3 L TENSOR REMARK 3 L11: 1.8325 L22: 0.9123 REMARK 3 L33: 0.9469 L12: -0.4241 REMARK 3 L13: -0.1857 L23: -0.0661 REMARK 3 S TENSOR REMARK 3 S11: 0.0821 S12: 0.1711 S13: -0.0468 REMARK 3 S21: -0.0661 S22: -0.0876 S23: 0.0130 REMARK 3 S31: -0.0126 S32: 0.0454 S33: 0.0055 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 108 REMARK 3 RESIDUE RANGE : H 2 H 113 REMARK 3 ORIGIN FOR THE GROUP (A): 39.5390 44.6540 22.6160 REMARK 3 T TENSOR REMARK 3 T11: -0.0661 T22: 0.0567 REMARK 3 T33: -0.0944 T12: 0.1095 REMARK 3 T13: -0.0488 T23: 0.0402 REMARK 3 L TENSOR REMARK 3 L11: 2.6076 L22: 2.1622 REMARK 3 L33: 2.9172 L12: -0.6744 REMARK 3 L13: 0.3886 L23: 0.6963 REMARK 3 S TENSOR REMARK 3 S11: 0.0946 S12: 0.4864 S13: 0.0916 REMARK 3 S21: -0.2527 S22: -0.0902 S23: 0.2577 REMARK 3 S31: -0.1479 S32: -0.2485 S33: -0.0045 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 109 L 205 REMARK 3 RESIDUE RANGE : H 114 H 180 REMARK 3 ORIGIN FOR THE GROUP (A): 56.1970 22.1890 10.9330 REMARK 3 T TENSOR REMARK 3 T11: 0.3041 T22: 0.6160 REMARK 3 T33: 0.1539 T12: 0.1086 REMARK 3 T13: -0.0746 T23: -0.2899 REMARK 3 L TENSOR REMARK 3 L11: 2.5536 L22: 2.5492 REMARK 3 L33: 3.4528 L12: 0.7631 REMARK 3 L13: 2.6041 L23: 2.1385 REMARK 3 S TENSOR REMARK 3 S11: 0.1520 S12: 0.6337 S13: -0.7801 REMARK 3 S21: -0.3444 S22: 0.4894 S23: -0.6394 REMARK 3 S31: 0.5276 S32: 0.6883 S33: -0.6414 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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. REMARK 4 REMARK 4 2J88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-06. REMARK 100 THE PDBE ID CODE IS EBI-28796. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-04 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 9.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.978 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32047 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 63.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.4 REMARK 200 DATA REDUNDANCY : 3.170 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 81.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.19 REMARK 200 R MERGE FOR SHELL (I) : 0.30000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.150 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 1FCQ, 1A7Q, 15C8 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.9 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.2M NACL, 0.1M REMARK 280 CHES PH9.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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+1/2,Y+1/2,Z 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 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 75.78150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.02500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.78150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.02500 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, 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 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 THR A 1 REMARK 465 PRO A 2 REMARK 465 ASP A 3 REMARK 465 ASN A 4 REMARK 465 ASN A 5 REMARK 465 LYS A 6 REMARK 465 THR A 7 REMARK 465 VAL A 8 REMARK 465 ARG A 9 REMARK 465 ASP A 66 REMARK 465 PRO A 67 REMARK 465 ASN A 68 REMARK 465 GLY A 69 REMARK 465 ASN A 70 REMARK 465 ASN A 334 REMARK 465 ASN A 335 REMARK 465 ASN A 336 REMARK 465 ALA A 337 REMARK 465 ASN A 338 REMARK 465 ASP A 339 REMARK 465 ARG A 340 REMARK 465 LEU A 341 REMARK 465 THR A 342 REMARK 465 VAL A 343 REMARK 465 ASP A 344 REMARK 465 VAL A 345 REMARK 465 SER A 346 REMARK 465 VAL A 347 REMARK 465 ASP A 348 REMARK 465 GLN A 349 REMARK 465 VAL A 350 REMARK 465 GLN H 1 REMARK 465 PRO H 122 REMARK 465 LEU H 123 REMARK 465 ALA H 124 REMARK 465 PRO H 125 REMARK 465 GLY H 126 REMARK 465 SER H 127 REMARK 465 ALA H 128 REMARK 465 ALA H 129 REMARK 465 GLN H 130 REMARK 465 THR H 131 REMARK 465 ASN H 132 REMARK 465 SER H 133 REMARK 465 MET H 134 REMARK 465 VAL H 135 REMARK 465 THR H 136 REMARK 465 LEU H 137 REMARK 465 SER H 157 REMARK 465 LEU H 158 REMARK 465 SER H 159 REMARK 465 SER H 160 REMARK 465 GLY H 161 REMARK 465 VAL H 162 REMARK 465 THR H 182 REMARK 465 VAL H 183 REMARK 465 PRO H 184 REMARK 465 SER H 185 REMARK 465 SER H 186 REMARK 465 THR H 187 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 SER L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 THR L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 GLY L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 ILE L 150 REMARK 465 ASP L 151 REMARK 465 GLY L 152 REMARK 465 SER L 153 REMARK 465 GLU L 154 REMARK 465 ARG L 155 REMARK 465 GLN L 156 REMARK 465 ASN L 157 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 GLU L 187 REMARK 465 ARG L 188 REMARK 465 HIS L 189 REMARK 465 ASN L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 VAL L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 ASN L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 GLU A 10 CG CD OE1 OE2 REMARK 470 LYS A 65 CB CG CD CE NZ REMARK 470 LYS A 86 CE NZ REMARK 470 ARG A 92 NE CZ NH1 NH2 REMARK 470 LYS A 102 CD CE NZ REMARK 470 LYS A 131 CD CE NZ REMARK 470 GLU A 135 CD OE1 OE2 REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 150 CG CD OE1 OE2 REMARK 470 GLN A 254 CD OE1 NE2 REMARK 470 GLU A 284 CD OE1 OE2 REMARK 470 ARG A 288 NE CZ NH1 NH2 REMARK 470 LYS A 289 CD CE NZ REMARK 470 ASP A 292 CG OD1 OD2 REMARK 470 ILE A 331 CB CG1 CG2 CD1 REMARK 470 ALA A 332 CB REMARK 470 LYS H 5 CD CE NZ REMARK 470 ILE H 11 CD1 REMARK 470 SER H 30 OG REMARK 470 THR H 73 OG1 CG2 REMARK 470 ARG H 75 CD NE CZ NH1 NH2 REMARK 470 LYS H 81 CE NZ REMARK 470 SER H 98 OG REMARK 470 GLN H 104 CG CD OE1 NE2 REMARK 470 LYS H 114 CB CG CD CE NZ REMARK 470 SER H 119 CB OG REMARK 470 VAL H 120 CB CG1 CG2 REMARK 470 GLY H 138 N REMARK 470 LYS H 142 CE NZ REMARK 470 VAL H 149 CG1 CG2 REMARK 470 VAL H 151 CG1 CG2 REMARK 470 SER H 155 CB OG REMARK 470 GLY H 156 C O REMARK 470 THR H 164 CB OG1 CG2 REMARK 470 SER H 171 CB OG REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 LEU L 11 CD1 CD2 REMARK 470 ILE L 21 CG2 CD1 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 27 CD OE1 OE2 REMARK 470 SER L 31 OG REMARK 470 GLN L 40 CB CG CD OE1 NE2 REMARK 470 GLY L 41 C O REMARK 470 LYS L 42 CD CE NZ REMARK 470 LYS L 52 CG CD CE NZ REMARK 470 GLU L 56 CG CD OE1 OE2 REMARK 470 SER L 60 OG REMARK 470 SER L 65 OG REMARK 470 SER L 67 OG REMARK 470 GLN L 70 CD OE1 NE2 REMARK 470 LYS L 74 CG CD CE NZ REMARK 470 ILE L 75 CG1 CD1 REMARK 470 SER L 77 OG REMARK 470 GLU L 81 CB CG CD OE1 OE2 REMARK 470 ARG L 103 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 105 CB CG CD OE1 OE2 REMARK 470 ILE L 106 CG1 CD1 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 PHE L 118 C O REMARK 470 VAL L 132 CB CG1 CG2 REMARK 470 LYS L 142 CE NZ REMARK 470 ILE L 144 CG1 CG2 CD1 REMARK 470 LYS L 147 CD CE NZ REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 GLY L 158 N CA REMARK 470 LEU L 160 CB CG CD1 CD2 REMARK 470 SER L 171 OG REMARK 470 LEU L 179 CD1 CD2 REMARK 470 LEU L 181 CD1 CD2 REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 ASP L 184 CB CG OD1 OD2 REMARK 470 GLU L 185 CG CD OE1 OE2 REMARK 470 THR L 193 CB OG1 CG2 REMARK 470 GLU L 195 CG CD OE1 OE2 REMARK 470 THR L 197 CB OG1 CG2 REMARK 470 LYS L 199 CB CG CD CE NZ REMARK 470 SER L 203 CB OG REMARK 470 PRO L 204 CB CG CD REMARK 470 ILE L 205 CB CG1 CG2 CD1 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 104 109.50 -37.97 REMARK 500 GLU A 113 10.06 57.77 REMARK 500 ALA A 124 -117.54 63.21 REMARK 500 ALA A 185 -7.91 86.04 REMARK 500 CYS A 189 -37.69 -150.96 REMARK 500 ILE A 307 50.17 -140.86 REMARK 500 GLU A 323 -62.81 -136.71 REMARK 500 ALA A 332 -50.73 142.97 REMARK 500 SER H 15 -11.30 92.40 REMARK 500 LEU H 48 -64.03 -109.19 REMARK 500 SER H 155 -51.78 101.26 REMARK 500 TYR L 30 -115.75 35.85 REMARK 500 ALA L 51 -42.75 69.81 REMARK 500 SER L 63 148.08 -170.28 REMARK 500 SER L 77 80.59 21.96 REMARK 500 HIS L 91 37.66 -143.67 REMARK 500 THR L 94 -178.79 -67.80 REMARK 500 ARG L 96 62.44 -151.49 REMARK 500 LYS L 199 30.09 -72.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU H 63 LYS H 64 149.46 REMARK 500 LYS H 64 SER H 65 -36.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FCQ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM REMARK 900 HYALURONIDASE REMARK 900 RELATED ID: 1FCU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE (TRIGONAL) OF BEE VENOM REMARK 900 HYALURONIDASE REMARK 900 RELATED ID: 1FCV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BEE VENOM HYALURONIDASE REMARK 900 IN COMPLEXWITH HYALURONIC ACID TETRAMER