REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.55 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 43380 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) : 0.251 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.295 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2308 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) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2990 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.39 REMARK 3 BIN R VALUE (WORKING SET) : 0.3010 REMARK 3 BIN FREE R VALUE SET COUNT : 169 REMARK 3 BIN FREE R VALUE : 0.3910 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6614 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 470 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.11 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.64000 REMARK 3 B22 (A**2) : -2.58000 REMARK 3 B33 (A**2) : 4.33000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.51000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.408 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.285 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.100 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.897 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6802 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 4620 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9266 ; 1.217 ; 1.947 REMARK 3 BOND ANGLES OTHERS (DEGREES): 11135 ; 0.850 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 836 ; 6.662 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;31.323 ;23.141 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1026 ;14.710 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;13.268 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 984 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7672 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1503 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1192 ; 0.165 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4902 ; 0.190 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3162 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 3726 ; 0.079 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 345 ; 0.171 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.053 ; 0.200 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): 24 ; 0.177 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 69 ; 0.191 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.145 ; 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): 5330 ; 0.524 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1699 ; 0.069 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6760 ; 0.612 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3225 ; 0.877 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2506 ; 1.308 ; 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 322 A 349 2 REMARK 3 1 C 322 C 349 2 REMARK 3 2 A 361 A 369 2 REMARK 3 2 C 361 C 369 2 REMARK 3 3 A 381 A 502 2 REMARK 3 3 C 381 C 502 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 930 ; 0.03 ; 0.05 REMARK 3 MEDIUM POSITIONAL 1 A (A): 1487 ; 0.14 ; 0.50 REMARK 3 TIGHT THERMAL 1 A (A**2): 930 ; 0.09 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 1487 ; 0.75 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 240 2 REMARK 3 1 D 1 D 240 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 B (A): 1319 ; 0.03 ; 0.05 REMARK 3 MEDIUM POSITIONAL 2 B (A): 1983 ; 0.13 ; 0.50 REMARK 3 TIGHT THERMAL 2 B (A**2): 1319 ; 0.08 ; 0.50 REMARK 3 MEDIUM THERMAL 2 B (A**2): 1983 ; 0.71 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 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 : B 1 B 244 REMARK 3 ORIGIN FOR THE GROUP (A): -3.3270 -24.4040 15.3570 REMARK 3 T TENSOR REMARK 3 T11: -0.1336 T22: -0.1788 REMARK 3 T33: -0.1579 T12: -0.0391 REMARK 3 T13: 0.0660 T23: -0.0009 REMARK 3 L TENSOR REMARK 3 L11: 2.2784 L22: 2.1958 REMARK 3 L33: 1.3683 L12: -0.6814 REMARK 3 L13: 0.7547 L23: 0.3151 REMARK 3 S TENSOR REMARK 3 S11: -0.0176 S12: -0.0623 S13: -0.1542 REMARK 3 S21: 0.0959 S22: 0.0020 S23: 0.0426 REMARK 3 S31: 0.1855 S32: -0.0073 S33: 0.0156 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 318 C 505 REMARK 3 ORIGIN FOR THE GROUP (A): 27.2230 56.9630 15.2330 REMARK 3 T TENSOR REMARK 3 T11: -0.1368 T22: -0.1580 REMARK 3 T33: -0.1466 T12: -0.0320 REMARK 3 T13: -0.0491 T23: 0.0149 REMARK 3 L TENSOR REMARK 3 L11: 2.1035 L22: 2.1672 REMARK 3 L33: 1.1555 L12: -0.5523 REMARK 3 L13: -0.8272 L23: -0.2871 REMARK 3 S TENSOR REMARK 3 S11: 0.0445 S12: -0.0494 S13: 0.1647 REMARK 3 S21: 0.0373 S22: -0.0597 S23: -0.1275 REMARK 3 S31: -0.1738 S32: 0.0346 S33: 0.0152 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 245 REMARK 3 ORIGIN FOR THE GROUP (A): 13.6840 1.8600 23.4500 REMARK 3 T TENSOR REMARK 3 T11: -0.1624 T22: -0.1586 REMARK 3 T33: -0.1844 T12: 0.0007 REMARK 3 T13: 0.0469 T23: -0.0311 REMARK 3 L TENSOR REMARK 3 L11: 3.0356 L22: 2.6452 REMARK 3 L33: 0.5113 L12: 0.5675 REMARK 3 L13: -0.2013 L23: -0.2761 REMARK 3 S TENSOR REMARK 3 S11: 0.0736 S12: -0.1291 S13: 0.2510 REMARK 3 S21: 0.1468 S22: -0.0906 S23: -0.2222 REMARK 3 S31: -0.0361 S32: 0.1262 S33: 0.0171 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 319 A 509 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1890 30.6650 23.4250 REMARK 3 T TENSOR REMARK 3 T11: -0.1794 T22: -0.1441 REMARK 3 T33: -0.1364 T12: 0.0093 REMARK 3 T13: -0.0266 T23: 0.0388 REMARK 3 L TENSOR REMARK 3 L11: 2.2400 L22: 2.7906 REMARK 3 L33: 0.7073 L12: 0.8526 REMARK 3 L13: 0.2043 L23: 0.0223 REMARK 3 S TENSOR REMARK 3 S11: 0.0977 S12: -0.2278 S13: -0.2331 REMARK 3 S21: 0.1663 S22: -0.0800 S23: 0.2730 REMARK 3 S31: 0.0181 S32: -0.1195 S33: -0.0177 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 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 2GHW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-06. REMARK 100 THE RCSB ID CODE IS RCSB037138. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-SEP-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE, DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51915 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.14500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP, PHASER REMARK 200 STARTING MODEL: 2AJF CHAIN F, 1DZB CHAIN A REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% PEG4000, 0.1M SODIUM ACETATE, REMARK 280 0.2M AMMONIUM SULFATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 290K 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 87.95100 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 350 REMARK 350 BIOMOLECULE: 2 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: 2490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 314 REMARK 465 ALA A 315 REMARK 465 ASP A 316 REMARK 465 PRO A 317 REMARK 465 ASN A 318 REMARK 465 VAL A 510 REMARK 465 SER A 511 REMARK 465 GLY A 512 REMARK 465 LEU A 513 REMARK 465 VAL A 514 REMARK 465 PRO A 515 REMARK 465 ARG A 516 REMARK 465 MET B -1 REMARK 465 ALA B 0 REMARK 465 GLY B 120 REMARK 465 GLY B 121 REMARK 465 SER B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 GLY B 126 REMARK 465 SER B 127 REMARK 465 GLY B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 ARG B 245 REMARK 465 MET C 314 REMARK 465 ALA C 315 REMARK 465 ASP C 316 REMARK 465 PRO C 317 REMARK 465 ALA C 506 REMARK 465 PRO C 507 REMARK 465 ALA C 508 REMARK 465 THR C 509 REMARK 465 VAL C 510 REMARK 465 SER C 511 REMARK 465 GLY C 512 REMARK 465 LEU C 513 REMARK 465 VAL C 514 REMARK 465 PRO C 515 REMARK 465 ARG C 516 REMARK 465 MET D -1 REMARK 465 ALA D 0 REMARK 465 GLY D 118 REMARK 465 GLY D 119 REMARK 465 GLY D 120 REMARK 465 GLY D 121 REMARK 465 SER D 122 REMARK 465 GLY D 123 REMARK 465 GLY D 124 REMARK 465 GLY D 125 REMARK 465 GLY D 126 REMARK 465 SER D 127 REMARK 465 GLY D 128 REMARK 465 GLY D 129 REMARK 465 GLY D 130 REMARK 465 GLY D 131 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 D 284 O HOH D 409 1.72 REMARK 500 O HOH D 368 O HOH D 377 1.93 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 ARG B 156 NE - CZ - NH1 ANGL. DEV. = 3.5 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 A 321 65.85 60.50 REMARK 500 LYS A 373 31.48 -88.60 REMARK 500 ASN A 409 -60.63 -122.87 REMARK 500 ASP A 415 33.39 -93.49 REMARK 500 LYS B 43 -167.75 -129.40 REMARK 500 VAL B 48 -62.12 -100.24 REMARK 500 SER B 101 60.32 37.37 REMARK 500 VAL B 115 78.76 -106.62 REMARK 500 SER B 117 -28.13 -156.02 REMARK 500 ARG B 162 -123.88 47.87 REMARK 500 ALA B 183 -45.36 74.87 REMARK 500 PRO B 212 -37.83 -39.70 REMARK 500 VAL B 243 62.31 -117.59 REMARK 500 ILE C 319 132.67 -173.31 REMARK 500 THR C 320 -68.69 -101.84 REMARK 500 ASN C 321 77.16 -111.21 REMARK 500 ASP C 351 68.80 -119.90 REMARK 500 THR C 359 56.54 -104.64 REMARK 500 ASN C 409 -65.95 -123.63 REMARK 500 LEU C 504 52.39 -90.88 REMARK 500 SER D 116 -152.65 -96.84 REMARK 500 ARG D 162 -123.28 43.67 REMARK 500 ASN D 164 47.52 -86.35 REMARK 500 ALA D 183 -47.18 78.99 REMARK 500 ARG D 209 80.73 32.60 REMARK 500 LEU D 242 95.35 -165.85 REMARK 500 VAL D 243 -65.70 -128.82 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 TYR B 102 TYR B 103 148.15 REMARK 500 TYR D 102 TYR D 103 147.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 126 DISTANCE = 9.76 ANGSTROMS REMARK 525 HOH D 282 DISTANCE = 8.20 ANGSTROMS REMARK 525 HOH C 517 DISTANCE = 6.80 ANGSTROMS REMARK 525 HOH D 283 DISTANCE = 7.88 ANGSTROMS REMARK 525 HOH C 522 DISTANCE = 7.27 ANGSTROMS REMARK 525 HOH C 542 DISTANCE = 5.16 ANGSTROMS REMARK 525 HOH B 339 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH A 547 DISTANCE = 5.04 ANGSTROMS REMARK 525 HOH A 548 DISTANCE = 25.72 ANGSTROMS REMARK 525 HOH A 549 DISTANCE = 27.80 ANGSTROMS REMARK 525 HOH B 343 DISTANCE = 5.30 ANGSTROMS REMARK 525 HOH A 553 DISTANCE = 17.38 ANGSTROMS REMARK 525 HOH A 554 DISTANCE = 15.99 ANGSTROMS REMARK 525 HOH C 552 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH A 555 DISTANCE = 26.21 ANGSTROMS REMARK 525 HOH D 319 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH D 321 DISTANCE = 5.55 ANGSTROMS REMARK 525 HOH D 322 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH C 557 DISTANCE = 5.54 ANGSTROMS REMARK 525 HOH B 358 DISTANCE = 8.03 ANGSTROMS REMARK 525 HOH B 359 DISTANCE = 10.35 ANGSTROMS REMARK 525 HOH B 360 DISTANCE = 7.92 ANGSTROMS REMARK 525 HOH B 362 DISTANCE = 9.40 ANGSTROMS REMARK 525 HOH D 334 DISTANCE = 13.57 ANGSTROMS REMARK 525 HOH B 365 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH D 336 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH B 366 DISTANCE = 12.20 ANGSTROMS REMARK 525 HOH A 574 DISTANCE = 5.94 ANGSTROMS REMARK 525 HOH B 368 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH D 339 DISTANCE = 8.44 ANGSTROMS REMARK 525 HOH B 369 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH C 574 DISTANCE = 6.46 ANGSTROMS REMARK 525 HOH D 341 DISTANCE = 14.16 ANGSTROMS REMARK 525 HOH B 371 DISTANCE = 18.10 ANGSTROMS REMARK 525 HOH B 372 DISTANCE = 13.00 ANGSTROMS REMARK 525 HOH D 343 DISTANCE = 11.87 ANGSTROMS REMARK 525 HOH D 344 DISTANCE = 11.31 ANGSTROMS REMARK 525 HOH D 345 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH B 378 DISTANCE = 8.22 ANGSTROMS REMARK 525 HOH D 349 DISTANCE = 7.35 ANGSTROMS REMARK 525 HOH B 379 DISTANCE = 9.03 ANGSTROMS REMARK 525 HOH D 350 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH A 587 DISTANCE = 7.05 ANGSTROMS REMARK 525 HOH A 589 DISTANCE = 7.32 ANGSTROMS REMARK 525 HOH A 591 DISTANCE = 6.58 ANGSTROMS REMARK 525 HOH B 384 DISTANCE = 8.51 ANGSTROMS REMARK 525 HOH B 385 DISTANCE = 8.40 ANGSTROMS REMARK 525 HOH C 594 DISTANCE = 5.73 ANGSTROMS REMARK 525 HOH D 360 DISTANCE = 11.60 ANGSTROMS REMARK 525 HOH D 362 DISTANCE = 7.40 ANGSTROMS REMARK 525 HOH A 599 DISTANCE = 34.96 ANGSTROMS REMARK 525 HOH C 597 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH B 393 DISTANCE = 11.07 ANGSTROMS REMARK 525 HOH D 364 DISTANCE = 5.49 ANGSTROMS REMARK 525 HOH A 602 DISTANCE = 8.14 ANGSTROMS REMARK 525 HOH B 395 DISTANCE = 8.76 ANGSTROMS REMARK 525 HOH B 396 DISTANCE = 10.07 ANGSTROMS REMARK 525 HOH D 367 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH B 397 DISTANCE = 8.24 ANGSTROMS REMARK 525 HOH C 604 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH D 370 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH C 605 DISTANCE = 7.55 ANGSTROMS REMARK 525 HOH D 374 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH C 612 DISTANCE = 5.69 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 20 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 88 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 142 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 246 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 517 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2GHV RELATED DB: PDB REMARK 900 CRYSTALS TRUCTURE OF S1 RBD REMARK 900 RELATED ID: 2AJF RELATED DB: PDB REMARK 900 CRYSTALS TRUCTURE OF S1 RBD IN COMPLEX WITH ITS RECEPTOR REMARK 900 RELATED ID: 1DZB RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE SEQUENCE OF ANTI-SARS SCFV ANTIBODY, 80R IS REMARK 999 NOT AVAILABLE AT UNIPROT SEQUENCE DATABASE AT THE TIME REMARK 999 OF PROCESSING.