REMARK 2 REMARK 2 RESOLUTION. 2.65 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.70 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 48955 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) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2478 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) : 2.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.71 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3327 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.09 REMARK 3 BIN R VALUE (WORKING SET) : 0.2950 REMARK 3 BIN FREE R VALUE SET COUNT : 161 REMARK 3 BIN FREE R VALUE : 0.3720 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8997 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 132 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 62.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.11 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.01000 REMARK 3 B22 (A**2) : 0.01000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.01000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.578 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.325 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.214 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9217 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6082 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12544 ; 0.927 ; 1.953 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14823 ; 0.643 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1202 ; 5.130 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 349 ;30.776 ;23.782 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1408 ;15.617 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;17.741 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1436 ; 0.054 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10362 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1875 ; 0.000 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1591 ; 0.208 ; 0.300 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5906 ; 0.208 ; 0.300 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4370 ; 0.188 ; 0.500 REMARK 3 NON-BONDED TORSION OTHERS (A): 5064 ; 0.089 ; 0.500 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 512 ; 0.188 ; 0.500 REMARK 3 H-BOND (X...Y) OTHERS (A): 6 ; 0.101 ; 0.500 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): 23 ; 0.132 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): 49 ; 0.230 ; 0.300 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.161 ; 0.500 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): 6112 ; 0.585 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2488 ; 0.067 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9526 ; 1.052 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3600 ; 1.039 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3014 ; 1.696 ; 6.000 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 : NULL 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 : 1.40 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3LH2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10. REMARK 100 THE RCSB ID CODE IS RCSB057269. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-OCT-08 REMARK 200 TEMPERATURE (KELVIN) : 107 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : RIGAKU VARIMAX HF REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK REMARK 200 DATA SCALING SOFTWARE : D*TREK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49017 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650 REMARK 200 RESOLUTION RANGE LOW (A) : 28.010 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.880 REMARK 200 R MERGE (I) : 0.09500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.68 REMARK 200 R MERGE FOR SHELL (I) : 0.37600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.700 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: COMPUTATIONALLY-DERIVED MODEL OF THE EPITOPE- REMARK 200 SCAFFOLD FV COMPLEX, WITH THE FV BASED ON PDB ID 1TZG. REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NA ACETATE, IMIDAZOLE, PH 8, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K 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 72.97500 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, V, K, O, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, U, I, M, J, N 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 S 1 REMARK 465 HIS S 2 REMARK 465 HIS S 3 REMARK 465 HIS S 4 REMARK 465 HIS S 5 REMARK 465 ALA S 51 REMARK 465 ALA S 54 REMARK 465 ALA S 72 REMARK 465 ILE S 73 REMARK 465 GLU S 74 REMARK 465 GLU S 75 REMARK 465 GLU S 76 REMARK 465 GLY H -1 REMARK 465 SER H 0 REMARK 465 GLN H 1 REMARK 465 GLY H 103 REMARK 465 ALA H 104 REMARK 465 GLY H 105 REMARK 465 TRP H 106 REMARK 465 HIS H 133 REMARK 465 HIS H 134 REMARK 465 HIS H 135 REMARK 465 HIS T 1 REMARK 465 HIS T 2 REMARK 465 HIS T 3 REMARK 465 HIS T 4 REMARK 465 HIS T 5 REMARK 465 HIS T 6 REMARK 465 GLU T 74 REMARK 465 GLU T 75 REMARK 465 GLU T 76 REMARK 465 GLY I -1 REMARK 465 SER I 0 REMARK 465 GLN I 1 REMARK 465 GLY I 103 REMARK 465 ALA I 104 REMARK 465 GLY I 105 REMARK 465 TRP I 106 REMARK 465 LEU I 107 REMARK 465 HIS I 134 REMARK 465 HIS I 135 REMARK 465 HIS V 1 REMARK 465 HIS V 2 REMARK 465 HIS V 3 REMARK 465 HIS V 4 REMARK 465 HIS V 5 REMARK 465 HIS V 6 REMARK 465 GLU V 75 REMARK 465 GLU V 76 REMARK 465 GLY K -1 REMARK 465 SER K 0 REMARK 465 GLN K 1 REMARK 465 LEU K 128 REMARK 465 GLU K 129 REMARK 465 HIS K 130 REMARK 465 HIS K 131 REMARK 465 HIS K 132 REMARK 465 HIS K 133 REMARK 465 HIS K 134 REMARK 465 HIS K 135 REMARK 465 MET L -1 REMARK 465 VAL L 110 REMARK 465 PRO L 111 REMARK 465 ARG L 112 REMARK 465 MET M -1 REMARK 465 ALA M 0 REMARK 465 LEU M 109 REMARK 465 VAL M 110 REMARK 465 PRO M 111 REMARK 465 ARG M 112 REMARK 465 MET O -1 REMARK 465 VAL O 110 REMARK 465 PRO O 111 REMARK 465 ARG O 112 REMARK 465 HIS U 1 REMARK 465 HIS U 2 REMARK 465 HIS U 3 REMARK 465 HIS U 4 REMARK 465 HIS U 5 REMARK 465 HIS U 6 REMARK 465 GLU U 75 REMARK 465 GLU U 76 REMARK 465 MET N -1 REMARK 465 VAL N 110 REMARK 465 PRO N 111 REMARK 465 ARG N 112 REMARK 465 GLY J -1 REMARK 465 SER J 0 REMARK 465 GLN J 1 REMARK 465 SER J 127 REMARK 465 LEU J 128 REMARK 465 GLU J 129 REMARK 465 HIS J 130 REMARK 465 HIS J 131 REMARK 465 HIS J 132 REMARK 465 HIS J 133 REMARK 465 HIS J 134 REMARK 465 HIS J 135 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 HIS S 6 CG ND1 CD2 CE1 NE2 REMARK 470 LYS S 32 CE NZ REMARK 470 ILE S 33 CD1 REMARK 470 GLN S 69 CD OE1 NE2 REMARK 470 GLN H 3 CD OE1 NE2 REMARK 470 LYS H 23 NZ REMARK 470 SER H 28 OG REMARK 470 ARG H 63 NE CZ NH1 NH2 REMARK 470 ARG H 87 NE CZ NH1 NH2 REMARK 470 LEU H 107 CD1 CD2 REMARK 470 ASP T 30 CG OD1 OD2 REMARK 470 LYS T 32 CE NZ REMARK 470 ILE T 34 CG1 CG2 CD1 REMARK 470 LYS T 52 NZ REMARK 470 ARG I 63 CZ NH1 NH2 REMARK 470 THR I 102 OG1 CG2 REMARK 470 LEU V 23 CD1 CD2 REMARK 470 ASP V 30 CG OD1 OD2 REMARK 470 LYS V 32 CG CD CE NZ REMARK 470 ARG V 45 CZ NH1 NH2 REMARK 470 SER V 67 OG REMARK 470 GLN V 69 CD OE1 NE2 REMARK 470 LEU V 71 CD1 CD2 REMARK 470 ILE V 73 CD1 REMARK 470 GLU V 74 CG CD OE1 OE2 REMARK 470 GLN K 3 CD OE1 NE2 REMARK 470 ARG K 13 CD NE CZ NH1 NH2 REMARK 470 SER K 28 OG REMARK 470 ARG K 43 CZ NH1 NH2 REMARK 470 ARG K 63 NE CZ NH1 NH2 REMARK 470 ARG K 87 NH1 NH2 REMARK 470 SER K 127 OG REMARK 470 ARG L 18 NE CZ NH1 NH2 REMARK 470 SER L 57 OG REMARK 470 LEU L 109 CG CD1 CD2 REMARK 470 ARG M 18 NE CZ NH1 NH2 REMARK 470 GLU M 80 CD OE1 OE2 REMARK 470 GLU M 82 CD OE1 OE2 REMARK 470 GLN O 11 OE1 NE2 REMARK 470 ARG O 78 CG CD NE CZ NH1 NH2 REMARK 470 LYS O 104 NZ REMARK 470 LEU O 109 CG CD1 CD2 REMARK 470 LEU U 23 CD1 CD2 REMARK 470 LYS U 32 CD CE NZ REMARK 470 ILE U 33 CD1 REMARK 470 GLU U 74 CG CD OE1 OE2 REMARK 470 ARG N 24 CG CD NE CZ NH1 NH2 REMARK 470 ARG N 46 CZ NH1 NH2 REMARK 470 ASP N 71 CG OD1 OD2 REMARK 470 ARG N 78 CZ NH1 NH2 REMARK 470 GLN J 3 CD OE1 NE2 REMARK 470 ARG J 13 CG CD NE CZ NH1 NH2 REMARK 470 ARG J 43 CZ NH1 NH2 REMARK 470 GLU J 46 CD OE1 OE2 REMARK 470 LEU J 55 CG CD1 CD2 REMARK 470 ARG J 63 NE CZ NH1 NH2 REMARK 470 ARG J 87 CZ NH1 NH2 REMARK 470 TRP J 106 CE3 CZ2 CZ3 CH2 REMARK 470 SER J 126 OG 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 H 92 171.15 178.41 REMARK 500 ALA L 52 -45.77 74.73 REMARK 500 ALA M 52 -44.65 84.15 REMARK 500 ALA O 52 -40.07 76.43 REMARK 500 ALA N 52 -37.20 75.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3LEF RELATED DB: PDB REMARK 900 RELATED ID: 3LF6 RELATED DB: PDB REMARK 900 RELATED ID: 3LF9 RELATED DB: PDB REMARK 900 RELATED ID: 3LG7 RELATED DB: PDB REMARK 900 RELATED ID: 3LHP RELATED DB: PDB