REMARK 2 REMARK 2 RESOLUTION. 1.92 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1553 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1552 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.2017 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.0 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4240 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 143072 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1500 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.1499 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.1960 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.0 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 4062 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 136255 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12878 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 540 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 13417.00 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 53672 REMARK 3 NUMBER OF RESTRAINTS : 100475 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 ANGLE DISTANCES (A) : 0.023 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.064 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.0287 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.035 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.042 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.015 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.044 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2V7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-07. REMARK 100 THE PDBE ID CODE IS EBI-33215. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-OCT-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 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) : 1.00000 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : BENT MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151552 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90 REMARK 200 RESOLUTION RANGE LOW (A) : 31.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 4.9 REMARK 200 R MERGE (I) : 0.12 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.20 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.9 REMARK 200 R MERGE FOR SHELL (I) : 0.37 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.50 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER1.3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.6 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG4000, 50 MM LI2SO4, 50 MM REMARK 280 NA2SO4, 50 MM N-(2ACETAMIDO) IMINODIACETIC ACID (ADA), PH REMARK 280 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 51.39500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.96000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.39500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 92.96000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: 3100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.4 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: 3040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.2 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 350 REMARK 350 BIOMOLECULE: 3 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: 3100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350 REMARK 350 BIOMOLECULE: 4 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: 3060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 GLU A 254 REMARK 465 ALA A 255 REMARK 465 GLN B 1 REMARK 465 LYS B 165 REMARK 465 SER B 166 REMARK 465 THR B 167 REMARK 465 SER B 168 REMARK 465 LYS B 250 REMARK 465 SER B 251 REMARK 465 GLU B 252 REMARK 465 PHE B 253 REMARK 465 HIS B 254 REMARK 465 HIS B 255 REMARK 465 HIS B 256 REMARK 465 HIS B 257 REMARK 465 HIS B 258 REMARK 465 HIS B 259 REMARK 465 GLY C 253 REMARK 465 GLU C 254 REMARK 465 ALA C 255 REMARK 465 SER D 163 REMARK 465 SER D 164 REMARK 465 LYS D 165 REMARK 465 SER D 166 REMARK 465 THR D 167 REMARK 465 SER D 168 REMARK 465 LYS D 250 REMARK 465 SER D 251 REMARK 465 GLU D 252 REMARK 465 PHE D 253 REMARK 465 HIS D 254 REMARK 465 HIS D 255 REMARK 465 HIS D 256 REMARK 465 HIS D 257 REMARK 465 HIS D 258 REMARK 465 HIS D 259 REMARK 465 GLU E 254 REMARK 465 ALA E 255 REMARK 465 GLN F 1 REMARK 465 SER F 163 REMARK 465 SER F 164 REMARK 465 LYS F 165 REMARK 465 SER F 166 REMARK 465 THR F 167 REMARK 465 SER F 168 REMARK 465 LYS F 250 REMARK 465 SER F 251 REMARK 465 GLU F 252 REMARK 465 PHE F 253 REMARK 465 HIS F 254 REMARK 465 HIS F 255 REMARK 465 HIS F 256 REMARK 465 HIS F 257 REMARK 465 HIS F 258 REMARK 465 HIS F 259 REMARK 465 GLY G 253 REMARK 465 GLU G 254 REMARK 465 ALA G 255 REMARK 465 GLN H 1 REMARK 465 SER H 163 REMARK 465 SER H 164 REMARK 465 LYS H 165 REMARK 465 SER H 166 REMARK 465 THR H 167 REMARK 465 SER H 168 REMARK 465 GLY H 169 REMARK 465 LYS H 250 REMARK 465 SER H 251 REMARK 465 GLU H 252 REMARK 465 PHE H 253 REMARK 465 HIS H 254 REMARK 465 HIS H 255 REMARK 465 HIS H 256 REMARK 465 HIS H 257 REMARK 465 HIS H 258 REMARK 465 HIS H 259 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 ASP C 111 N ILE C 135 2.19 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 A 252 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 TYR B 70 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ASP B 83 CB - CG - OD1 ANGL. DEV. = -7.3 DEGREES REMARK 500 ASP B 83 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES REMARK 500 ARG C 183 CD - NE - CZ ANGL. DEV. = 20.3 DEGREES REMARK 500 ARG C 183 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG C 183 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ASP D 83 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES REMARK 500 LEU D 214 CA - CB - CG ANGL. DEV. = 15.1 DEGREES REMARK 500 ARG E 183 CD - NE - CZ ANGL. DEV. = 11.9 DEGREES REMARK 500 ARG E 183 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG E 252 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES REMARK 500 TYR F 60 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 LEU F 214 CA - CB - CG ANGL. DEV. = 22.1 DEGREES REMARK 500 ARG G 183 CD - NE - CZ ANGL. DEV. = 11.2 DEGREES REMARK 500 ARG G 183 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG G 183 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 LEU H 144 CB - CG - CD2 ANGL. DEV. = 11.1 DEGREES REMARK 500 LEU H 214 CA - CB - CG ANGL. DEV. = 18.1 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 SER A 33 13.88 59.71 REMARK 500 TYR A 40 71.92 -69.03 REMARK 500 SER A 67 -38.98 69.00 REMARK 500 ASN A 179 72.17 35.68 REMARK 500 ASN B 67 87.70 -151.52 REMARK 500 ALA B 135 -131.44 49.32 REMARK 500 PRO B 238 -18.20 -49.96 REMARK 500 SER C 33 14.79 59.93 REMARK 500 SER C 67 -35.66 74.99 REMARK 500 SER C 68 -1.55 -147.75 REMARK 500 ALA C 102 -174.62 -171.89 REMARK 500 ASN C 179 71.53 49.00 REMARK 500 GLN D 3 144.91 -171.41 REMARK 500 ASN D 67 73.67 54.71 REMARK 500 ALA D 135 -136.82 52.36 REMARK 500 PHE D 182 136.85 -170.74 REMARK 500 THR D 196 -31.40 -130.02 REMARK 500 THR D 227 -57.53 -121.95 REMARK 500 SER E 33 17.66 57.62 REMARK 500 SER E 67 -35.65 72.25 REMARK 500 ASP E 111 -158.01 -152.16 REMARK 500 ASN E 179 74.95 38.35 REMARK 500 SER F 66 -179.83 -61.01 REMARK 500 ASN F 67 65.20 38.65 REMARK 500 ALA F 135 -137.39 46.84 REMARK 500 PHE F 182 137.48 -171.56 REMARK 500 SER F 192 17.93 58.87 REMARK 500 PRO F 238 -19.62 -47.20 REMARK 500 SER G 67 -40.40 68.27 REMARK 500 ASN G 179 76.99 41.53 REMARK 500 ASN H 67 68.44 39.40 REMARK 500 ALA H 135 -136.72 50.06 REMARK 500 PHE H 182 140.41 -175.55 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 999 REMARK 999 SEQUENCE REMARK 999 C-TERMINAL HISTIDINE TAG AT HEAVY CHAIN