HEADER IMMUNE SYSTEM 18-NOV-15 5EU5
TITLE HLA CLASS I ANTIGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PEPTIDE ANTIGEN YLEPAPVTA;
COMPND 12 CHAIN: C;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 32630;
SOURCE 19 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 32630
KEYWDS IMMUNO, HLA-A02, 1E6-TCR, CROSS-REACTIVITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.RIZKALLAH,V.BIANCHI,D.K.COLE,A.K.SEWELL
REVDAT 4 10-JAN-24 5EU5 1 REMARK
REVDAT 3 11-MAY-16 5EU5 1 JRNL
REVDAT 2 09-MAR-16 5EU5 1 JRNL
REVDAT 1 02-MAR-16 5EU5 0
JRNL AUTH V.BIANCHI,A.BULEK,A.FULLER,A.LLOYD,M.ATTAF,P.J.RIZKALLAH,
JRNL AUTH 2 G.DOLTON,A.K.SEWELL,D.K.COLE
JRNL TITL A MOLECULAR SWITCH ABROGATES GLYCOPROTEIN 100 (GP100) T-CELL
JRNL TITL 2 RECEPTOR (TCR) TARGETING OF A HUMAN MELANOMA ANTIGEN.
JRNL REF J.BIOL.CHEM. V. 291 8951 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26917722
JRNL DOI 10.1074/JBC.M115.707414
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 63875
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3406
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) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4715
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3159
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 0.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.130
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3501 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3183 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4719 ; 1.914 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7320 ; 1.080 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 405 ; 6.609 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;31.468 ;23.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 549 ;13.199 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;20.325 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 483 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3881 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 854 ; 0.002 ; 0.020
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): 1590 ; 0.895 ; 1.007
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1589 ; 0.895 ; 1.007
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1999 ; 1.503 ; 1.503
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 3
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 : A 1 A 180
REMARK 3 RESIDUE RANGE : C 1 C 9
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0808 -9.9476 27.5832
REMARK 3 T TENSOR
REMARK 3 T11: 0.0106 T22: 0.0062
REMARK 3 T33: 0.0191 T12: -0.0024
REMARK 3 T13: 0.0116 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.0280 L22: 1.8153
REMARK 3 L33: 0.9348 L12: 0.1505
REMARK 3 L13: -0.0216 L23: 0.4581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.0447 S13: 0.0883
REMARK 3 S21: 0.1354 S22: -0.0144 S23: 0.1377
REMARK 3 S31: 0.0381 S32: -0.0598 S33: -0.0183
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 : A 181 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6544 16.5311 5.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0379 T22: 0.0465
REMARK 3 T33: 0.0208 T12: 0.0202
REMARK 3 T13: 0.0079 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.2931 L22: 1.0121
REMARK 3 L33: 5.3418 L12: -0.1040
REMARK 3 L13: 0.1248 L23: -1.6840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0536 S12: 0.0903 S13: 0.0534
REMARK 3 S21: -0.0403 S22: -0.0182 S23: 0.0175
REMARK 3 S31: -0.1877 S32: -0.0840 S33: -0.0354
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 : B 0 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2260 -2.8147 12.9519
REMARK 3 T TENSOR
REMARK 3 T11: 0.0331 T22: 0.0432
REMARK 3 T33: 0.0582 T12: -0.0003
REMARK 3 T13: 0.0376 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 3.7059 L22: 3.7066
REMARK 3 L33: 1.1513 L12: 2.4413
REMARK 3 L13: 0.0231 L23: 0.4600
REMARK 3 S TENSOR
REMARK 3 S11: -0.1448 S12: 0.1542 S13: -0.3115
REMARK 3 S21: -0.3009 S22: 0.1982 S23: -0.4641
REMARK 3 S31: 0.0333 S32: 0.1670 S33: -0.0533
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5EU5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67308
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 43.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.58200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.5
REMARK 200 STARTING MODEL: 4I4W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.2 M AMMONIUM
REMARK 280 SULPHATE, 25 % PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
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 39.82000
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 O1 GOL A 316 O2 GOL A 320 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 409 O HOH A 526 2745 2.06
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 17 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 37 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = -3.0 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 ARG A 17 134.35 -174.29
REMARK 500 ASP A 29 -128.43 52.96
REMARK 500 HIS A 114 111.06 -161.90
REMARK 500 TYR A 123 -70.03 -114.79
REMARK 500 GLN B 2 128.30 84.95
REMARK 500 GLN B 2 126.28 84.95
REMARK 500 TRP B 60 -5.60 78.73
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 102
DBREF 5EU5 A 1 276 UNP P01892 1A02_HUMAN 25 300
DBREF 5EU5 B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5EU5 C 1 9 PDB 5EU5 5EU5 1 9
SEQADV 5EU5 MET B 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 276 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 276 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 276 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 276 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 276 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 276 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 276 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 276 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 276 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 276 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 276 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 276 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 276 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 276 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 9 TYR LEU GLU PRO ALA PRO VAL THR ALA
HET EDO A 301 4
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HET EDO A 308 4
HET EDO A 309 4
HET EDO A 310 4
HET GOL A 311 6
HET GOL A 312 6
HET GOL A 313 6
HET GOL A 314 6
HET GOL A 315 6
HET GOL A 316 6
HET GOL A 317 6
HET GOL A 318 6
HET GOL A 319 6
HET GOL A 320 6
HET SO4 A 321 5
HET SO4 A 322 5
HET SO4 A 323 5
HET SO4 A 324 5
HET SO4 A 325 5
HET EDO B 101 4
HET EDO B 102 4
HET EDO B 103 4
HET EDO B 104 4
HET EDO B 105 4
HET EDO B 106 4
HET SO4 B 107 5
HET SO4 B 108 5
HET SO4 B 109 5
HET EDO C 101 4
HET EDO C 102 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 EDO 18(C2 H6 O2)
FORMUL 14 GOL 10(C3 H8 O3)
FORMUL 24 SO4 8(O4 S 2-)
FORMUL 40 HOH *206(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 53 5 5
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 ALA A 150 1 14
HELIX 4 AA4 HIS A 151 GLY A 162 1 12
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 GLY A 175 GLN A 180 1 6
HELIX 7 AA7 GLN A 253 GLN A 255 5 3
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N ALA A 24 O PHE A 36
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O TYR A 99 N TYR A 7
SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O GLN A 115 N MET A 98
SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114
SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA2 4 LYS A 186 ALA A 193 0
SHEET 2 AA2 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA2 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 AA3 4 LYS A 186 ALA A 193 0
SHEET 2 AA3 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AA4 4 GLU A 222 GLN A 224 0
SHEET 2 AA4 4 THR A 214 ARG A 219 -1 N TRP A 217 O GLN A 224
SHEET 3 AA4 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 4 AA4 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 AA5 4 LYS B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.06
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.09
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.00
CISPEP 1 TYR A 209 PRO A 210 0 5.16
CISPEP 2 HIS B 31 PRO B 32 0 -2.28
SITE 1 AC1 5 GLU A 19 PRO A 20 SER A 71 ARG A 75
SITE 2 AC1 5 HOH A 467
SITE 1 AC2 2 GLN A 43 LYS A 68
SITE 1 AC3 6 PHE A 36 SER A 38 GLN A 43 SER A 71
SITE 2 AC3 6 GLN A 72 HOH A 441
SITE 1 AC4 8 ARG A 131 TRP A 133 GLU A 148 HIS A 151
SITE 2 AC4 8 ALA A 153 GLU A 154 HOH A 402 HOH A 468
SITE 1 AC5 3 ARG A 181 LYS A 186 SER A 207
SITE 1 AC6 5 TYR A 85 TYR A 118 LYS A 121 HOH A 403
SITE 2 AC6 5 HOH A 443
SITE 1 AC7 4 ARG A 6 PHE A 8 ASP A 29 HOH A 438
SITE 1 AC8 3 ALA A 184 PRO A 185 HOH A 459
SITE 1 AC9 1 ARG A 273
SITE 1 AD1 4 GLY A 1 HIS A 3 TRP A 107 GLN A 180
SITE 1 AD2 3 HIS A 192 THR A 200 ARG A 202
SITE 1 AD3 7 PRO A 235 ALA A 236 GLY A 237 ASP A 238
SITE 2 AD3 7 GLY A 239 THR A 240 LEU B 65
SITE 1 AD4 5 VAL A 12 ARG A 14 ARG A 21 ASP B 34
SITE 2 AD4 5 EDO B 106
SITE 1 AD5 6 PRO A 20 ARG A 75 GLY A 79 ARG A 82
SITE 2 AD5 6 HOH A 407 HOH A 424
SITE 1 AD6 4 THR A 187 HIS A 188 MET A 189 HOH A 547
SITE 1 AD7 6 LYS A 186 LEU A 206 SER A 207 GOL A 320
SITE 2 AD7 6 HIS B 13 PRO B 14
SITE 1 AD8 3 ALA A 41 SER A 42 HOH A 417
SITE 1 AD9 6 TYR A 116 ASP A 122 TYR A 123 ILE A 124
SITE 2 AD9 6 ALA A 125 THR A 134
SITE 1 AE1 6 ARG A 108 PHE A 109 GLU A 161 VAL A 165
SITE 2 AE1 6 ARG A 169 HOH A 433
SITE 1 AE2 10 LEU A 206 SER A 207 ALA A 236 ASP A 238
SITE 2 AE2 10 THR A 240 PHE A 241 GLN A 242 GOL A 316
SITE 3 AE2 10 ARG B 12 HIS B 13
SITE 1 AE3 4 ARG A 14 PRO A 15 GLY A 16 ARG A 17
SITE 1 AE4 3 GLN A 87 SER A 88 HOH A 444
SITE 1 AE5 1 ARG A 21
SITE 1 AE6 3 SER A 2 LEU A 110 ARG A 111
SITE 1 AE7 5 PRO A 47 ARG A 48 ALA A 49 PRO A 50
SITE 2 AE7 5 GLU A 53
SITE 1 AE8 7 GLN B 8 VAL B 9 VAL B 93 LYS B 94
SITE 2 AE8 7 ASP B 96 MET B 99 HOH B 220
SITE 1 AE9 8 LEU A 206 ARG A 234 GLN A 242 SER B 11
SITE 2 AE9 8 HIS B 13 PRO B 14 SO4 B 107 HOH B 241
SITE 1 AF1 3 ASP A 238 ARG B 12 HIS B 13
SITE 1 AF2 4 GLN A 115 SER B 57 LYS B 58 TRP B 60
SITE 1 AF3 7 LEU B 40 LYS B 41 ASN B 42 GLY B 43
SITE 2 AF3 7 GLU B 77 ALA B 79 LYS B 94
SITE 1 AF4 4 GOL A 313 SER B 33 ASP B 34 HOH B 213
SITE 1 AF5 7 HIS A 188 TRP A 204 PRO B 14 ARG B 97
SITE 2 AF5 7 ASP B 98 EDO B 102 HOH B 212
SITE 1 AF6 6 ILE B 35 GLU B 36 ASN B 83 HIS B 84
SITE 2 AF6 6 VAL B 85 HOH B 209
SITE 1 AF7 4 SER B 20 GLU B 69 PHE B 70 THR B 71
SITE 1 AF8 6 ARG A 97 TRP A 147 GLU C 3 PRO C 6
SITE 2 AF8 6 VAL C 7 EDO C 102
SITE 1 AF9 6 GLN A 155 LEU A 156 GLU C 3 ALA C 5
SITE 2 AF9 6 VAL C 7 EDO C 101
CRYST1 56.330 79.640 57.740 90.00 116.22 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017753 0.000000 0.008743 0.00000
SCALE2 0.000000 0.012557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
