HEADER IMMUNE SYSTEM 18-MAR-14 4P5M
TITLE STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP
TITLE 2 BETWEEN ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 32-214;
COMPND 5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC
COMPND 6 CLASS II DPA1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP BETA 1
COMPND 10 CHAIN;
COMPND 11 CHAIN: B, D, F, H;
COMPND 12 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W2) BETA CHAIN,
COMPND 13 MHC CLASS II ANTIGEN DPB1;
COMPND 14 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-DPA1, HLA-DP1A, HLASB;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: HLA-DPB1;
SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS CBD, AUTOIMMUNITY, BERYLLIUM, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WANG,S.DAI,J.KAPPLER
REVDAT 6 23-OCT-24 4P5M 1 REMARK
REVDAT 5 27-DEC-23 4P5M 1 HETSYN LINK
REVDAT 4 29-JUL-20 4P5M 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 14-OCT-15 4P5M 1 REMARK
REVDAT 2 14-JAN-15 4P5M 1 LINK ATOM
REVDAT 1 27-AUG-14 4P5M 0
JRNL AUTH G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,
JRNL AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,
JRNL AUTH 3 S.DAI,J.W.KAPPLER
JRNL TITL STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING
JRNL TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.
JRNL REF CELL V. 158 132 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 24995984
JRNL DOI 10.1016/J.CELL.2014.04.048
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 196507
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 10563
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8046
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 48.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 477
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12284
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 290
REMARK 3 SOLVENT ATOMS : 1660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : -0.55000
REMARK 3 B33 (A**2) : 0.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.965
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13154 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11789 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17960 ; 2.222 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27039 ; 1.046 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1528 ; 7.286 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 718 ;33.820 ;24.471
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2029 ;14.957 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;14.301 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1939 ; 0.181 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14958 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3218 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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
REMARK 4
REMARK 4 4P5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000200706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-11
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 : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 196507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M CITRATE PH6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 65.23400
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, 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: 7290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
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: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, 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: 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: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, M
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: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, N, O
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 GLN A 181
REMARK 465 GLU A 182
REMARK 465 PRO A 183
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 LEU B -10
REMARK 465 VAL B -9
REMARK 465 PRO B -8
REMARK 465 ARG B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 SER B 3
REMARK 465 GLN C 181
REMARK 465 GLU C 182
REMARK 465 PRO C 183
REMARK 465 GLY D -12
REMARK 465 SER D -11
REMARK 465 LEU D -10
REMARK 465 VAL D -9
REMARK 465 PRO D -8
REMARK 465 ARG D -7
REMARK 465 GLY D -6
REMARK 465 SER D -5
REMARK 465 GLY D -4
REMARK 465 GLY D -3
REMARK 465 GLY D -2
REMARK 465 GLY D -1
REMARK 465 SER D 3
REMARK 465 GLN E 181
REMARK 465 GLU E 182
REMARK 465 PRO E 183
REMARK 465 GLY F -12
REMARK 465 SER F -11
REMARK 465 LEU F -10
REMARK 465 VAL F -9
REMARK 465 PRO F -8
REMARK 465 ARG F -7
REMARK 465 GLY F -6
REMARK 465 SER F -5
REMARK 465 GLY F -4
REMARK 465 GLY F -3
REMARK 465 GLY F -2
REMARK 465 GLY F -1
REMARK 465 SER F 3
REMARK 465 LYS F 103
REMARK 465 LYS F 104
REMARK 465 GLY F 105
REMARK 465 PRO F 106
REMARK 465 LEU F 107
REMARK 465 GLN F 108
REMARK 465 HIS F 109
REMARK 465 HIS F 110
REMARK 465 GLN F 189
REMARK 465 GLN G 181
REMARK 465 GLU G 182
REMARK 465 PRO G 183
REMARK 465 GLY H -12
REMARK 465 SER H -11
REMARK 465 LEU H -10
REMARK 465 VAL H -9
REMARK 465 PRO H -8
REMARK 465 ARG H -7
REMARK 465 GLY H -6
REMARK 465 SER H -5
REMARK 465 GLY H -4
REMARK 465 GLY H -3
REMARK 465 GLY H -2
REMARK 465 GLY H -1
REMARK 465 LYS H 103
REMARK 465 LYS H 104
REMARK 465 GLY H 105
REMARK 465 PRO H 106
REMARK 465 LEU H 107
REMARK 465 GLN H 108
REMARK 465 HIS H 109
REMARK 465 HIS H 110
REMARK 465 GLN H 189
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 GLN B -25 CG CD OE1 NE2
REMARK 470 GLN D -25 CG CD OE1 NE2
REMARK 470 GLN F -25 CG CD OE1 NE2
REMARK 470 GLN H -25 CG CD OE1 NE2
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 C 387 O HOH C 489 1.66
REMARK 500 O HOH H 342 O HOH H 381 1.80
REMARK 500 O HOH B 381 O HOH B 456 1.89
REMARK 500 OE1 GLU F 44 O HOH F 301 1.94
REMARK 500 OD1 ASP G 85 O HOH G 368 1.94
REMARK 500 OE1 GLU E 95 OD2 ASP F 119 1.95
REMARK 500 O HOH A 362 O HOH A 473 1.99
REMARK 500 O HOH C 362 O HOH C 493 2.00
REMARK 500 O HOH D 436 O HOH D 460 2.00
REMARK 500 OD1 ASN E 118 O HOH E 482 2.04
REMARK 500 OE2 GLU F 44 NH1 ARG F 46 2.04
REMARK 500 O HOH B 492 O HOH H 513 2.05
REMARK 500 O HOH B 303 O HOH B 310 2.05
REMARK 500 O HOH C 335 O HOH C 494 2.08
REMARK 500 OE1 GLU D 185 O HOH D 444 2.08
REMARK 500 O HOH B 365 O HOH D 347 2.10
REMARK 500 OD1 ASP D -22 O HOH D 454 2.11
REMARK 500 O HOH D 471 O HOH F 442 2.11
REMARK 500 O HOH F 486 O HOH F 507 2.12
REMARK 500 OD1 ASP B -22 O HOH B 482 2.13
REMARK 500 OD1 ASN G 118 O HOH G 433 2.13
REMARK 500 NH1 ARG B 53 O HOH B 421 2.13
REMARK 500 OD1 ASN A 118 O HOH A 301 2.13
REMARK 500 O HOH G 431 O HOH G 465 2.14
REMARK 500 O HOH H 438 O HOH H 488 2.14
REMARK 500 O HOH B 360 O HOH B 423 2.15
REMARK 500 O ALA E 180 O HOH E 515 2.15
REMARK 500 O HOH E 403 O HOH E 442 2.15
REMARK 500 O LEU E 170 O HOH E 331 2.16
REMARK 500 O HOH F 301 O HOH F 320 2.16
REMARK 500 O HOH A 342 O HOH A 487 2.16
REMARK 500 O HOH C 443 O HOH C 478 2.17
REMARK 500 O HOH E 390 O HOH E 498 2.17
REMARK 500 O HOH B 366 O HOH D 438 2.17
REMARK 500 OE1 GLU H 57 O HOH H 301 2.19
REMARK 500 O HOH A 336 O HOH A 337 2.19
REMARK 500 O HOH E 386 O HOH E 520 2.19
REMARK 500 O HOH E 414 O HOH E 507 2.19
REMARK 500 O ALA H 188 O HOH H 507 2.19
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 301 O HOH G 313 2645 2.01
REMARK 500 NZ LYS A 39 OD2 ASP F 64 2545 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 40 CD GLU C 40 OE1 0.076
REMARK 500 TYR C 150 CG TYR C 150 CD1 0.087
REMARK 500 GLU E 55 CD GLU E 55 OE1 0.077
REMARK 500 GLU E 55 CD GLU E 55 OE2 0.089
REMARK 500 GLU E 95 CD GLU E 95 OE2 0.085
REMARK 500 GLU F 69 CD GLU F 69 OE2 0.070
REMARK 500 GLU F 82 CD GLU F 82 OE2 0.086
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 LEU A 60 CA - CB - CG ANGL. DEV. = -16.2 DEGREES
REMARK 500 LEU A 73 CA - CB - CG ANGL. DEV. = -17.6 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 LEU A 117 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG B 78 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 78 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP C 110 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP D 39 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP D 39 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG D 75 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 GLU E 21 OE1 - CD - OE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG F 12 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP F 39 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG G 140 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG H 12 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG H 12 NE - CZ - NH2 ANGL. DEV. = -6.0 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 ASP A 27 46.94 38.83
REMARK 500 ASN B 31 -112.30 59.19
REMARK 500 ARG B 75 -97.74 -100.17
REMARK 500 TRP B 151 31.04 71.72
REMARK 500 ASP C 27 50.13 38.02
REMARK 500 ASN D 31 -111.12 59.94
REMARK 500 ARG D 75 -95.92 -103.07
REMARK 500 TRP D 151 31.66 70.60
REMARK 500 ASN F 31 -110.45 52.37
REMARK 500 ARG F 75 -97.60 -106.02
REMARK 500 THR F 88 -70.78 -134.59
REMARK 500 ASN H 31 -109.21 53.80
REMARK 500 ARG H 75 -98.13 -108.65
REMARK 500 THR H 88 -79.79 -122.09
REMARK 500 ASP H 119 35.21 70.74
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 A 478 DISTANCE = 8.06 ANGSTROMS
REMARK 525 HOH B 472 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH C 518 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH C 525 DISTANCE = 6.33 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 313 O
REMARK 620 2 HOH A 326 O 47.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 98 OE2
REMARK 620 2 HOH C 352 O 100.1
REMARK 620 3 HOH C 474 O 56.0 152.9
REMARK 620 4 GLU H 135 OE2 107.3 113.0 88.4
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P4K RELATED DB: PDB
REMARK 900 RELATED ID: 4P4R RELATED DB: PDB
REMARK 900 RELATED ID: 4P57 RELATED DB: PDB
REMARK 900 RELATED ID: 4P5K RELATED DB: PDB
DBREF 4P5M A 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5M B -25 -14 PDB 4P5M 4P5M -25 -14
DBREF 4P5M B 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
DBREF 4P5M C 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5M D -25 -14 PDB 4P5M 4P5M -25 -14
DBREF 4P5M D 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
DBREF 4P5M E 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5M F -25 -14 PDB 4P5M 4P5M -25 -14
DBREF 4P5M F 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
DBREF 4P5M G 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5M H -25 -14 PDB 4P5M 4P5M -25 -14
DBREF 4P5M H 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
SEQADV 4P5M GLY B -13 PDB LINKER
SEQADV 4P5M GLY B -12 PDB LINKER
SEQADV 4P5M SER B -11 PDB LINKER
SEQADV 4P5M LEU B -10 PDB LINKER
SEQADV 4P5M VAL B -9 PDB LINKER
SEQADV 4P5M PRO B -8 PDB LINKER
SEQADV 4P5M ARG B -7 PDB LINKER
SEQADV 4P5M GLY B -6 PDB LINKER
SEQADV 4P5M SER B -5 PDB LINKER
SEQADV 4P5M GLY B -4 PDB LINKER
SEQADV 4P5M GLY B -3 PDB LINKER
SEQADV 4P5M GLY B -2 PDB LINKER
SEQADV 4P5M GLY B -1 PDB LINKER
SEQADV 4P5M SER B 3 UNP Q5EP54 THR 32 VARIANT
SEQADV 4P5M GLY D -13 PDB LINKER
SEQADV 4P5M GLY D -12 PDB LINKER
SEQADV 4P5M SER D -11 PDB LINKER
SEQADV 4P5M LEU D -10 PDB LINKER
SEQADV 4P5M VAL D -9 PDB LINKER
SEQADV 4P5M PRO D -8 PDB LINKER
SEQADV 4P5M ARG D -7 PDB LINKER
SEQADV 4P5M GLY D -6 PDB LINKER
SEQADV 4P5M SER D -5 PDB LINKER
SEQADV 4P5M GLY D -4 PDB LINKER
SEQADV 4P5M GLY D -3 PDB LINKER
SEQADV 4P5M GLY D -2 PDB LINKER
SEQADV 4P5M GLY D -1 PDB LINKER
SEQADV 4P5M SER D 3 UNP Q5EP54 THR 32 VARIANT
SEQADV 4P5M GLY F -13 PDB LINKER
SEQADV 4P5M GLY F -12 PDB LINKER
SEQADV 4P5M SER F -11 PDB LINKER
SEQADV 4P5M LEU F -10 PDB LINKER
SEQADV 4P5M VAL F -9 PDB LINKER
SEQADV 4P5M PRO F -8 PDB LINKER
SEQADV 4P5M ARG F -7 PDB LINKER
SEQADV 4P5M GLY F -6 PDB LINKER
SEQADV 4P5M SER F -5 PDB LINKER
SEQADV 4P5M GLY F -4 PDB LINKER
SEQADV 4P5M GLY F -3 PDB LINKER
SEQADV 4P5M GLY F -2 PDB LINKER
SEQADV 4P5M GLY F -1 PDB LINKER
SEQADV 4P5M SER F 3 UNP Q5EP54 THR 32 VARIANT
SEQADV 4P5M GLY H -13 PDB LINKER
SEQADV 4P5M GLY H -12 PDB LINKER
SEQADV 4P5M SER H -11 PDB LINKER
SEQADV 4P5M LEU H -10 PDB LINKER
SEQADV 4P5M VAL H -9 PDB LINKER
SEQADV 4P5M PRO H -8 PDB LINKER
SEQADV 4P5M ARG H -7 PDB LINKER
SEQADV 4P5M GLY H -6 PDB LINKER
SEQADV 4P5M SER H -5 PDB LINKER
SEQADV 4P5M GLY H -4 PDB LINKER
SEQADV 4P5M GLY H -3 PDB LINKER
SEQADV 4P5M GLY H -2 PDB LINKER
SEQADV 4P5M GLY H -1 PDB LINKER
SEQADV 4P5M SER H 3 UNP Q5EP54 THR 32 VARIANT
SEQRES 1 A 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 A 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 A 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 A 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 A 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 A 183 PRO
SEQRES 1 B 212 GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY
SEQRES 2 B 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 B 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 B 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 B 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 B 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 B 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 B 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 B 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 B 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 B 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 B 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 B 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 B 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 B 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 B 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 B 212 TRP LYS ALA GLN
SEQRES 1 C 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 C 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 C 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 C 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 C 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 C 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 C 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 C 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 C 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 C 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 C 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 C 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 C 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 C 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 C 183 PRO
SEQRES 1 D 212 GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY
SEQRES 2 D 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 D 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 D 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 D 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 D 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 D 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 D 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 D 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 D 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 D 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 D 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 D 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 D 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 D 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 D 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 D 212 TRP LYS ALA GLN
SEQRES 1 E 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 E 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 E 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 E 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 E 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 E 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 E 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 E 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 E 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 E 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 E 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 E 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 E 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 E 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 E 183 PRO
SEQRES 1 F 212 GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY
SEQRES 2 F 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 F 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 F 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 F 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 F 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 F 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 F 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 F 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 F 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 F 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 F 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 F 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 F 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 F 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 F 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 F 212 TRP LYS ALA GLN
SEQRES 1 G 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 G 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 G 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 G 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 G 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 G 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 G 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 G 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 G 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 G 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 G 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 G 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 G 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 G 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 G 183 PRO
SEQRES 1 H 212 GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY
SEQRES 2 H 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 H 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 H 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 H 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 H 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 H 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 H 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 H 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 H 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 H 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 H 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 H 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 H 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 H 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 H 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 H 212 TRP LYS ALA GLN
MODRES 4P5M ASN A 118 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN B 19 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN C 118 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN D 19 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN E 118 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN F 19 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN G 118 ASN GLYCOSYLATION SITE
MODRES 4P5M ASN H 19 ASN GLYCOSYLATION SITE
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG J 3 14
HET NAG J 4 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG L 3 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG M 3 14
HET BMA M 4 11
HET NAG N 1 14
HET NAG N 2 14
HET NAG O 1 14
HET BMA O 2 11
HET NAG O 3 14
HET NA A 201 1
HET NA C 201 1
HET NAG E 201 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM NA SODIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 9 NAG 19(C8 H15 N O6)
FORMUL 13 BMA 2(C6 H12 O6)
FORMUL 16 NA 2(NA 1+)
FORMUL 19 HOH *1660(H2 O)
HELIX 1 AA1 LEU A 45 PHE A 52 1 8
HELIX 2 AA2 GLU A 55 SER A 77 1 23
HELIX 3 AA3 THR B 49 LEU B 51 5 3
HELIX 4 AA4 GLY B 52 SER B 61 1 10
HELIX 5 AA5 GLN B 62 ALA B 71 1 10
HELIX 6 AA6 ARG B 75 GLY B 84 1 10
HELIX 7 AA7 GLY B 84 GLN B 90 1 7
HELIX 8 AA8 LYS B 104 HIS B 109 1 6
HELIX 9 AA9 LEU C 45 PHE C 52 1 8
HELIX 10 AB1 GLU C 55 SER C 77 1 23
HELIX 11 AB2 THR D 49 LEU D 51 5 3
HELIX 12 AB3 GLY D 52 SER D 61 1 10
HELIX 13 AB4 GLN D 62 ALA D 71 1 10
HELIX 14 AB5 ARG D 75 GLY D 84 1 10
HELIX 15 AB6 GLY D 84 GLN D 90 1 7
HELIX 16 AB7 LYS D 104 HIS D 109 1 6
HELIX 17 AB8 LEU E 45 PHE E 52 1 8
HELIX 18 AB9 GLU E 55 SER E 77 1 23
HELIX 19 AC1 THR F 49 LEU F 51 5 3
HELIX 20 AC2 GLY F 52 SER F 61 1 10
HELIX 21 AC3 GLN F 62 ALA F 71 1 10
HELIX 22 AC4 ARG F 75 GLY F 85 1 11
HELIX 23 AC5 PRO F 86 THR F 88 5 3
HELIX 24 AC6 LEU G 45 PHE G 52 1 8
HELIX 25 AC7 GLU G 55 SER G 77 1 23
HELIX 26 AC8 THR H 49 LEU H 51 5 3
HELIX 27 AC9 GLY H 52 SER H 61 1 10
HELIX 28 AD1 GLN H 62 ALA H 71 1 10
HELIX 29 AD2 ARG H 75 GLY H 85 1 11
HELIX 30 AD3 PRO H 86 THR H 88 5 3
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N ASP A 35 O GLU A 40
SHEET 3 AA1 8 GLY A 20 PHE A 26 -1 N PHE A 24 O MET A 31
SHEET 4 AA1 8 HIS A 5 GLN A 14 -1 N THR A 8 O GLU A 25
SHEET 5 AA1 8 LEU B 8 PHE B 18 -1 O CYS B 15 N SER A 7
SHEET 6 AA1 8 THR B 21 TYR B 30 -1 O LEU B 25 N GLU B 14
SHEET 7 AA1 8 GLU B 33 ASP B 39 -1 O GLU B 33 N TYR B 30
SHEET 8 AA1 8 PHE B 45 ALA B 47 -1 O ARG B 46 N ARG B 37
SHEET 1 AA2 4 GLU A 88 PRO A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O HIS A 149 N CYS A 107
SHEET 4 AA2 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 PRO A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O HIS A 149 N CYS A 107
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 AA4 4 GLU A 126 VAL A 128 0
SHEET 2 AA4 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 AA4 4 PHE A 160 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 GLU A 179 -1 O LEU A 174 N VAL A 165
SHEET 1 AA5 4 ARG B 96 PRO B 101 0
SHEET 2 AA5 4 LEU B 112 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 AA5 4 PHE B 153 GLU B 160 -1 O VAL B 157 N CYS B 115
SHEET 4 AA5 4 VAL B 140 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 AA6 4 ARG B 96 PRO B 101 0
SHEET 2 AA6 4 LEU B 112 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 AA6 4 PHE B 153 GLU B 160 -1 O VAL B 157 N CYS B 115
SHEET 4 AA6 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 AA7 4 GLN B 134 GLU B 136 0
SHEET 2 AA7 4 GLN B 126 LEU B 131 -1 N TRP B 129 O GLU B 136
SHEET 3 AA7 4 VAL B 168 GLU B 174 -1 O GLN B 172 N ARG B 128
SHEET 4 AA7 4 VAL B 182 LYS B 187 -1 O TRP B 186 N TYR B 169
SHEET 1 AA8 8 GLU C 40 TRP C 43 0
SHEET 2 AA8 8 ASP C 29 ASP C 35 -1 N TYR C 33 O VAL C 42
SHEET 3 AA8 8 GLY C 20 PHE C 26 -1 N PHE C 24 O PHE C 32
SHEET 4 AA8 8 HIS C 5 GLN C 14 -1 N THR C 8 O GLU C 25
SHEET 5 AA8 8 LEU D 8 PHE D 18 -1 O CYS D 15 N SER C 7
SHEET 6 AA8 8 THR D 21 TYR D 30 -1 O LEU D 25 N GLU D 14
SHEET 7 AA8 8 GLU D 33 ASP D 39 -1 O GLU D 33 N TYR D 30
SHEET 8 AA8 8 PHE D 45 ALA D 47 -1 O ARG D 46 N ARG D 37
SHEET 1 AA9 4 GLU C 88 PRO C 93 0
SHEET 2 AA9 4 ASN C 103 PHE C 112 -1 O HIS C 108 N THR C 90
SHEET 3 AA9 4 PHE C 145 PHE C 153 -1 O HIS C 149 N CYS C 107
SHEET 4 AA9 4 VAL C 132 GLU C 134 -1 N ALA C 133 O TYR C 150
SHEET 1 AB1 4 GLU C 88 PRO C 93 0
SHEET 2 AB1 4 ASN C 103 PHE C 112 -1 O HIS C 108 N THR C 90
SHEET 3 AB1 4 PHE C 145 PHE C 153 -1 O HIS C 149 N CYS C 107
SHEET 4 AB1 4 LEU C 138 PRO C 139 -1 N LEU C 138 O HIS C 146
SHEET 1 AB2 4 GLU C 126 VAL C 128 0
SHEET 2 AB2 4 ASN C 118 CYS C 123 -1 N TRP C 121 O VAL C 128
SHEET 3 AB2 4 PHE C 160 GLU C 166 -1 O ARG C 164 N THR C 120
SHEET 4 AB2 4 LEU C 174 GLU C 179 -1 O TRP C 178 N TYR C 161
SHEET 1 AB3 4 ARG D 96 PRO D 101 0
SHEET 2 AB3 4 LEU D 112 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 AB3 4 PHE D 153 GLU D 160 -1 O ILE D 155 N VAL D 117
SHEET 4 AB3 4 VAL D 140 SER D 142 -1 N VAL D 141 O MET D 158
SHEET 1 AB4 4 ARG D 96 PRO D 101 0
SHEET 2 AB4 4 LEU D 112 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 AB4 4 PHE D 153 GLU D 160 -1 O ILE D 155 N VAL D 117
SHEET 4 AB4 4 ILE D 146 ARG D 147 -1 N ILE D 146 O GLN D 154
SHEET 1 AB5 4 GLN D 134 GLU D 136 0
SHEET 2 AB5 4 GLN D 126 LEU D 131 -1 N TRP D 129 O GLU D 136
SHEET 3 AB5 4 VAL D 168 GLU D 174 -1 O GLN D 172 N ARG D 128
SHEET 4 AB5 4 VAL D 182 LYS D 187 -1 O VAL D 182 N VAL D 173
SHEET 1 AB6 8 GLU E 40 TRP E 43 0
SHEET 2 AB6 8 ASP E 29 ASP E 35 -1 N TYR E 33 O VAL E 42
SHEET 3 AB6 8 GLY E 20 PHE E 26 -1 N PHE E 24 O MET E 31
SHEET 4 AB6 8 HIS E 5 GLN E 14 -1 N THR E 8 O GLU E 25
SHEET 5 AB6 8 LEU F 8 PHE F 18 -1 O CYS F 15 N SER E 7
SHEET 6 AB6 8 THR F 21 TYR F 30 -1 O LEU F 25 N GLU F 14
SHEET 7 AB6 8 GLU F 33 ASP F 39 -1 O GLU F 33 N TYR F 30
SHEET 8 AB6 8 PHE F 45 ALA F 47 -1 O ARG F 46 N ARG F 37
SHEET 1 AB7 4 GLU E 88 PRO E 93 0
SHEET 2 AB7 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 AB7 4 PHE E 145 PHE E 153 -1 O LYS E 147 N ILE E 109
SHEET 4 AB7 4 VAL E 132 GLU E 134 -1 N ALA E 133 O TYR E 150
SHEET 1 AB8 4 GLU E 88 PRO E 93 0
SHEET 2 AB8 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 AB8 4 PHE E 145 PHE E 153 -1 O LYS E 147 N ILE E 109
SHEET 4 AB8 4 LEU E 138 PRO E 139 -1 N LEU E 138 O HIS E 146
SHEET 1 AB9 4 GLU E 126 VAL E 128 0
SHEET 2 AB9 4 ASN E 118 CYS E 123 -1 N CYS E 123 O GLU E 126
SHEET 3 AB9 4 PHE E 160 GLU E 166 -1 O GLU E 166 N ASN E 118
SHEET 4 AB9 4 LEU E 174 GLU E 179 -1 O TRP E 178 N TYR E 161
SHEET 1 AC1 4 ARG F 96 PRO F 101 0
SHEET 2 AC1 4 LEU F 112 PHE F 120 -1 O HIS F 116 N ASN F 98
SHEET 3 AC1 4 PHE F 153 GLU F 160 -1 O VAL F 157 N CYS F 115
SHEET 4 AC1 4 VAL F 140 SER F 142 -1 N VAL F 141 O MET F 158
SHEET 1 AC2 4 ARG F 96 PRO F 101 0
SHEET 2 AC2 4 LEU F 112 PHE F 120 -1 O HIS F 116 N ASN F 98
SHEET 3 AC2 4 PHE F 153 GLU F 160 -1 O VAL F 157 N CYS F 115
SHEET 4 AC2 4 ILE F 146 ARG F 147 -1 N ILE F 146 O GLN F 154
SHEET 1 AC3 4 GLN F 134 GLU F 136 0
SHEET 2 AC3 4 GLN F 126 LEU F 131 -1 N LEU F 131 O GLN F 134
SHEET 3 AC3 4 VAL F 168 GLU F 174 -1 O GLN F 172 N ARG F 128
SHEET 4 AC3 4 VAL F 182 LYS F 187 -1 O VAL F 182 N VAL F 173
SHEET 1 AC4 8 GLU G 40 TRP G 43 0
SHEET 2 AC4 8 ASP G 29 ASP G 35 -1 N TYR G 33 O VAL G 42
SHEET 3 AC4 8 GLY G 20 PHE G 26 -1 N PHE G 24 O MET G 31
SHEET 4 AC4 8 HIS G 5 GLN G 14 -1 N THR G 8 O GLU G 25
SHEET 5 AC4 8 LEU H 8 PHE H 18 -1 O CYS H 15 N SER G 7
SHEET 6 AC4 8 THR H 21 TYR H 30 -1 O LEU H 25 N GLU H 14
SHEET 7 AC4 8 GLU H 33 ASP H 39 -1 O GLU H 33 N TYR H 30
SHEET 8 AC4 8 PHE H 45 ALA H 47 -1 O ARG H 46 N ARG H 37
SHEET 1 AC5 4 GLU G 88 PRO G 93 0
SHEET 2 AC5 4 ASN G 103 PHE G 112 -1 O ASP G 110 N GLU G 88
SHEET 3 AC5 4 PHE G 145 PHE G 153 -1 O LEU G 151 N LEU G 105
SHEET 4 AC5 4 VAL G 132 GLU G 134 -1 N ALA G 133 O TYR G 150
SHEET 1 AC6 4 GLU G 88 PRO G 93 0
SHEET 2 AC6 4 ASN G 103 PHE G 112 -1 O ASP G 110 N GLU G 88
SHEET 3 AC6 4 PHE G 145 PHE G 153 -1 O LEU G 151 N LEU G 105
SHEET 4 AC6 4 LEU G 138 PRO G 139 -1 N LEU G 138 O HIS G 146
SHEET 1 AC7 4 GLU G 126 LEU G 127 0
SHEET 2 AC7 4 ASN G 118 CYS G 123 -1 N CYS G 123 O GLU G 126
SHEET 3 AC7 4 PHE G 160 GLU G 166 -1 O GLU G 166 N ASN G 118
SHEET 4 AC7 4 LEU G 174 GLU G 179 -1 O LEU G 174 N VAL G 165
SHEET 1 AC8 4 ARG H 96 PRO H 101 0
SHEET 2 AC8 4 LEU H 112 PHE H 120 -1 O HIS H 116 N ASN H 98
SHEET 3 AC8 4 PHE H 153 GLU H 160 -1 O VAL H 157 N CYS H 115
SHEET 4 AC8 4 VAL H 140 SER H 142 -1 N VAL H 141 O MET H 158
SHEET 1 AC9 4 ARG H 96 PRO H 101 0
SHEET 2 AC9 4 LEU H 112 PHE H 120 -1 O HIS H 116 N ASN H 98
SHEET 3 AC9 4 PHE H 153 GLU H 160 -1 O VAL H 157 N CYS H 115
SHEET 4 AC9 4 ILE H 146 ARG H 147 -1 N ILE H 146 O GLN H 154
SHEET 1 AD1 4 GLN H 134 GLU H 136 0
SHEET 2 AD1 4 GLN H 126 LEU H 131 -1 N TRP H 129 O GLU H 136
SHEET 3 AD1 4 VAL H 168 GLU H 174 -1 O GLN H 172 N ARG H 128
SHEET 4 AD1 4 VAL H 182 LYS H 187 -1 O TRP H 186 N TYR H 169
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.13
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.15
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.00
SSBOND 4 CYS C 107 CYS C 163 1555 1555 2.10
SSBOND 5 CYS D 15 CYS D 77 1555 1555 2.15
SSBOND 6 CYS D 115 CYS D 171 1555 1555 2.15
SSBOND 7 CYS E 107 CYS E 163 1555 1555 2.15
SSBOND 8 CYS F 15 CYS F 77 1555 1555 2.12
SSBOND 9 CYS F 115 CYS F 171 1555 1555 2.06
SSBOND 10 CYS G 107 CYS G 163 1555 1555 2.20
SSBOND 11 CYS H 15 CYS H 77 1555 1555 2.11
SSBOND 12 CYS H 115 CYS H 171 1555 1555 2.04
LINK ND2 ASN A 118 C1 NAG I 1 1555 1555 1.47
LINK ND2 ASN B 19 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN C 118 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN D 19 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN E 118 C1 NAG E 201 1555 1555 1.46
LINK ND2 ASN F 19 C1 NAG M 1 1555 1555 1.45
LINK ND2 ASN G 118 C1 NAG N 1 1555 1555 1.46
LINK ND2 ASN H 19 C1 NAG O 1 1555 1555 1.43
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.46
LINK O3 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 3 1555 1555 1.47
LINK O6 NAG J 1 C1 NAG J 4 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.47
LINK O3 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 3 1555 1555 1.47
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.43
LINK O3 NAG M 1 C1 BMA M 4 1555 1555 1.45
LINK O4 NAG M 2 C1 NAG M 3 1555 1555 1.46
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O3 NAG O 1 C1 BMA O 2 1555 1555 1.36
LINK O4 NAG O 1 C1 NAG O 3 1555 1555 1.45
LINK NA NA A 201 O HOH A 313 1555 1555 3.08
LINK NA NA A 201 O HOH A 326 1555 1555 2.60
LINK OE2AGLU C 98 NA NA C 201 1555 1555 3.13
LINK NA NA C 201 O HOH C 352 1555 1555 2.78
LINK NA NA C 201 O HOH C 474 1555 1555 3.04
LINK NA NA C 201 OE2 GLU H 135 1555 1555 2.79
CISPEP 1 ARG A 17 PRO A 18 0 -2.98
CISPEP 2 PHE A 113 PRO A 114 0 6.29
CISPEP 3 TYR B 121 PRO B 122 0 0.31
CISPEP 4 ARG C 17 PRO C 18 0 6.14
CISPEP 5 PHE C 113 PRO C 114 0 3.81
CISPEP 6 TYR D 121 PRO D 122 0 2.82
CISPEP 7 ARG E 17 PRO E 18 0 -5.40
CISPEP 8 PHE E 113 PRO E 114 0 1.17
CISPEP 9 TYR F 121 PRO F 122 0 -2.51
CISPEP 10 ARG G 17 PRO G 18 0 1.36
CISPEP 11 PHE G 113 PRO G 114 0 6.15
CISPEP 12 TYR H 121 PRO H 122 0 -3.46
CRYST1 81.631 130.468 107.994 90.00 107.16 90.00 P 1 21 1 8
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 0.012250 0.000000 0.003782 0.00000
SCALE2 0.000000 0.007665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
