HEADER TRANSPORT PROTEIN 22-DEC-10 3Q41
TITLE CRYSTAL STRUCTURE OF THE GLUN1 N-TERMINAL DOMAIN (NTD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE [NMDA] RECEPTOR SUBUNIT ZETA-1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, UNP RESIDUES 21-393;
COMPND 5 SYNONYM: N-METHYL-D-ASPARTATE RECEPTOR SUBUNIT NR1, NMD-R1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 STRAIN: E;
SOURCE 6 GENE: GRIN1, NMDAR1;
SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: GNTI(-) HEK CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: IRES-MCHERRY
KEYWDS NTD, NMDA, GLUN1, ION CHANNEL, GLYCOSYLATION, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.N.FARINA,K.Y.BLAIN,T.MARUO,W.KWIATKOWSKI,S.CHOE,T.NAKAGAWA
REVDAT 2 29-JUL-20 3Q41 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 23-MAR-11 3Q41 0
JRNL AUTH A.N.FARINA,K.Y.BLAIN,T.MARUO,W.KWIATKOWSKI,S.CHOE,T.NAKAGAWA
JRNL TITL SEPARATION OF DOMAIN CONTACTS IS REQUIRED FOR
JRNL TITL 2 HETEROTETRAMERIC ASSEMBLY OF FUNCTIONAL NMDA RECEPTORS.
JRNL REF J.NEUROSCI. V. 31 3565 2011
JRNL REFN ISSN 0270-6474
JRNL PMID 21389213
JRNL DOI 10.1523/JNEUROSCI.6041-10.2011
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 30371
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1617
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2200
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8725
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 218
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : 0.27000
REMARK 3 B12 (A**2) : -0.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.526
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.403
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.524
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.857
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9141 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12414 ; 1.269 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1106 ; 6.144 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 406 ;37.409 ;23.818
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1535 ;20.175 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;16.282 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1415 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6881 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 5522 ; 0.335 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8946 ; 0.630 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3619 ; 0.615 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3468 ; 1.127 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 24 A 394 6
REMARK 3 1 B 24 B 394 6
REMARK 3 1 C 24 C 394 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 2887 ; 0.68 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2887 ; 0.83 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 2887 ; 0.76 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2887 ; 3.21 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2887 ; 1.68 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 2887 ; 3.14 ; 10.00
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 : 1.40
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 3Q41 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063166.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : RIGAKU VARIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32023
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 142.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.63000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD,SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN IN (20MM TRIS-HCL PH 7.5,
REMARK 280 150MM NACL) WAS MIXED 1:1 WITH 4M FORMATE AND 20MM TCEP,
REMARK 280 TEMPERATURE 277K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.08600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 98.17200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 98.17200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.08600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ALA A 21
REMARK 465 CYS A 22
REMARK 465 ASP A 23
REMARK 465 ASP A 395
REMARK 465 GLY A 396
REMARK 465 GLY A 397
REMARK 465 GLY A 398
REMARK 465 GLY A 399
REMARK 465 GLY A 400
REMARK 465 LEU A 401
REMARK 465 VAL A 402
REMARK 465 PRO A 403
REMARK 465 ARG A 404
REMARK 465 ALA B 21
REMARK 465 CYS B 22
REMARK 465 ASP B 23
REMARK 465 GLY B 391
REMARK 465 TYR B 392
REMARK 465 GLN B 393
REMARK 465 VAL B 394
REMARK 465 ASP B 395
REMARK 465 GLY B 396
REMARK 465 GLY B 397
REMARK 465 GLY B 398
REMARK 465 GLY B 399
REMARK 465 GLY B 400
REMARK 465 LEU B 401
REMARK 465 VAL B 402
REMARK 465 PRO B 403
REMARK 465 ARG B 404
REMARK 465 ALA C 21
REMARK 465 CYS C 22
REMARK 465 ASP C 23
REMARK 465 ASP C 395
REMARK 465 GLY C 396
REMARK 465 GLY C 397
REMARK 465 GLY C 398
REMARK 465 GLY C 399
REMARK 465 GLY C 400
REMARK 465 LEU C 401
REMARK 465 VAL C 402
REMARK 465 PRO C 403
REMARK 465 ARG C 404
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 ND2 ASN A 368 C2 NAG A 409 1.88
REMARK 500 O ASN C 368 N THR C 370 2.11
REMARK 500 ND2 ASN A 276 C2 NAG A 408 2.15
REMARK 500 OD1 ASP C 283 O GLY C 333 2.18
REMARK 500 ND2 ASN A 239 C2 NAG A 407 2.18
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 GLY A 344 N - CA - C ANGL. DEV. = -15.2 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 LYS A 25 95.32 71.06
REMARK 500 LEU A 82 -70.08 -95.67
REMARK 500 GLN A 86 77.86 47.88
REMARK 500 PRO A 96 37.35 -92.24
REMARK 500 SER A 132 -4.01 103.63
REMARK 500 TYR A 158 11.98 49.18
REMARK 500 ASN A 159 74.31 9.62
REMARK 500 ASP A 169 49.35 -81.35
REMARK 500 LYS A 193 141.32 -174.19
REMARK 500 ASN A 239 69.51 70.40
REMARK 500 SER A 243 -104.64 47.95
REMARK 500 VAL A 249 -165.62 -125.37
REMARK 500 ARG A 252 -40.24 98.52
REMARK 500 LEU A 259 -28.89 81.55
REMARK 500 VAL A 334 -28.49 125.15
REMARK 500 ASN A 368 -172.72 -68.89
REMARK 500 THR A 370 -52.04 -130.16
REMARK 500 ASN A 375 -169.90 -100.67
REMARK 500 GLN A 393 -30.22 52.02
REMARK 500 LEU B 82 -71.52 -100.96
REMARK 500 GLN B 86 71.07 56.88
REMARK 500 PRO B 96 41.87 -74.82
REMARK 500 HIS B 101 3.25 -57.58
REMARK 500 LEU B 121 12.73 -143.38
REMARK 500 THR B 122 -49.83 -133.13
REMARK 500 SER B 132 -157.16 -121.78
REMARK 500 ILE B 133 -60.75 51.56
REMARK 500 HIS B 134 74.46 -106.36
REMARK 500 ARG B 156 -51.16 96.80
REMARK 500 ASN B 161 13.67 -142.10
REMARK 500 GLU B 186 -2.39 60.83
REMARK 500 GLU B 192 -91.34 64.52
REMARK 500 ASN B 203 72.71 85.53
REMARK 500 ARG B 217 43.42 -142.47
REMARK 500 SER B 243 -130.92 63.42
REMARK 500 ARG B 252 -44.64 94.33
REMARK 500 GLU B 299 6.92 56.74
REMARK 500 VAL B 309 93.52 -178.64
REMARK 500 ARG B 337 73.66 58.86
REMARK 500 HIS B 371 129.28 87.65
REMARK 500 GLU B 387 118.98 85.25
REMARK 500 ILE C 26 108.15 74.89
REMARK 500 LYS C 37 0.68 -64.70
REMARK 500 ALA C 62 103.60 70.35
REMARK 500 ALA C 71 -20.93 97.10
REMARK 500 SER C 85 44.19 -150.95
REMARK 500 GLN C 86 65.01 31.40
REMARK 500 THR C 122 -44.74 -133.38
REMARK 500 SER C 132 -4.58 99.87
REMARK 500 TYR C 158 -20.33 69.03
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 201 LYS B 202 149.62
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3Q41 A 21 393 UNP P35439 NMDZ1_RAT 21 393
DBREF 3Q41 B 21 393 UNP P35439 NMDZ1_RAT 21 393
DBREF 3Q41 C 21 393 UNP P35439 NMDZ1_RAT 21 393
SEQADV 3Q41 VAL A 394 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ASP A 395 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY A 396 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY A 397 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY A 398 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY A 399 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY A 400 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 LEU A 401 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 VAL A 402 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 PRO A 403 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ARG A 404 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 VAL B 394 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ASP B 395 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY B 396 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY B 397 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY B 398 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY B 399 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY B 400 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 LEU B 401 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 VAL B 402 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 PRO B 403 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ARG B 404 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 VAL C 394 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ASP C 395 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY C 396 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY C 397 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY C 398 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY C 399 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 GLY C 400 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 LEU C 401 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 VAL C 402 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 PRO C 403 UNP P35439 EXPRESSION TAG
SEQADV 3Q41 ARG C 404 UNP P35439 EXPRESSION TAG
SEQRES 1 A 384 ALA CYS ASP PRO LYS ILE VAL ASN ILE GLY ALA VAL LEU
SEQRES 2 A 384 SER THR ARG LYS HIS GLU GLN MET PHE ARG GLU ALA VAL
SEQRES 3 A 384 ASN GLN ALA ASN LYS ARG HIS GLY SER TRP LYS ILE GLN
SEQRES 4 A 384 LEU ASN ALA THR SER VAL THR HIS LYS PRO ASN ALA ILE
SEQRES 5 A 384 GLN MET ALA LEU SER VAL CYS GLU ASP LEU ILE SER SER
SEQRES 6 A 384 GLN VAL TYR ALA ILE LEU VAL SER HIS PRO PRO THR PRO
SEQRES 7 A 384 ASN ASP HIS PHE THR PRO THR PRO VAL SER TYR THR ALA
SEQRES 8 A 384 GLY PHE TYR ARG ILE PRO VAL LEU GLY LEU THR THR ARG
SEQRES 9 A 384 MET SER ILE TYR SER ASP LYS SER ILE HIS LEU SER PHE
SEQRES 10 A 384 LEU ARG THR VAL PRO PRO TYR SER HIS GLN SER SER VAL
SEQRES 11 A 384 TRP PHE GLU MET MET ARG VAL TYR ASN TRP ASN HIS ILE
SEQRES 12 A 384 ILE LEU LEU VAL SER ASP ASP HIS GLU GLY ARG ALA ALA
SEQRES 13 A 384 GLN LYS ARG LEU GLU THR LEU LEU GLU GLU ARG GLU SER
SEQRES 14 A 384 LYS ALA GLU LYS VAL LEU GLN PHE ASP PRO GLY THR LYS
SEQRES 15 A 384 ASN VAL THR ALA LEU LEU MET GLU ALA ARG GLU LEU GLU
SEQRES 16 A 384 ALA ARG VAL ILE ILE LEU SER ALA SER GLU ASP ASP ALA
SEQRES 17 A 384 ALA THR VAL TYR ARG ALA ALA ALA MET LEU ASN MET THR
SEQRES 18 A 384 GLY SER GLY TYR VAL TRP LEU VAL GLY GLU ARG GLU ILE
SEQRES 19 A 384 SER GLY ASN ALA LEU ARG TYR ALA PRO ASP GLY ILE ILE
SEQRES 20 A 384 GLY LEU GLN LEU ILE ASN GLY LYS ASN GLU SER ALA HIS
SEQRES 21 A 384 ILE SER ASP ALA VAL GLY VAL VAL ALA GLN ALA VAL HIS
SEQRES 22 A 384 GLU LEU LEU GLU LYS GLU ASN ILE THR ASP PRO PRO ARG
SEQRES 23 A 384 GLY CYS VAL GLY ASN THR ASN ILE TRP LYS THR GLY PRO
SEQRES 24 A 384 LEU PHE LYS ARG VAL LEU MET SER SER LYS TYR ALA ASP
SEQRES 25 A 384 GLY VAL THR GLY ARG VAL GLU PHE ASN GLU ASP GLY ASP
SEQRES 26 A 384 ARG LYS PHE ALA ASN TYR SER ILE MET ASN LEU GLN ASN
SEQRES 27 A 384 ARG LYS LEU VAL GLN VAL GLY ILE TYR ASN GLY THR HIS
SEQRES 28 A 384 VAL ILE PRO ASN ASP ARG LYS ILE ILE TRP PRO GLY GLY
SEQRES 29 A 384 GLU THR GLU LYS PRO ARG GLY TYR GLN VAL ASP GLY GLY
SEQRES 30 A 384 GLY GLY GLY LEU VAL PRO ARG
SEQRES 1 B 384 ALA CYS ASP PRO LYS ILE VAL ASN ILE GLY ALA VAL LEU
SEQRES 2 B 384 SER THR ARG LYS HIS GLU GLN MET PHE ARG GLU ALA VAL
SEQRES 3 B 384 ASN GLN ALA ASN LYS ARG HIS GLY SER TRP LYS ILE GLN
SEQRES 4 B 384 LEU ASN ALA THR SER VAL THR HIS LYS PRO ASN ALA ILE
SEQRES 5 B 384 GLN MET ALA LEU SER VAL CYS GLU ASP LEU ILE SER SER
SEQRES 6 B 384 GLN VAL TYR ALA ILE LEU VAL SER HIS PRO PRO THR PRO
SEQRES 7 B 384 ASN ASP HIS PHE THR PRO THR PRO VAL SER TYR THR ALA
SEQRES 8 B 384 GLY PHE TYR ARG ILE PRO VAL LEU GLY LEU THR THR ARG
SEQRES 9 B 384 MET SER ILE TYR SER ASP LYS SER ILE HIS LEU SER PHE
SEQRES 10 B 384 LEU ARG THR VAL PRO PRO TYR SER HIS GLN SER SER VAL
SEQRES 11 B 384 TRP PHE GLU MET MET ARG VAL TYR ASN TRP ASN HIS ILE
SEQRES 12 B 384 ILE LEU LEU VAL SER ASP ASP HIS GLU GLY ARG ALA ALA
SEQRES 13 B 384 GLN LYS ARG LEU GLU THR LEU LEU GLU GLU ARG GLU SER
SEQRES 14 B 384 LYS ALA GLU LYS VAL LEU GLN PHE ASP PRO GLY THR LYS
SEQRES 15 B 384 ASN VAL THR ALA LEU LEU MET GLU ALA ARG GLU LEU GLU
SEQRES 16 B 384 ALA ARG VAL ILE ILE LEU SER ALA SER GLU ASP ASP ALA
SEQRES 17 B 384 ALA THR VAL TYR ARG ALA ALA ALA MET LEU ASN MET THR
SEQRES 18 B 384 GLY SER GLY TYR VAL TRP LEU VAL GLY GLU ARG GLU ILE
SEQRES 19 B 384 SER GLY ASN ALA LEU ARG TYR ALA PRO ASP GLY ILE ILE
SEQRES 20 B 384 GLY LEU GLN LEU ILE ASN GLY LYS ASN GLU SER ALA HIS
SEQRES 21 B 384 ILE SER ASP ALA VAL GLY VAL VAL ALA GLN ALA VAL HIS
SEQRES 22 B 384 GLU LEU LEU GLU LYS GLU ASN ILE THR ASP PRO PRO ARG
SEQRES 23 B 384 GLY CYS VAL GLY ASN THR ASN ILE TRP LYS THR GLY PRO
SEQRES 24 B 384 LEU PHE LYS ARG VAL LEU MET SER SER LYS TYR ALA ASP
SEQRES 25 B 384 GLY VAL THR GLY ARG VAL GLU PHE ASN GLU ASP GLY ASP
SEQRES 26 B 384 ARG LYS PHE ALA ASN TYR SER ILE MET ASN LEU GLN ASN
SEQRES 27 B 384 ARG LYS LEU VAL GLN VAL GLY ILE TYR ASN GLY THR HIS
SEQRES 28 B 384 VAL ILE PRO ASN ASP ARG LYS ILE ILE TRP PRO GLY GLY
SEQRES 29 B 384 GLU THR GLU LYS PRO ARG GLY TYR GLN VAL ASP GLY GLY
SEQRES 30 B 384 GLY GLY GLY LEU VAL PRO ARG
SEQRES 1 C 384 ALA CYS ASP PRO LYS ILE VAL ASN ILE GLY ALA VAL LEU
SEQRES 2 C 384 SER THR ARG LYS HIS GLU GLN MET PHE ARG GLU ALA VAL
SEQRES 3 C 384 ASN GLN ALA ASN LYS ARG HIS GLY SER TRP LYS ILE GLN
SEQRES 4 C 384 LEU ASN ALA THR SER VAL THR HIS LYS PRO ASN ALA ILE
SEQRES 5 C 384 GLN MET ALA LEU SER VAL CYS GLU ASP LEU ILE SER SER
SEQRES 6 C 384 GLN VAL TYR ALA ILE LEU VAL SER HIS PRO PRO THR PRO
SEQRES 7 C 384 ASN ASP HIS PHE THR PRO THR PRO VAL SER TYR THR ALA
SEQRES 8 C 384 GLY PHE TYR ARG ILE PRO VAL LEU GLY LEU THR THR ARG
SEQRES 9 C 384 MET SER ILE TYR SER ASP LYS SER ILE HIS LEU SER PHE
SEQRES 10 C 384 LEU ARG THR VAL PRO PRO TYR SER HIS GLN SER SER VAL
SEQRES 11 C 384 TRP PHE GLU MET MET ARG VAL TYR ASN TRP ASN HIS ILE
SEQRES 12 C 384 ILE LEU LEU VAL SER ASP ASP HIS GLU GLY ARG ALA ALA
SEQRES 13 C 384 GLN LYS ARG LEU GLU THR LEU LEU GLU GLU ARG GLU SER
SEQRES 14 C 384 LYS ALA GLU LYS VAL LEU GLN PHE ASP PRO GLY THR LYS
SEQRES 15 C 384 ASN VAL THR ALA LEU LEU MET GLU ALA ARG GLU LEU GLU
SEQRES 16 C 384 ALA ARG VAL ILE ILE LEU SER ALA SER GLU ASP ASP ALA
SEQRES 17 C 384 ALA THR VAL TYR ARG ALA ALA ALA MET LEU ASN MET THR
SEQRES 18 C 384 GLY SER GLY TYR VAL TRP LEU VAL GLY GLU ARG GLU ILE
SEQRES 19 C 384 SER GLY ASN ALA LEU ARG TYR ALA PRO ASP GLY ILE ILE
SEQRES 20 C 384 GLY LEU GLN LEU ILE ASN GLY LYS ASN GLU SER ALA HIS
SEQRES 21 C 384 ILE SER ASP ALA VAL GLY VAL VAL ALA GLN ALA VAL HIS
SEQRES 22 C 384 GLU LEU LEU GLU LYS GLU ASN ILE THR ASP PRO PRO ARG
SEQRES 23 C 384 GLY CYS VAL GLY ASN THR ASN ILE TRP LYS THR GLY PRO
SEQRES 24 C 384 LEU PHE LYS ARG VAL LEU MET SER SER LYS TYR ALA ASP
SEQRES 25 C 384 GLY VAL THR GLY ARG VAL GLU PHE ASN GLU ASP GLY ASP
SEQRES 26 C 384 ARG LYS PHE ALA ASN TYR SER ILE MET ASN LEU GLN ASN
SEQRES 27 C 384 ARG LYS LEU VAL GLN VAL GLY ILE TYR ASN GLY THR HIS
SEQRES 28 C 384 VAL ILE PRO ASN ASP ARG LYS ILE ILE TRP PRO GLY GLY
SEQRES 29 C 384 GLU THR GLU LYS PRO ARG GLY TYR GLN VAL ASP GLY GLY
SEQRES 30 C 384 GLY GLY GLY LEU VAL PRO ARG
MODRES 3Q41 ASN C 239 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN C 203 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN B 203 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN A 61 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN A 276 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN B 61 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN A 203 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN C 368 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN C 61 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN C 276 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN A 239 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN B 239 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN A 368 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN B 276 ASN GLYCOSYLATION SITE
MODRES 3Q41 ASN B 368 ASN GLYCOSYLATION SITE
HET NAG A 405 14
HET NAG A 406 14
HET NAG A 407 14
HET NAG A 408 14
HET NAG A 409 14
HET CL A 1 1
HET CL A 3 1
HET CL A 4 1
HET CL A 5 1
HET NAG B 405 14
HET NAG B 406 14
HET NAG B 407 14
HET NAG B 408 14
HET NAG B 409 14
HET CL B 6 1
HET CL B 7 1
HET NAG C 405 14
HET NAG C 406 14
HET NAG C 407 14
HET NAG C 408 14
HET NAG C 409 14
HET CL C 2 1
HET CL C 8 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
FORMUL 4 NAG 15(C8 H15 N O6)
FORMUL 9 CL 8(CL 1-)
FORMUL 27 HOH *25(H2 O)
HELIX 1 1 THR A 35 LYS A 51 1 17
HELIX 2 2 ASN A 70 ASP A 81 1 12
HELIX 3 3 LEU A 82 SER A 85 5 4
HELIX 4 4 THR A 103 PHE A 113 1 11
HELIX 5 5 MET A 125 ASP A 130 5 6
HELIX 6 6 PRO A 143 SER A 145 5 3
HELIX 7 7 HIS A 146 VAL A 157 1 12
HELIX 8 8 TYR A 158 TRP A 160 5 3
HELIX 9 9 ASP A 170 GLU A 186 1 17
HELIX 10 10 VAL A 204 GLU A 213 1 10
HELIX 11 11 SER A 224 LEU A 238 1 15
HELIX 12 12 ASN A 276 GLU A 297 1 22
HELIX 13 13 LYS A 316 SER A 327 1 12
HELIX 14 14 THR B 35 GLY B 54 1 20
HELIX 15 15 ASN B 70 ASP B 81 1 12
HELIX 16 16 LEU B 82 SER B 85 5 4
HELIX 17 17 THR B 103 PHE B 113 1 11
HELIX 18 18 MET B 125 ASP B 130 5 6
HELIX 19 19 PRO B 143 SER B 145 5 3
HELIX 20 20 HIS B 146 TYR B 158 1 13
HELIX 21 21 ASP B 170 GLU B 185 1 16
HELIX 22 22 VAL B 204 GLU B 213 1 10
HELIX 23 23 SER B 224 MET B 237 1 14
HELIX 24 24 GLY B 256 TYR B 261 1 6
HELIX 25 25 ASN B 276 LEU B 296 1 21
HELIX 26 26 THR B 317 SER B 327 1 11
HELIX 27 27 THR C 35 GLN C 48 1 14
HELIX 28 28 ILE C 72 LEU C 82 1 11
HELIX 29 29 ILE C 83 SER C 85 5 3
HELIX 30 30 THR C 103 PHE C 113 1 11
HELIX 31 31 MET C 125 SER C 129 5 5
HELIX 32 32 TYR C 144 HIS C 146 5 3
HELIX 33 33 GLN C 147 VAL C 157 1 11
HELIX 34 34 ASP C 170 GLU C 186 1 17
HELIX 35 35 VAL C 204 GLU C 213 1 10
HELIX 36 36 SER C 224 MET C 237 1 14
HELIX 37 37 GLY C 256 ALA C 262 1 7
HELIX 38 38 ASN C 276 LEU C 296 1 21
HELIX 39 39 LYS C 316 SER C 327 1 12
SHEET 1 A 5 GLN A 59 THR A 66 0
SHEET 2 A 5 ILE A 26 LEU A 33 1 N VAL A 27 O ASN A 61
SHEET 3 A 5 VAL A 87 VAL A 92 1 O LEU A 91 N VAL A 32
SHEET 4 A 5 VAL A 118 GLY A 120 1 O LEU A 119 N ILE A 90
SHEET 5 A 5 PHE A 137 ARG A 139 1 O LEU A 138 N GLY A 120
SHEET 1 B 4 LYS A 193 PHE A 197 0
SHEET 2 B 4 ILE A 163 SER A 168 1 N VAL A 167 O LEU A 195
SHEET 3 B 4 VAL A 218 SER A 222 1 O ILE A 220 N ILE A 164
SHEET 4 B 4 VAL A 246 LEU A 248 1 O VAL A 246 N ILE A 219
SHEET 1 C 3 ILE A 267 LEU A 271 0
SHEET 2 C 3 TYR A 351 GLN A 357 -1 O MET A 354 N GLY A 268
SHEET 3 C 3 LYS A 360 GLN A 363 -1 O VAL A 362 N ASN A 355
SHEET 1 D 2 LYS A 329 TYR A 330 0
SHEET 2 D 2 VAL A 338 GLU A 339 -1 O VAL A 338 N TYR A 330
SHEET 1 E 2 GLY A 365 TYR A 367 0
SHEET 2 E 2 VAL A 372 PRO A 374 -1 O ILE A 373 N ILE A 366
SHEET 1 F 5 ILE B 58 THR B 66 0
SHEET 2 F 5 LYS B 25 LEU B 33 1 N LYS B 25 O GLN B 59
SHEET 3 F 5 VAL B 87 VAL B 92 1 O LEU B 91 N VAL B 32
SHEET 4 F 5 VAL B 118 GLY B 120 1 O LEU B 119 N ILE B 90
SHEET 5 F 5 PHE B 137 ARG B 139 1 O LEU B 138 N VAL B 118
SHEET 1 G 4 LYS B 190 GLN B 196 0
SHEET 2 G 4 HIS B 162 VAL B 167 1 N LEU B 165 O LEU B 195
SHEET 3 G 4 VAL B 218 LEU B 221 1 O ILE B 220 N LEU B 166
SHEET 4 G 4 VAL B 246 LEU B 248 1 O LEU B 248 N ILE B 219
SHEET 1 H 3 ILE B 267 GLY B 268 0
SHEET 2 H 3 ASN B 350 GLN B 357 -1 O MET B 354 N GLY B 268
SHEET 3 H 3 LYS B 360 LEU B 361 -1 O LYS B 360 N GLN B 357
SHEET 1 I 3 ILE B 267 GLY B 268 0
SHEET 2 I 3 ASN B 350 GLN B 357 -1 O MET B 354 N GLY B 268
SHEET 3 I 3 GLY B 365 ASN B 368 -1 O TYR B 367 N TYR B 351
SHEET 1 J 3 LYS B 329 TYR B 330 0
SHEET 2 J 3 VAL B 338 PHE B 340 -1 O VAL B 338 N TYR B 330
SHEET 3 J 3 ARG B 346 LYS B 347 -1 O LYS B 347 N GLU B 339
SHEET 1 K 5 THR C 63 THR C 66 0
SHEET 2 K 5 ASN C 28 LEU C 33 1 N ALA C 31 O VAL C 65
SHEET 3 K 5 VAL C 87 VAL C 92 1 O LEU C 91 N VAL C 32
SHEET 4 K 5 VAL C 118 GLY C 120 1 O LEU C 119 N ILE C 90
SHEET 5 K 5 PHE C 137 ARG C 139 1 O LEU C 138 N GLY C 120
SHEET 1 L 4 LYS C 193 PHE C 197 0
SHEET 2 L 4 ILE C 164 SER C 168 1 N LEU C 165 O LEU C 195
SHEET 3 L 4 VAL C 218 SER C 222 1 O ILE C 220 N LEU C 166
SHEET 4 L 4 VAL C 246 VAL C 249 1 O VAL C 246 N ILE C 219
SHEET 1 M 4 ILE C 267 LEU C 271 0
SHEET 2 M 4 TYR C 351 GLN C 357 -1 O MET C 354 N GLY C 268
SHEET 3 M 4 LYS C 360 ASN C 368 -1 O TYR C 367 N TYR C 351
SHEET 4 M 4 HIS C 371 PRO C 374 -1 O ILE C 373 N ILE C 366
SHEET 1 N 2 LYS C 329 TYR C 330 0
SHEET 2 N 2 VAL C 338 GLU C 339 -1 O VAL C 338 N TYR C 330
SSBOND 1 CYS A 79 CYS A 308 1555 1555 2.05
SSBOND 2 CYS B 79 CYS B 308 1555 1555 2.05
SSBOND 3 CYS C 79 CYS C 308 1555 1555 2.05
LINK ND2 ASN A 61 C1 NAG A 405 1555 1555 1.44
LINK ND2 ASN A 203 C1 NAG A 406 1555 1555 1.44
LINK ND2 ASN A 239 C1 NAG A 407 1555 1555 1.45
LINK ND2 ASN A 276 C1 NAG A 408 1555 1555 1.44
LINK ND2 ASN A 368 C1 NAG A 409 1555 1555 1.45
LINK ND2 ASN B 61 C1 NAG B 405 1555 1555 1.44
LINK ND2 ASN B 203 C1 NAG B 406 1555 1555 1.44
LINK ND2 ASN B 239 C1 NAG B 407 1555 1555 1.45
LINK ND2 ASN B 276 C1 NAG B 408 1555 1555 1.45
LINK ND2 ASN B 368 C1 NAG B 409 1555 1555 1.46
LINK ND2 ASN C 61 C1 NAG C 405 1555 1555 1.44
LINK ND2 ASN C 203 C1 NAG C 406 1555 1555 1.43
LINK ND2 ASN C 239 C1 NAG C 407 1555 1555 1.43
LINK ND2 ASN C 276 C1 NAG C 408 1555 1555 1.44
LINK ND2 ASN C 368 C1 NAG C 409 1555 1555 1.44
CRYST1 164.679 164.679 147.258 90.00 90.00 120.00 P 31 2 1 18
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 0.006072 0.003506 0.000000 0.00000
SCALE2 0.000000 0.007012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
