HEADER HYDROLASE 22-MAY-08 3D7W
TITLE MISTLETOE LECTIN I IN COMPLEX WITH ZEATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDE-SPECIFIC LECTIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA-GALACTOSIDE-SPECIFIC LECTIN 1 CHAIN A ISOFORM 1;
COMPND 5 SYNONYM: BETA-GALACTOSIDE-SPECIFIC LECTIN I, VISCUMIN;
COMPND 6 EC: 3.2.2.22;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-GALACTOSIDE-SPECIFIC LECTIN 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: BETA-GALACTOSIDE-SPECIFIC LECTIN 1 CHAIN B;
COMPND 11 SYNONYM: BETA-GALACTOSIDE-SPECIFIC LECTIN I, VISCUMIN;
COMPND 12 EC: 3.2.2.22
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 4 ORGANISM_TAXID: 3972;
SOURCE 5 OTHER_DETAILS: SEMIPARASITIC PLANT;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 8 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 9 ORGANISM_TAXID: 3972;
SOURCE 10 OTHER_DETAILS: SEMIPARASITIC PLANT
KEYWDS MISTLETOE LECTIN I, CYTOKININ, ZEATIN, PLANT HORMONES, MICROGRAVITY,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, LECTIN, PLANT DEFENSE, PROTEIN SYNTHESIS
KEYWDS 3 INHIBITOR, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MEYER,W.RYPNIEWSKI,M.SZYMANSKI,W.VOELTER,J.BARCISZEWSKI,C.BETZEL
REVDAT 6 01-NOV-23 3D7W 1 HETSYN
REVDAT 5 29-JUL-20 3D7W 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 05-FEB-14 3D7W 1 REMARK
REVDAT 3 13-JUL-11 3D7W 1 VERSN
REVDAT 2 09-DEC-08 3D7W 1 JRNL VERSN
REVDAT 1 17-JUN-08 3D7W 0
SPRSDE 17-JUN-08 3D7W 3CEF
JRNL AUTH A.MEYER,W.RYPNIEWSKI,M.SZYMANSKI,W.VOELTER,J.BARCISZEWSKI,
JRNL AUTH 2 C.BETZEL
JRNL TITL STRUCTURE OF MISTLETOE LECTIN I FROM VISCUM ALBUM IN COMPLEX
JRNL TITL 2 WITH THE PHYTOHORMONE ZEATIN
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1784 1590 2008
JRNL REFN ISSN 0006-3002
JRNL PMID 18718563
JRNL DOI 10.1016/J.BBAPAP.2008.07.010
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35020
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1858
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2413
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3927
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 150
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.65000
REMARK 3 B22 (A**2) : 1.65000
REMARK 3 B33 (A**2) : -2.48000
REMARK 3 B12 (A**2) : 0.83000
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): 0.230
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4168 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5685 ; 2.082 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 515 ; 8.585 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;38.361 ;24.570
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 636 ;18.149 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;20.830 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 653 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3149 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2093 ; 0.262 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2894 ; 0.326 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 291 ; 0.192 ; 0.200
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): 39 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.296 ; 0.200
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): 2618 ; 1.193 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4131 ; 2.134 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1776 ; 3.187 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1554 ; 4.889 ; 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 : 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; THE LINK RECORDS HERE ARE EITHER N- OR O GLYCOSIDIC
REMARK 3 BONDS WHICH CAN BE ASSUMED AS A LENGTH OF 1.51 A. SOME OF THAT
REMARK 3 LINKAGES ARE LONGER. THAT CAN BE ASSUMED AS UNRELIABILITY OF THE
REMARK 3 COORDINATES BECAUSE OF THE HIGH TEMPERATURE DISORDER.
REMARK 4
REMARK 4 3D7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 2.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8073
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
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) : 0.62000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1M2T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: COUNTER DIFFUSION UNDER MICROGRAVITY
REMARK 280 CONDITIONS DURING JAXA-GCF-FLIGHT NUMBER 6, PH 2.5, LIQUID
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 207.77800
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 103.88900
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 155.83350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.94450
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 259.72250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 207.77800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 103.88900
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 51.94450
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 155.83350
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 259.72250
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 765 LIES ON A SPECIAL POSITION.
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 ARG A 250
REMARK 465 PRO A 251
REMARK 465 SER A 252
REMARK 465 SER A 253
REMARK 465 SER A 254
REMARK 465 ASP B 248
REMARK 465 MET B 511
REMARK 465 THR B 512
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 N TYR A 17 O HOH A 748 1.59
REMARK 500 O HOH B 708 O HOH B 853 1.90
REMARK 500 O THR A 13 O HOH A 748 1.91
REMARK 500 O4 NAG D 1 O5 NAG D 2 2.04
REMARK 500 O HOH A 730 O HOH A 758 2.10
REMARK 500 O HOH A 737 O HOH B 766 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 754 O HOH B 781 6554 2.02
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 SER B 489 N SER B 489 CA 0.133
REMARK 500 SER B 489 CB SER B 489 OG 0.108
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 ASP A 211 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 384 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 388 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 492 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 9 -168.12 -163.75
REMARK 500 ASN A 35 46.52 39.17
REMARK 500 ASN A 74 0.61 -152.00
REMARK 500 ASP A 100 -73.25 -70.19
REMARK 500 ILE A 163 -79.40 -111.22
REMARK 500 ALA A 223 -131.30 45.77
REMARK 500 CYS B 252 53.31 -152.51
REMARK 500 ALA B 254 -29.57 50.29
REMARK 500 ASP B 327 125.96 -36.41
REMARK 500 ASP B 372 8.60 -152.45
REMARK 500 ALA B 484 13.39 -142.83
REMARK 500 GLN B 485 179.32 -58.20
REMARK 500 ALA B 486 -14.54 -150.20
REMARK 500 ASN B 487 112.50 85.34
REMARK 500 SER B 489 -33.94 166.86
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 CYS A 247 GLY A 248 145.47
REMARK 500 VAL B 483 ALA B 484 -33.67
REMARK 500 PRO B 488 SER B 489 50.09
REMARK 500 LEU B 490 GLN B 491 -38.12
REMARK 500 GLN B 491 ARG B 492 -65.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE LIGAND ZEATIN IS IN CIS- AND TRANS- FORMS.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M2T RELATED DB: PDB
REMARK 900 MISTLETOE LECTIN I COMPLEXED WITH ADENINE
REMARK 900 RELATED ID: 2R9K RELATED DB: PDB
REMARK 900 MISTLETOE LECTIN I COMPLEXED WITH PHLORETAMIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STAE THAT THE PLANT PROTEINS CAN DIFFER IN
REMARK 999 SOME CODONS DEPENDING ON THE SEASON AND ON THE HOST WHERE
REMARK 999 THE MISTLETOE HAS GROWN.
REMARK 999 THE SEQUENCES IN THE CHAINS A AND B WERE ALIGNED ALONG
REMARK 999 WITH 1M2T. ASP AT POSITION 249 IN CHAIN B HAS BEEN DERIVED
REMARK 999 BY INTERPRETATION OF THE 2FO-FC SIGNAL, EVEN THOUGH IT IS
REMARK 999 ALA IN 1M2T.
DBREF 3D7W A 1 254 UNP P81446 ML1_VISAL 34 287
DBREF 3D7W B 248 510 UNP P81446 ML1_VISAL 302 564
SEQADV 3D7W THR A 8 UNP P81446 VAL 41 SEE REMARK 999
SEQADV 3D7W ASP A 9 UNP P81446 THR 42 SEE REMARK 999
SEQADV 3D7W GLN A 10 UNP P81446 HIS 43 SEE REMARK 999
SEQADV 3D7W SER A 19 UNP P81446 ARG 52 SEE REMARK 999
SEQADV 3D7W ASN A 36 UNP P81446 GLU 69 SEE REMARK 999
SEQADV 3D7W VAL A 45 UNP P81446 ILE 78 SEE REMARK 999
SEQADV 3D7W GLU A 49 UNP P81446 ASP 82 SEE REMARK 999
SEQADV 3D7W GLY A 50 UNP P81446 ALA 83 SEE REMARK 999
SEQADV 3D7W ALA A 61 UNP P81446 GLU 94 SEE REMARK 999
SEQADV 3D7W THR A 65 UNP P81446 SER 98 SEE REMARK 999
SEQADV 3D7W GLU A 81 UNP P81446 GLN 114 SEE REMARK 999
SEQADV 3D7W ASN A 84 UNP P81446 ASP 117 SEE REMARK 999
SEQADV 3D7W SER A 90 UNP P81446 ARG 123 SEE REMARK 999
SEQADV 3D7W ALA A 94 UNP P81446 ARG 127 SEE REMARK 999
SEQADV 3D7W GLN A 99 UNP P81446 HIS 132 SEE REMARK 999
SEQADV 3D7W ASP A 100 UNP P81446 LEU 133 SEE REMARK 999
SEQADV 3D7W SER A 102 UNP P81446 THR 135 SEE REMARK 999
SEQADV 3D7W SER A 106 UNP P81446 ARG 139 SEE REMARK 999
SEQADV 3D7W GLN A 109 UNP P81446 LEU 142 SEE REMARK 999
SEQADV 3D7W GLN A 148 UNP P81446 SER 181 SEE REMARK 999
SEQADV 3D7W LYS A 150 UNP P81446 ARG 183 SEE REMARK 999
SEQADV 3D7W HIS A 208 UNP P81446 GLN 241 SEE REMARK 999
SEQADV 3D7W ALA A 219 UNP P81446 ARG 252 SEE REMARK 999
SEQADV 3D7W ALA A 223 UNP P81446 PRO 256 SEE REMARK 999
SEQADV 3D7W VAL A 226 UNP P81446 ASN 259 SEE REMARK 999
SEQADV 3D7W ILE A 227 UNP P81446 PHE 260 SEE REMARK 999
SEQADV 3D7W ILE A 233 UNP P81446 VAL 266 SEE REMARK 999
SEQADV 3D7W MET B 511 UNP P81446 SEE REMARK 999
SEQADV 3D7W THR B 512 UNP P81446 SEE REMARK 999
SEQRES 1 A 254 TYR GLU ARG LEU ARG LEU ARG THR ASP GLN GLN THR THR
SEQRES 2 A 254 GLY GLU GLU TYR PHE SER PHE ILE THR LEU LEU ARG ASP
SEQRES 3 A 254 TYR VAL SER SER GLY SER PHE SER ASN ASN ILE PRO LEU
SEQRES 4 A 254 LEU ARG GLN SER THR VAL PRO VAL SER GLU GLY GLN ARG
SEQRES 5 A 254 PHE VAL LEU VAL GLU LEU THR ASN ALA GLY GLY ASP THR
SEQRES 6 A 254 ILE THR ALA ALA ILE ASP VAL THR ASN LEU TYR VAL VAL
SEQRES 7 A 254 ALA TYR GLU ALA GLY ASN GLN SER TYR PHE LEU SER ASP
SEQRES 8 A 254 ALA PRO ALA GLY ALA GLU THR GLN ASP PHE SER GLY THR
SEQRES 9 A 254 THR SER SER SER GLN PRO PHE ASN GLY SER TYR PRO ASP
SEQRES 10 A 254 LEU GLU ARG TYR ALA GLY HIS ARG ASP GLN ILE PRO LEU
SEQRES 11 A 254 GLY ILE ASP GLN LEU ILE GLN SER VAL THR ALA LEU ARG
SEQRES 12 A 254 PHE PRO GLY GLY GLN THR LYS THR GLN ALA ARG SER ILE
SEQRES 13 A 254 LEU ILE LEU ILE GLN MET ILE SER GLU ALA ALA ARG PHE
SEQRES 14 A 254 ASN PRO ILE LEU TRP ARG ALA ARG GLN TYR ILE ASN SER
SEQRES 15 A 254 GLY ALA SER PHE LEU PRO ASP VAL TYR MET LEU GLU LEU
SEQRES 16 A 254 GLU THR SER TRP GLY GLN GLN SER THR GLN VAL GLN HIS
SEQRES 17 A 254 SER THR ASP GLY VAL PHE ASN ASN PRO ILE ALA LEU ALA
SEQRES 18 A 254 ILE ALA PRO GLY VAL ILE VAL THR LEU THR ASN ILE ARG
SEQRES 19 A 254 ASP VAL ILE ALA SER LEU ALA ILE MET LEU PHE VAL CYS
SEQRES 20 A 254 GLY GLU ARG PRO SER SER SER
SEQRES 1 B 265 ASP ASP VAL THR CYS THR ALA SER GLU PRO ILE VAL ARG
SEQRES 2 B 265 ILE VAL GLY ARG ASN GLY MET THR VAL ASP VAL ARG ASP
SEQRES 3 B 265 ASP ASP PHE HIS ASP GLY ASN GLN ILE GLN LEU TRP PRO
SEQRES 4 B 265 SER LYS SER ASN ASN ASP PRO ASN GLN LEU TRP THR ILE
SEQRES 5 B 265 LYS LYS ASP GLY THR ILE ARG SER ASN GLY SER CYS LEU
SEQRES 6 B 265 THR THR TYR GLY TYR THR ALA GLY VAL TYR VAL MET ILE
SEQRES 7 B 265 PHE ASP CYS ASN THR ALA VAL ARG GLU ALA THR ILE TRP
SEQRES 8 B 265 GLN ILE TRP GLY ASN GLY THR ILE ILE ASN PRO ARG SER
SEQRES 9 B 265 ASN LEU VAL LEU ALA ALA SER SER GLY ILE LYS GLY THR
SEQRES 10 B 265 THR LEU THR VAL GLN THR LEU ASP TYR THR LEU GLY GLN
SEQRES 11 B 265 GLY TRP LEU ALA GLY ASN ASP THR ALA PRO ARG GLU THR
SEQRES 12 B 265 THR ILE TYR GLY PHE ARG ASP LEU CYS MET GLU SER ALA
SEQRES 13 B 265 GLY GLY SER VAL TYR VAL GLU THR CYS THR ALA GLY GLN
SEQRES 14 B 265 GLU ASN GLN ARG TRP ALA LEU TYR GLY ASP GLY SER ILE
SEQRES 15 B 265 ARG PRO LYS GLN LEU GLN SER GLN CYS LEU THR ASN GLY
SEQRES 16 B 265 ARG ASP SER ILE SER THR VAL ILE ASN ILE VAL SER CYS
SEQRES 17 B 265 SER ALA GLY SER SER GLY GLN ARG TRP VAL PHE THR ASN
SEQRES 18 B 265 GLU GLY ALA ILE LEU ASN LEU LYS ASN GLY LEU ALA MET
SEQRES 19 B 265 ASP VAL ALA GLN ALA ASN PRO SER LEU GLN ARG ILE ILE
SEQRES 20 B 265 ILE TYR PRO ALA THR GLY ASN PRO ASN GLN MET TRP LEU
SEQRES 21 B 265 PRO VAL PRO MET THR
MODRES 3D7W ASN A 112 ASN GLYCOSYLATION SITE
MODRES 3D7W ASN B 308 ASN GLYCOSYLATION SITE
MODRES 3D7W ASN B 343 ASN GLYCOSYLATION SITE
MODRES 3D7W ASN B 383 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG A 500 14
HET SO4 A 660 5
HET SO4 A 661 5
HET GOL A 648 6
HET GOL A 652 6
HET NAG B 600 14
HET ZEA B 701 16
HET ZEZ B 702 16
HET GOL B 650 6
HET GOL B 651 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM ZEA (2E)-2-METHYL-4-(9H-PURIN-6-YLAMINO)BUT-2-EN-1-OL
HETNAM ZEZ (2Z)-2-METHYL-4-(9H-PURIN-6-YLAMINO)BUT-2-EN-1-OL
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 GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN ZEA TRANS-ZEATIN
HETSYN ZEZ CIS-ZEATIN
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 GOL 4(C3 H8 O3)
FORMUL 11 ZEA C10 H13 N5 O
FORMUL 12 ZEZ C10 H13 N5 O
FORMUL 15 HOH *282(H2 O)
HELIX 1 1 THR A 13 VAL A 28 1 16
HELIX 2 2 GLY A 95 ASP A 100 1 6
HELIX 3 3 SER A 114 GLY A 123 1 10
HELIX 4 4 HIS A 124 ILE A 128 5 5
HELIX 5 5 GLY A 131 PHE A 144 1 14
HELIX 6 6 GLN A 148 ILE A 163 1 16
HELIX 7 7 ILE A 163 PHE A 169 1 7
HELIX 8 8 PHE A 169 GLY A 183 1 15
HELIX 9 9 ASP A 189 SER A 209 1 21
HELIX 10 10 ILE A 233 ILE A 237 1 5
HELIX 11 11 GLY B 263 MET B 267 5 5
HELIX 12 12 ASP B 273 ASP B 275 5 3
HELIX 13 13 ASP B 292 LEU B 296 5 5
HELIX 14 14 VAL B 332 ILE B 337 5 6
HELIX 15 15 THR B 374 GLY B 378 5 5
HELIX 16 16 GLY B 394 LEU B 398 5 5
HELIX 17 17 GLN B 416 ASN B 418 5 3
HELIX 18 18 SER B 459 GLN B 462 5 4
HELIX 19 19 ASN B 501 MET B 505 5 5
SHEET 1 A 6 GLU A 2 ARG A 7 0
SHEET 2 A 6 PHE A 53 THR A 59 1 O GLU A 57 N LEU A 4
SHEET 3 A 6 THR A 65 ASP A 71 -1 O ILE A 70 N VAL A 54
SHEET 4 A 6 VAL A 77 ALA A 82 -1 O VAL A 78 N ALA A 69
SHEET 5 A 6 GLN A 85 PHE A 88 -1 O TYR A 87 N TYR A 80
SHEET 6 A 6 THR A 105 SER A 108 1 O THR A 105 N SER A 86
SHEET 1 B 2 SER A 29 SER A 34 0
SHEET 2 B 2 ILE A 37 LEU A 40 -1 O LEU A 39 N SER A 30
SHEET 1 C 2 VAL A 213 ILE A 222 0
SHEET 2 C 2 VAL A 226 ASN A 232 -1 O VAL A 228 N LEU A 220
SHEET 1 D 5 ILE B 258 VAL B 259 0
SHEET 2 D 5 TRP B 297 ILE B 299 -1 O TRP B 297 N VAL B 259
SHEET 3 D 5 ILE B 305 SER B 307 -1 O ARG B 306 N THR B 298
SHEET 4 D 5 SER B 310 THR B 314 -1 O SER B 310 N SER B 307
SHEET 5 D 5 VAL B 323 PHE B 326 -1 O MET B 324 N THR B 313
SHEET 1 E 2 ILE B 261 VAL B 262 0
SHEET 2 E 2 LEU B 380 ALA B 381 -1 O LEU B 380 N VAL B 262
SHEET 1 F 2 THR B 268 VAL B 271 0
SHEET 2 F 2 ILE B 282 TRP B 285 -1 O GLN B 283 N ASP B 270
SHEET 1 G 4 GLN B 339 ILE B 340 0
SHEET 2 G 4 ILE B 346 ASN B 348 -1 O ILE B 347 N GLN B 339
SHEET 3 G 4 LEU B 353 ALA B 356 -1 O LEU B 353 N ASN B 348
SHEET 4 G 4 THR B 367 GLN B 369 -1 O GLN B 369 N VAL B 354
SHEET 1 H 4 ILE B 429 PRO B 431 0
SHEET 2 H 4 ARG B 420 LEU B 423 -1 N ALA B 422 O ARG B 430
SHEET 3 H 4 ARG B 388 TYR B 393 -1 N ARG B 388 O LEU B 423
SHEET 4 H 4 LEU B 507 VAL B 509 -1 O LEU B 507 N TYR B 393
SHEET 1 I 2 CYS B 399 ALA B 403 0
SHEET 2 I 2 SER B 406 GLU B 410 -1 O TYR B 408 N GLU B 401
SHEET 1 J 2 GLN B 437 THR B 440 0
SHEET 2 J 2 ASN B 451 SER B 454 -1 O ASN B 451 N THR B 440
SHEET 1 K 2 TRP B 464 PHE B 466 0
SHEET 2 K 2 ILE B 472 ASN B 474 -1 O LEU B 473 N VAL B 465
SHEET 1 L 2 ALA B 480 VAL B 483 0
SHEET 2 L 2 ILE B 493 TYR B 496 -1 O TYR B 496 N ALA B 480
SSBOND 1 CYS A 247 CYS B 252 1555 1555 2.06
SSBOND 2 CYS B 311 CYS B 328 1555 1555 2.12
SSBOND 3 CYS B 399 CYS B 412 1555 1555 2.11
SSBOND 4 CYS B 438 CYS B 455 1555 1555 2.09
LINK ND2 ASN A 112 C1 NAG A 500 1555 1555 1.51
LINK ND2 ASN B 308 C1 NAG B 600 1555 1555 1.89
LINK ND2 ASN B 343 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 383 C1 NAG D 1 1555 1555 1.41
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.74
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.78
CISPEP 1 GLY A 248 GLU A 249 0 24.13
CISPEP 2 ALA B 484 GLN B 485 0 -14.95
CISPEP 3 GLN B 485 ALA B 486 0 -4.82
CISPEP 4 ALA B 486 ASN B 487 0 -14.14
CISPEP 5 SER B 489 LEU B 490 0 17.43
CRYST1 106.644 106.644 311.667 90.00 90.00 120.00 P 65 2 2 12
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 0.009377 0.005414 0.000000 0.00000
SCALE2 0.000000 0.010828 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003209 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
