HEADER RIBOSOME INHIBITOR, HYDROLASE 25-JUN-02 1M2T
TITLE MISTLETOE LECTIN I FROM VISCUM ALBUM IN COMPLEX WITH ADENINE
TITLE 2 MONOPHOSPHATE. CRYSTAL STRUCTURE AT 1.9 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MISTLETOE LECTIN I A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-GALACTOSIDE SPECIFIC LECTIN I A CHAIN; MLA; ML-I A;
COMPND 5 RRNA N-GLYCOSIDASE;
COMPND 6 EC: 3.2.2.22;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MISTLETOE LECTIN I B CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: LECTIN CHAIN A ISOFORM 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 4 ORGANISM_TAXID: 3972;
SOURCE 5 ORGAN: LEAF;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 8 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 9 ORGANISM_TAXID: 3972;
SOURCE 10 ORGAN: LEAF
KEYWDS RIBOSOME INACTIVATION, RIBOSOME INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KRAUSPENHAAR,W.RYPNIEWSKI,N.KALKURA,K.MOORE,L.DELUCAS,S.STOEVA,
AUTHOR 2 A.MIKHAILOV,W.VOELTER,C.BETZEL
REVDAT 5 03-APR-24 1M2T 1 HETSYN
REVDAT 4 29-JUL-20 1M2T 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 13-JUL-11 1M2T 1 VERSN
REVDAT 2 24-FEB-09 1M2T 1 VERSN
REVDAT 1 24-JUN-03 1M2T 0
JRNL AUTH R.KRAUSPENHAAR,W.RYPNIEWSKI,N.KALKURA,K.MOORE,L.DELUCAS,
JRNL AUTH 2 S.STOEVA,A.MIKHAILOV,W.VOELTER,C.H.BETZEL
JRNL TITL CRYSTALLISATION UNDER MICROGRAVITY OF MISTLETOE LECTIN I
JRNL TITL 2 FROM VISCUM ALBUM WITH ADENINE MONOPHOSPHATE AND THE CRYSTAL
JRNL TITL 3 STRUCTURE AT 1.9 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 1704 2002
JRNL REFN ISSN 0907-4449
JRNL PMID 12351890
JRNL DOI 10.1107/S0907444902014270
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 83270
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4159
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3907
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.029 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-01
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 : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8459
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83270
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 38.00
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.76400
REMARK 200 R SYM FOR SHELL (I) : 0.76400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: UNPUBLISHED STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 2.5, VAPOR
REMARK 280 DIFFUSION UNDER MICROGRAVITY AT 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 206.54667
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 103.27333
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 154.91000
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 51.63667
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 258.18333
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 206.54667
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 103.27333
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 51.63667
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 154.91000
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 258.18333
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: 6780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 249
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 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 ARG A 5 NE CZ NH1 NH2
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 B 768 O HOH B 768 12554 1.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 3 CD - NE - CZ ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 9 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 LEU A 118 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 333 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 333 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 LYS B 362 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ASN B 383 CB - CG - OD1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG B 420 NE - CZ - NH1 ANGL. DEV. = 5.3 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 ASN A 36 3.87 80.94
REMARK 500 SER A 43 43.26 -92.54
REMARK 500 ILE A 163 -74.43 -116.46
REMARK 500 ALA A 223 -61.02 -18.09
REMARK 500 PRO A 224 46.42 -92.23
REMARK 500 VAL A 226 -169.79 -106.33
REMARK 500 CYS B 252 61.07 -157.65
REMARK 500 ALA B 254 7.20 50.77
REMARK 500 SER B 447 10.09 80.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 7 11.95
REMARK 500 SER A 86 14.57
REMARK 500 SER B 255 11.44
REMARK 500 LYS B 288 11.95
REMARK 500 ASN B 343 -11.95
REMARK 500 ASN B 352 10.69
REMARK 500 ASP B 384 -10.48
REMARK 500 CYS B 438 -10.67
REMARK 500 LEU B 479 -12.07
REMARK 500 ASN B 487 -11.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 500
REMARK 610 FUC A 501
REMARK 610 NAG A 502
REMARK 610 NAG B 600
REMARK 610 FUC B 601
REMARK 610 NAG B 602
REMARK 610 NAG B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2MLL RELATED DB: PDB
REMARK 900 2.7 A RESOLUTION
DBREF 1M2T A 1 254 UNP P81446 ML1_VISAL 1 254
DBREF 1M2T B 248 510 UNP P81830 MLB1_VISAL 1 264
SEQADV 1M2T THR A 8 UNP P81446 VAL 8 CONFLICT
SEQADV 1M2T ASP A 9 UNP P81446 THR 9 CONFLICT
SEQADV 1M2T GLN A 10 UNP P81446 HIS 10 CONFLICT
SEQADV 1M2T ALA A 15 UNP P81446 GLU 15 CONFLICT
SEQADV 1M2T SER A 19 UNP P81446 ARG 19 CONFLICT
SEQADV 1M2T VAL A 23 UNP P81446 LEU 23 CONFLICT
SEQADV 1M2T ASN A 36 UNP P81446 GLU 36 CONFLICT
SEQADV 1M2T VAL A 45 UNP P81446 ILE 45 CONFLICT
SEQADV 1M2T GLU A 49 UNP P81446 ASP 49 CONFLICT
SEQADV 1M2T GLY A 50 UNP P81446 ALA 50 CONFLICT
SEQADV 1M2T ALA A 61 UNP P81446 GLN 61 CONFLICT
SEQADV 1M2T GLY A 63 UNP P81446 GLN 63 CONFLICT
SEQADV 1M2T THR A 65 UNP P81446 SER 65 CONFLICT
SEQADV 1M2T ILE A 66 UNP P81446 VAL 66 CONFLICT
SEQADV 1M2T LEU A 75 UNP P81446 ALA 75 CONFLICT
SEQADV 1M2T GLU A 81 UNP P81446 GLN 81 CONFLICT
SEQADV 1M2T ASN A 84 UNP P81446 ASP 84 CONFLICT
SEQADV 1M2T SER A 90 UNP P81446 ARG 90 CONFLICT
SEQADV 1M2T ALA A 94 UNP P81446 ARG 94 CONFLICT
SEQADV 1M2T GLN A 99 UNP P81446 HIS 99 CONFLICT
SEQADV 1M2T ASP A 100 UNP P81446 LEU 100 CONFLICT
SEQADV 1M2T SER A 102 UNP P81446 THR 102 CONFLICT
SEQADV 1M2T SER A 106 UNP P81446 ARG 106 CONFLICT
SEQADV 1M2T GLN A 109 UNP P81446 LEU 109 CONFLICT
SEQADV 1M2T GLN A 148 UNP P81446 SER 148 CONFLICT
SEQADV 1M2T LYS A 150 UNP P81446 ARG 150 CONFLICT
SEQADV 1M2T ALA A 176 UNP P81446 TYR 176 CONFLICT
SEQADV 1M2T ALA A 219 UNP P81446 ARG 219 CONFLICT
SEQADV 1M2T ALA A 223 UNP P81446 PRO 223 CONFLICT
SEQADV 1M2T VAL A 226 UNP P81446 ASN 226 CONFLICT
SEQADV 1M2T ILE A 227 UNP P81446 PHE 227 CONFLICT
SEQADV 1M2T ILE A 233 UNP P81446 VAL 233 CONFLICT
SEQADV 1M2T ALA B 249 UNP P81830 ASP 2 CONFLICT
SEQADV 1M2T THR B 253 UNP P81830 SER 6 CONFLICT
SEQADV 1M2T ILE B 258 UNP P81830 THR 11 CONFLICT
SEQADV 1M2T THR B 268 UNP P81830 ARG 21 CONFLICT
SEQADV 1M2T LYS B 301 UNP P81830 ARG 54 CONFLICT
SEQADV 1M2T GLY B 342 UNP P81830 ASP 95 CONFLICT
SEQADV 1M2T THR B 390 UNP P81830 VAL 143 CONFLICT
SEQADV 1M2T ALA B 403 UNP P81830 ASN 156 CONFLICT
SEQADV 1M2T TYR B 408 UNP P81830 TRP 161 CONFLICT
SEQADV 1M2T THR B 413 UNP P81830 ASP 166 CONFLICT
SEQADV 1M2T ALA B 414 UNP P81830 SER 167 CONFLICT
SEQADV 1M2T GLY B 415 UNP P81830 SER 168 CONFLICT
SEQADV 1M2T GLU B 417 UNP P81830 LYS 170 CONFLICT
SEQADV 1M2T B UNP P81830 GLY 173 DELETION
SEQADV 1M2T ARG B 420 UNP P81830 LYS 174 CONFLICT
SEQADV 1M2T LEU B 434 UNP P81830 ASN 188 CONFLICT
SEQADV 1M2T SER B 436 UNP P81830 ASP 190 CONFLICT
SEQADV 1M2T ASN B 441 UNP P81830 SER 195 CONFLICT
SEQADV 1M2T ILE B 446 UNP P81830 VAL 200 CONFLICT
SEQADV 1M2T ALA B 457 UNP P81830 INSERTION
SEQADV 1M2T SER B 459 UNP P81830 ALA 212 CONFLICT
SEQADV 1M2T B UNP P81830 SER 215 DELETION
SEQADV 1M2T SER B 489 UNP P81830 LYS 243 CONFLICT
SEQADV 1M2T GLN B 491 UNP P81830 ARG 245 CONFLICT
SEQADV 1M2T ASN B 501 UNP P81830 LYS 255 CONFLICT
SEQADV 1M2T PRO B 510 UNP P81830 PHE 264 CONFLICT
SEQRES 1 A 254 TYR GLU ARG LEU ARG LEU ARG THR ASP GLN GLN THR THR
SEQRES 2 A 254 GLY ALA GLU TYR PHE SER PHE ILE THR VAL 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 263 ASP ALA VAL THR CYS THR ALA SER GLU PRO ILE VAL ARG
SEQRES 2 B 263 ILE VAL GLY ARG ASN GLY MET THR VAL ASP VAL ARG ASP
SEQRES 3 B 263 ASP ASP PHE HIS ASP GLY ASN GLN ILE GLN LEU TRP PRO
SEQRES 4 B 263 SER LYS SER ASN ASN ASP PRO ASN GLN LEU TRP THR ILE
SEQRES 5 B 263 LYS LYS ASP GLY THR ILE ARG SER ASN GLY SER CYS LEU
SEQRES 6 B 263 THR THR TYR GLY TYR THR ALA GLY VAL TYR VAL MET ILE
SEQRES 7 B 263 PHE ASP CYS ASN THR ALA VAL ARG GLU ALA THR ILE TRP
SEQRES 8 B 263 GLN ILE TRP GLY ASN GLY THR ILE ILE ASN PRO ARG SER
SEQRES 9 B 263 ASN LEU VAL LEU ALA ALA SER SER GLY ILE LYS GLY THR
SEQRES 10 B 263 THR LEU THR VAL GLN THR LEU ASP TYR THR LEU GLY GLN
SEQRES 11 B 263 GLY TRP LEU ALA GLY ASN ASP THR ALA PRO ARG GLU THR
SEQRES 12 B 263 THR ILE TYR GLY PHE ARG ASP LEU CYS MET GLU SER ALA
SEQRES 13 B 263 GLY GLY SER VAL TYR VAL GLU THR CYS THR ALA GLY GLN
SEQRES 14 B 263 GLU ASN GLN ARG TRP ALA LEU TYR GLY ASP GLY SER ILE
SEQRES 15 B 263 ARG PRO LYS GLN LEU GLN SER GLN CYS LEU THR ASN GLY
SEQRES 16 B 263 ARG ASP SER ILE SER THR VAL ILE ASN ILE VAL SER CYS
SEQRES 17 B 263 SER ALA GLY SER SER GLY GLN ARG TRP VAL PHE THR ASN
SEQRES 18 B 263 GLU GLY ALA ILE LEU ASN LEU LYS ASN GLY LEU ALA MET
SEQRES 19 B 263 ASP VAL ALA GLN ALA ASN PRO SER LEU GLN ARG ILE ILE
SEQRES 20 B 263 ILE TYR PRO ALA THR GLY ASN PRO ASN GLN MET TRP LEU
SEQRES 21 B 263 PRO VAL PRO
MODRES 1M2T ASN B 383 ASN GLYCOSYLATION SITE
HET NAG A 500 14
HET FUC A 501 10
HET NAG A 502 14
HET ADE A9550 10
HET GOL A 600 6
HET GOL A 601 6
HET GOL A 700 6
HET GOL A 702 6
HET NAG B 600 14
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET GOL B 701 6
HET GOL B 703 6
HET GOL B 704 6
HET GOL B 705 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM ADE ADENINE
HETNAM GOL GLYCEROL
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 4 FUC 2(C6 H12 O5)
FORMUL 6 ADE C5 H5 N5
FORMUL 7 GOL 8(C3 H8 O3)
FORMUL 20 HOH *503(H2 O)
HELIX 1 1 THR A 13 VAL A 28 1 16
HELIX 2 2 GLY A 95 GLN A 99 5 5
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 HIS A 208 1 20
HELIX 10 10 ARG A 234 VAL A 236 5 3
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 GLN B 419 5 4
HELIX 18 18 SER B 459 GLN B 462 5 4
HELIX 19 19 GLN B 485 GLN B 491 5 7
HELIX 20 20 ASN B 501 MET B 505 5 5
SHEET 1 A 6 GLU A 2 THR A 8 0
SHEET 2 A 6 PHE A 53 ASN A 60 1 O LEU A 55 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 ALA A 79 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 SER A 107 N PHE A 88
SHEET 1 B 2 SER A 29 SER A 34 0
SHEET 2 B 2 ILE A 37 LEU A 40 -1 O ILE A 37 N SER A 34
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 226 N ILE A 222
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 ASP B 327 -1 O PHE B 326 N CYS B 311
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 TRP B 421 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 ILE B 494 N ASP B 482
SSBOND 1 CYS A 247 CYS B 252 1555 1555 2.04
SSBOND 2 CYS B 311 CYS B 328 1555 1555 2.08
SSBOND 3 CYS B 399 CYS B 412 1555 1555 2.08
SSBOND 4 CYS B 438 CYS B 455 1555 1555 2.04
LINK ND2 ASN B 383 C1 NAG B 603 1555 1555 1.61
CRYST1 107.120 107.120 309.820 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 0.009335 0.005390 0.000000 0.00000
SCALE2 0.000000 0.010780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003228 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
