HEADER TRANSFERASE 30-SEP-15 5E2B
TITLE CRYSTAL STRUCTURE OF NTMT1 IN COMPLEX WITH N-TERMINALLY METHYLATED
TITLE 2 PPKRIA PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-TERMINAL XAA-PRO-LYS N-METHYLTRANSFERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1A,
COMPND 5 METHYLTRANSFERASE-LIKE PROTEIN 11A,N-TERMINAL RCC1 METHYLTRANSFERASE,
COMPND 6 X-PRO-LYS N-TERMINAL PROTEIN METHYLTRANSFERASE 1A,NTM1A;
COMPND 7 EC: 2.1.1.244;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RCC1;
COMPND 11 CHAIN: D, E;
COMPND 12 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: NTMT1, C9ORF32, METTL11A, NRMT, NRMT1, AD-003;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V3R;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS TRANSFERASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DONG,W.TEMPEL,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (SGC)
REVDAT 3 02-DEC-15 5E2B 1 JRNL
REVDAT 2 18-NOV-15 5E2B 1 JRNL
REVDAT 1 28-OCT-15 5E2B 0
JRNL AUTH C.DONG,Y.MAO,W.TEMPEL,S.QIN,L.LI,P.LOPPNAU,R.HUANG,J.MIN
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY THE HUMAN
JRNL TITL 2 N-TERMINAL METHYLTRANSFERASE 1.
JRNL REF GENES DEV. V. 29 2343 2015
JRNL REFN ISSN 0890-9369
JRNL PMID 26543161
JRNL DOI 10.1101/GAD.270611.115
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 49282
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2019
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3488
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.1630
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 385
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.07000
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): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.148
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3948 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3725 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5381 ; 1.766 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8592 ; 1.339 ; 3.005
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 503 ; 6.172 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;37.292 ;23.516
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 675 ;12.196 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;18.934 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 600 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4470 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 893 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1922 ; 0.539 ; 0.857
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1921 ; 0.533 ; 0.854
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2407 ; 0.913 ; 1.276
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -3 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1550 31.6861 -14.5341
REMARK 3 T TENSOR
REMARK 3 T11: 0.0334 T22: 0.0117
REMARK 3 T33: 0.0080 T12: 0.0116
REMARK 3 T13: 0.0139 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.1342 L22: 1.0286
REMARK 3 L33: 1.9583 L12: -0.1643
REMARK 3 L13: 0.1286 L23: -0.1605
REMARK 3 S TENSOR
REMARK 3 S11: -0.0559 S12: -0.0287 S13: -0.0157
REMARK 3 S21: 0.1013 S22: 0.0326 S23: 0.0606
REMARK 3 S31: -0.0786 S32: -0.1431 S33: 0.0233
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -1 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8214 38.8316 14.2835
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.0337
REMARK 3 T33: 0.0432 T12: 0.0362
REMARK 3 T13: 0.0500 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 2.0431 L22: 1.6554
REMARK 3 L33: 1.7670 L12: -1.0370
REMARK 3 L13: -0.9242 L23: 0.4079
REMARK 3 S TENSOR
REMARK 3 S11: -0.1670 S12: -0.1366 S13: -0.2013
REMARK 3 S21: 0.1829 S22: 0.0883 S23: 0.1156
REMARK 3 S31: 0.2304 S32: 0.0823 S33: 0.0787
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: COOT WAS USED FOR INTERACTIVE MODEL
REMARK 3 BUILDING. PRODRG WAS USED TO PREPARE REFINEMENT RESTRAINTS.
REMARK 3 MOLPROBITY WAS USED FOR GEOMETRY VALIDATION.
REMARK 4
REMARK 4 5E2B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64736
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 21.10
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.10
REMARK 200 R MERGE FOR SHELL (I) : 1.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: ISOMORPHOUS STRUCTURE OF NTMT1 IN COMPLEX WITH
REMARK 200 DIFFERENT PEPTIDE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG3350, 16% TACSIMATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 137.06933
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 68.53467
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 102.80200
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 34.26733
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 171.33667
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 137.06933
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 68.53467
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 34.26733
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 102.80200
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 171.33667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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 MET A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 SER A -7
REMARK 465 SER A -6
REMARK 465 GLY A -5
REMARK 465 LEU A -4
REMARK 465 MET B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 SER B -7
REMARK 465 SER B -6
REMARK 465 GLY B -5
REMARK 465 LEU B -4
REMARK 465 VAL B -3
REMARK 465 PRO B -2
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 VAL A -3 CG1 CG2
REMARK 470 LYS A 10 CD CE NZ
REMARK 470 LYS A 15 CE NZ
REMARK 470 LYS A 47 CE NZ
REMARK 470 LYS A 59 CE NZ
REMARK 470 ARG A 85 CD NE CZ NH1 NH2
REMARK 470 LYS A 101 CD CE NZ
REMARK 470 LYS A 109 CD CE NZ
REMARK 470 ARG A 158 CZ NH1 NH2
REMARK 470 ARG B -1 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 7 CG CD OE1 OE2
REMARK 470 LYS B 10 CD CE NZ
REMARK 470 LYS B 15 NZ
REMARK 470 LYS B 21 NZ
REMARK 470 LYS B 77 NZ
REMARK 470 ARG B 85 CD NE CZ NH1 NH2
REMARK 470 LYS B 101 CD CE NZ
REMARK 470 GLU B 125 OE1 OE2
REMARK 470 LYS B 154 CE NZ
REMARK 470 GLN B 171 CD OE1 NE2
REMARK 470 ARG E 4 CG CD NE CZ NH1 NH2
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 OE1 GLU A 9 UNK UNX A 307 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 ARG B 158 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 186 CB - CG - OD1 ANGL. DEV. = 7.2 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 ARG A 112 -76.61 -93.08
REMARK 500 VAL A 137 -17.22 -147.92
REMARK 500 SER A 181 66.55 60.51
REMARK 500 ASN B 58 63.65 -107.16
REMARK 500 VAL B 137 -17.41 -148.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E1D RELATED DB: PDB
REMARK 900 RELATED ID: 5E2A RELATED DB: PDB
REMARK 900 RELATED ID: 5E1M RELATED DB: PDB
REMARK 900 RELATED ID: 5E1O RELATED DB: PDB
REMARK 900 RELATED ID: 5E1B RELATED DB: PDB
DBREF 5E2B A 2 223 UNP Q9BV86 NTM1A_HUMAN 2 223
DBREF 5E2B B 2 223 UNP Q9BV86 NTM1A_HUMAN 2 223
DBREF 5E2B D 1 6 PDB 5E2B 5E2B 1 6
DBREF 5E2B E 1 6 PDB 5E2B 5E2B 1 6
SEQADV 5E2B MET A -17 UNP Q9BV86 INITIATING METHIONINE
SEQADV 5E2B GLY A -16 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER A -15 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER A -14 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -13 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -12 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -11 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -10 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -9 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS A -8 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER A -7 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER A -6 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B GLY A -5 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B LEU A -4 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B VAL A -3 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B PRO A -2 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B ARG A -1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B GLY A 0 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER A 1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B MET B -17 UNP Q9BV86 INITIATING METHIONINE
SEQADV 5E2B GLY B -16 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER B -15 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER B -14 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -13 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -12 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -11 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -10 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -9 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B HIS B -8 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER B -7 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER B -6 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B GLY B -5 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B LEU B -4 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B VAL B -3 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B PRO B -2 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B ARG B -1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B GLY B 0 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E2B SER B 1 UNP Q9BV86 EXPRESSION TAG
SEQRES 1 A 241 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 241 LEU VAL PRO ARG GLY SER THR SER GLU VAL ILE GLU ASP
SEQRES 3 A 241 GLU LYS GLN PHE TYR SER LYS ALA LYS THR TYR TRP LYS
SEQRES 4 A 241 GLN ILE PRO PRO THR VAL ASP GLY MET LEU GLY GLY TYR
SEQRES 5 A 241 GLY HIS ILE SER SER ILE ASP ILE ASN SER SER ARG LYS
SEQRES 6 A 241 PHE LEU GLN ARG PHE LEU ARG GLU GLY PRO ASN LYS THR
SEQRES 7 A 241 GLY THR SER CYS ALA LEU ASP CYS GLY ALA GLY ILE GLY
SEQRES 8 A 241 ARG ILE THR LYS ARG LEU LEU LEU PRO LEU PHE ARG GLU
SEQRES 9 A 241 VAL ASP MET VAL ASP ILE THR GLU ASP PHE LEU VAL GLN
SEQRES 10 A 241 ALA LYS THR TYR LEU GLY GLU GLU GLY LYS ARG VAL ARG
SEQRES 11 A 241 ASN TYR PHE CYS CYS GLY LEU GLN ASP PHE THR PRO GLU
SEQRES 12 A 241 PRO ASP SER TYR ASP VAL ILE TRP ILE GLN TRP VAL ILE
SEQRES 13 A 241 GLY HIS LEU THR ASP GLN HIS LEU ALA GLU PHE LEU ARG
SEQRES 14 A 241 ARG CYS LYS GLY SER LEU ARG PRO ASN GLY ILE ILE VAL
SEQRES 15 A 241 ILE LYS ASP ASN MET ALA GLN GLU GLY VAL ILE LEU ASP
SEQRES 16 A 241 ASP VAL ASP SER SER VAL CYS ARG ASP LEU ASP VAL VAL
SEQRES 17 A 241 ARG ARG ILE ILE CYS SER ALA GLY LEU SER LEU LEU ALA
SEQRES 18 A 241 GLU GLU ARG GLN GLU ASN LEU PRO ASP GLU ILE TYR HIS
SEQRES 19 A 241 VAL TYR SER PHE ALA LEU ARG
SEQRES 1 B 241 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 241 LEU VAL PRO ARG GLY SER THR SER GLU VAL ILE GLU ASP
SEQRES 3 B 241 GLU LYS GLN PHE TYR SER LYS ALA LYS THR TYR TRP LYS
SEQRES 4 B 241 GLN ILE PRO PRO THR VAL ASP GLY MET LEU GLY GLY TYR
SEQRES 5 B 241 GLY HIS ILE SER SER ILE ASP ILE ASN SER SER ARG LYS
SEQRES 6 B 241 PHE LEU GLN ARG PHE LEU ARG GLU GLY PRO ASN LYS THR
SEQRES 7 B 241 GLY THR SER CYS ALA LEU ASP CYS GLY ALA GLY ILE GLY
SEQRES 8 B 241 ARG ILE THR LYS ARG LEU LEU LEU PRO LEU PHE ARG GLU
SEQRES 9 B 241 VAL ASP MET VAL ASP ILE THR GLU ASP PHE LEU VAL GLN
SEQRES 10 B 241 ALA LYS THR TYR LEU GLY GLU GLU GLY LYS ARG VAL ARG
SEQRES 11 B 241 ASN TYR PHE CYS CYS GLY LEU GLN ASP PHE THR PRO GLU
SEQRES 12 B 241 PRO ASP SER TYR ASP VAL ILE TRP ILE GLN TRP VAL ILE
SEQRES 13 B 241 GLY HIS LEU THR ASP GLN HIS LEU ALA GLU PHE LEU ARG
SEQRES 14 B 241 ARG CYS LYS GLY SER LEU ARG PRO ASN GLY ILE ILE VAL
SEQRES 15 B 241 ILE LYS ASP ASN MET ALA GLN GLU GLY VAL ILE LEU ASP
SEQRES 16 B 241 ASP VAL ASP SER SER VAL CYS ARG ASP LEU ASP VAL VAL
SEQRES 17 B 241 ARG ARG ILE ILE CYS SER ALA GLY LEU SER LEU LEU ALA
SEQRES 18 B 241 GLU GLU ARG GLN GLU ASN LEU PRO ASP GLU ILE TYR HIS
SEQRES 19 B 241 VAL TYR SER PHE ALA LEU ARG
SEQRES 1 D 6 3BY PRO LYS ARG ILE ALA
SEQRES 1 E 6 3BY PRO LYS ARG ILE ALA
HET 3BY D 1 16
HET 3BY E 1 16
HET SAH A 301 26
HET GOL A 302 6
HET GOL A 303 6
HET UNX A 304 1
HET UNX A 305 1
HET UNX A 306 1
HET UNX A 307 1
HET UNX A 308 1
HET UNX A 309 1
HET UNX A 310 1
HET UNX A 311 1
HET UNX A 312 1
HET UNX A 313 1
HET UNX A 314 1
HET UNX A 315 1
HET UNX A 316 1
HET UNX A 317 1
HET UNX A 318 1
HET UNX A 319 1
HET UNX A 320 1
HET UNX A 321 1
HET UNX A 322 1
HET UNX A 323 1
HET UNX A 324 1
HET UNX A 325 1
HET UNX A 326 1
HET UNX A 327 1
HET UNX A 328 1
HET UNX A 329 1
HET SAH B 301 26
HET UNX B 302 1
HET UNX B 303 1
HET UNX B 304 2
HET UNX B 305 1
HET UNX B 306 1
HET UNX B 307 1
HET UNX B 308 1
HET UNX B 309 1
HET UNX B 310 1
HET UNX B 311 1
HET UNX B 312 1
HET UNX B 313 1
HET UNX B 314 1
HET UNX B 315 1
HET UNX B 316 1
HET UNX B 317 1
HET UNX B 318 1
HET UNX B 319 1
HET UNX B 320 1
HET UNX B 321 1
HET UNX B 322 1
HET UNX B 323 1
HET UNX D 101 1
HET UNX E 101 1
HETNAM 3BY 1-METHYL-L-PROLINE
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM GOL GLYCEROL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 3BY 2(C6 H11 N O2)
FORMUL 5 SAH 2(C14 H20 N6 O5 S)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 UNX 50(X)
FORMUL 59 HOH *385(H2 O)
HELIX 1 AA1 SER A 1 VAL A 5 5 5
HELIX 2 AA2 ASP A 8 GLN A 22 1 15
HELIX 3 AA3 THR A 26 LEU A 31 1 6
HELIX 4 AA4 TYR A 34 HIS A 36 5 3
HELIX 5 AA5 ILE A 37 ARG A 51 1 15
HELIX 6 AA6 GLY A 73 LEU A 79 1 7
HELIX 7 AA7 THR A 93 LEU A 104 1 12
HELIX 8 AA8 GLY A 105 LYS A 109 5 5
HELIX 9 AA9 GLY A 118 PHE A 122 5 5
HELIX 10 AB1 VAL A 137 LEU A 141 5 5
HELIX 11 AB2 THR A 142 SER A 156 1 15
HELIX 12 AB3 LEU A 187 ALA A 197 1 11
HELIX 13 AB4 SER B 1 ILE B 6 1 6
HELIX 14 AB5 ASP B 8 GLN B 22 1 15
HELIX 15 AB6 THR B 26 LEU B 31 1 6
HELIX 16 AB7 TYR B 34 HIS B 36 5 3
HELIX 17 AB8 ILE B 37 GLU B 55 1 19
HELIX 18 AB9 GLY B 73 LEU B 79 1 7
HELIX 19 AC1 THR B 93 LEU B 104 1 12
HELIX 20 AC2 GLY B 105 LYS B 109 5 5
HELIX 21 AC3 GLY B 118 PHE B 122 5 5
HELIX 22 AC4 VAL B 137 LEU B 141 5 5
HELIX 23 AC5 THR B 142 SER B 156 1 15
HELIX 24 AC6 LEU B 187 ALA B 197 1 11
SHEET 1 AA1 7 VAL A 111 CYS A 116 0
SHEET 2 AA1 7 GLU A 86 ASP A 91 1 N MET A 89 O PHE A 115
SHEET 3 AA1 7 CYS A 64 CYS A 68 1 N ASP A 67 O ASP A 88
SHEET 4 AA1 7 TYR A 129 GLN A 135 1 O TRP A 133 N LEU A 66
SHEET 5 AA1 7 LEU A 157 ALA A 170 1 O VAL A 164 N ILE A 134
SHEET 6 AA1 7 SER A 182 ASP A 186 1 O ARG A 185 N ALA A 170
SHEET 7 AA1 7 VAL A 174 ASP A 177 -1 N ASP A 177 O SER A 182
SHEET 1 AA2 7 VAL A 111 CYS A 116 0
SHEET 2 AA2 7 GLU A 86 ASP A 91 1 N MET A 89 O PHE A 115
SHEET 3 AA2 7 CYS A 64 CYS A 68 1 N ASP A 67 O ASP A 88
SHEET 4 AA2 7 TYR A 129 GLN A 135 1 O TRP A 133 N LEU A 66
SHEET 5 AA2 7 LEU A 157 ALA A 170 1 O VAL A 164 N ILE A 134
SHEET 6 AA2 7 HIS A 216 ARG A 223 -1 O LEU A 222 N ILE A 163
SHEET 7 AA2 7 SER A 200 ARG A 206 -1 N LEU A 202 O ALA A 221
SHEET 1 AA3 7 VAL B 111 CYS B 116 0
SHEET 2 AA3 7 GLU B 86 ASP B 91 1 N MET B 89 O PHE B 115
SHEET 3 AA3 7 CYS B 64 CYS B 68 1 N ASP B 67 O ASP B 88
SHEET 4 AA3 7 TYR B 129 GLN B 135 1 O TRP B 133 N CYS B 68
SHEET 5 AA3 7 LEU B 157 ALA B 170 1 O VAL B 164 N ILE B 132
SHEET 6 AA3 7 SER B 182 ASP B 186 1 O ARG B 185 N ALA B 170
SHEET 7 AA3 7 VAL B 174 ASP B 177 -1 N ASP B 177 O SER B 182
SHEET 1 AA4 7 VAL B 111 CYS B 116 0
SHEET 2 AA4 7 GLU B 86 ASP B 91 1 N MET B 89 O PHE B 115
SHEET 3 AA4 7 CYS B 64 CYS B 68 1 N ASP B 67 O ASP B 88
SHEET 4 AA4 7 TYR B 129 GLN B 135 1 O TRP B 133 N CYS B 68
SHEET 5 AA4 7 LEU B 157 ALA B 170 1 O VAL B 164 N ILE B 132
SHEET 6 AA4 7 HIS B 216 ARG B 223 -1 O LEU B 222 N ILE B 163
SHEET 7 AA4 7 SER B 200 ARG B 206 -1 N LEU B 202 O ALA B 221
LINK C A3BY D 1 N PRO D 2 1555 1555 1.35
LINK C B3BY D 1 N PRO D 2 1555 1555 1.36
LINK C A3BY E 1 N PRO E 2 1555 1555 1.34
LINK C B3BY E 1 N PRO E 2 1555 1555 1.35
CISPEP 1 GLY B 56 PRO B 57 0 -1.85
CISPEP 2 GLY B 56 PRO B 57 0 9.52
SITE 1 AC1 21 TRP A 20 MET A 30 GLY A 69 GLY A 71
SITE 2 AC1 21 ARG A 74 ILE A 75 ASP A 91 ILE A 92
SITE 3 AC1 21 THR A 93 PHE A 96 GLY A 118 LEU A 119
SITE 4 AC1 21 GLN A 120 GLN A 135 TRP A 136 VAL A 137
SITE 5 AC1 21 HIS A 140 HOH A 424 HOH A 467 HOH A 538
SITE 6 AC1 21 3BY D 1
SITE 1 AC2 7 HIS A 36 ILE A 37 HOH A 411 HOH A 489
SITE 2 AC2 7 TYR B 19 GLY B 32 HOH B 463
SITE 1 AC3 5 GLU A 86 ARG A 112 HOH A 436 HOH A 501
SITE 2 AC3 5 ARG B 46
SITE 1 AC4 21 TRP B 20 MET B 30 GLY B 69 GLY B 71
SITE 2 AC4 21 ARG B 74 ILE B 75 ASP B 91 ILE B 92
SITE 3 AC4 21 THR B 93 PHE B 96 GLY B 118 LEU B 119
SITE 4 AC4 21 GLN B 120 GLN B 135 TRP B 136 VAL B 137
SITE 5 AC4 21 HIS B 140 HOH B 437 HOH B 473 HOH B 493
SITE 6 AC4 21 3BY E 1
CRYST1 107.268 107.268 205.604 90.00 90.00 120.00 P 65 2 2 24
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 0.009322 0.005382 0.000000 0.00000
SCALE2 0.000000 0.010765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004864 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
