HEADER TRANSFERASE 29-SEP-15 5E1B
TITLE CRYSTAL STRUCTURE OF NRMT1 IN COMPLEX WITH SPKRIA 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_PLASMID: PET28A-LIC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
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 4 27-SEP-23 5E1B 1 JRNL REMARK
REVDAT 3 02-DEC-15 5E1B 1 JRNL
REVDAT 2 18-NOV-15 5E1B 1 JRNL
REVDAT 1 28-OCT-15 5E1B 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. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 80997
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3324
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5866
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 236
REMARK 3 BIN FREE R VALUE : 0.2220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 130
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.02000
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.274
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3974 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3775 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5409 ; 1.815 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8717 ; 1.040 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 510 ; 6.182 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;36.740 ;23.187
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 693 ;11.088 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;18.522 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 606 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4487 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 907 ; 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): 1925 ; 0.517 ; 0.682
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1924 ; 0.512 ; 0.680
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2412 ; 0.878 ; 1.018
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): 16.1451 31.6356 -14.4660
REMARK 3 T TENSOR
REMARK 3 T11: 0.0433 T22: 0.0139
REMARK 3 T33: 0.0043 T12: 0.0168
REMARK 3 T13: 0.0075 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.9712 L22: 0.8877
REMARK 3 L33: 1.6274 L12: -0.2087
REMARK 3 L13: 0.0849 L23: -0.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0492 S12: -0.0271 S13: -0.0141
REMARK 3 S21: 0.0731 S22: 0.0217 S23: 0.0433
REMARK 3 S31: -0.0605 S32: -0.1027 S33: 0.0275
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 -2 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8357 38.8117 14.2247
REMARK 3 T TENSOR
REMARK 3 T11: 0.1039 T22: 0.0531
REMARK 3 T33: 0.0365 T12: 0.0277
REMARK 3 T13: 0.0413 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.7626 L22: 1.5069
REMARK 3 L33: 1.6010 L12: -0.9721
REMARK 3 L13: -0.7647 L23: 0.3576
REMARK 3 S TENSOR
REMARK 3 S11: -0.1351 S12: -0.1070 S13: -0.1810
REMARK 3 S21: 0.1707 S22: 0.0679 S23: 0.1278
REMARK 3 S31: 0.1855 S32: 0.0552 S33: 0.0672
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. MOLPROBITY WAS USED FOR GEOMETRY VALIDATION.
REMARK 4
REMARK 4 5E1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92380
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.70
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.80
REMARK 200 R MERGE FOR SHELL (I) : 1.21300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDBID 2EX4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
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 136.94400
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 68.47200
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 102.70800
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 34.23600
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 171.18000
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 136.94400
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 68.47200
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 34.23600
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 102.70800
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 171.18000
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: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10320 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: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 47 CE NZ
REMARK 470 LYS A 59 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 GLN A 171 OE1 NE2
REMARK 470 ARG B -1 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 4 OE1 OE2
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 ARG B 85 CD NE CZ NH1 NH2
REMARK 470 LYS B 154 CE NZ
REMARK 470 ARG B 158 NH1 NH2
REMARK 470 GLN B 171 CG CD OE1 NE2
REMARK 470 ASP B 178 OD1 OD2
REMARK 470 ILE E 5 CG1 CD1
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 SG CYS A 195 UNK UNX A 326 2.04
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 A 1 CB SER A 1 OG -0.099
REMARK 500 CYS A 117 CB CYS A 117 SG -0.124
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 8 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 178 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = -4.7 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 -77.78 -91.72
REMARK 500 VAL A 137 -14.14 -147.23
REMARK 500 SER A 181 67.79 64.94
REMARK 500 ASN B 58 62.44 -110.65
REMARK 500 VAL B 137 -16.27 -146.70
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 GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
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: 5E2B RELATED DB: PDB
REMARK 900 RELATED ID: 5E1O RELATED DB: PDB
DBREF 5E1B A 2 223 UNP Q9BV86 NTM1A_HUMAN 2 223
DBREF 5E1B B 2 223 UNP Q9BV86 NTM1A_HUMAN 2 223
DBREF 5E1B D 1 6 PDB 5E1B 5E1B 1 6
DBREF 5E1B E 1 6 PDB 5E1B 5E1B 1 6
SEQADV 5E1B MET A -17 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY A -16 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER A -15 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER A -14 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -13 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -12 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -11 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -10 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -9 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS A -8 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER A -7 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER A -6 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY A -5 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B LEU A -4 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B VAL A -3 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B PRO A -2 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B ARG A -1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY A 0 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER A 1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B MET B -17 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY B -16 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER B -15 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER B -14 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -13 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -12 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -11 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -10 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -9 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B HIS B -8 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER B -7 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B SER B -6 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY B -5 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B LEU B -4 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B VAL B -3 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B PRO B -2 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B ARG B -1 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B GLY B 0 UNP Q9BV86 EXPRESSION TAG
SEQADV 5E1B 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 SER PRO LYS ARG ILE ALA
SEQRES 1 E 6 SER PRO LYS ARG ILE ALA
HET SAH A 301 26
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
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 SAH B 301 26
HET GOL B 302 6
HET UNX B 303 1
HET UNX B 304 1
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 B 324 1
HET UNX B 325 1
HET UNX B 326 1
HET UNX B 327 1
HET UNX B 328 1
HET UNX B 329 1
HET UNX D 101 1
HET UNX E 101 1
HET UNX E 102 1
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM GOL GLYCEROL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SAH 2(C14 H20 N6 O5 S)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 9 UNX 54(X)
FORMUL 65 HOH *436(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 PHE A 52 ARG A 54 5 3
HELIX 7 AA7 GLY A 73 LEU A 79 1 7
HELIX 8 AA8 THR A 93 LEU A 104 1 12
HELIX 9 AA9 GLY A 105 LYS A 109 5 5
HELIX 10 AB1 GLY A 118 PHE A 122 5 5
HELIX 11 AB2 VAL A 137 LEU A 141 5 5
HELIX 12 AB3 THR A 142 SER A 156 1 15
HELIX 13 AB4 LEU A 187 ALA A 197 1 11
HELIX 14 AB5 SER B 1 ILE B 6 1 6
HELIX 15 AB6 ASP B 8 GLN B 22 1 15
HELIX 16 AB7 THR B 26 LEU B 31 1 6
HELIX 17 AB8 TYR B 34 HIS B 36 5 3
HELIX 18 AB9 ILE B 37 GLU B 55 1 19
HELIX 19 AC1 GLY B 73 LEU B 79 1 7
HELIX 20 AC2 THR B 93 LEU B 104 1 12
HELIX 21 AC3 GLY B 105 LYS B 109 5 5
HELIX 22 AC4 GLY B 118 PHE B 122 5 5
HELIX 23 AC5 VAL B 137 LEU B 141 5 5
HELIX 24 AC6 THR B 142 SER B 156 1 15
HELIX 25 AC7 ASP B 186 ALA B 197 1 12
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 CYS A 68
SHEET 5 AA1 7 LEU A 157 ALA A 170 1 O VAL A 164 N ILE A 132
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 CYS A 68
SHEET 5 AA2 7 LEU A 157 ALA A 170 1 O VAL A 164 N ILE A 132
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 MET B 169 1 O VAL B 164 N ILE B 132
SHEET 6 AA3 7 HIS B 216 ARG B 223 -1 O LEU B 222 N ILE B 163
SHEET 7 AA3 7 SER B 200 ARG B 206 -1 N LEU B 202 O ALA B 221
SHEET 1 AA4 2 VAL B 174 ASP B 177 0
SHEET 2 AA4 2 SER B 182 ARG B 185 -1 O SER B 182 N ASP B 177
CISPEP 1 GLY B 56 PRO B 57 0 0.17
CISPEP 2 GLY B 56 PRO B 57 0 7.27
SITE 1 AC1 20 TRP A 20 MET A 30 GLY A 69 GLY A 71
SITE 2 AC1 20 ARG A 74 ILE A 75 ASP A 91 ILE A 92
SITE 3 AC1 20 THR A 93 PHE A 96 GLY A 118 LEU A 119
SITE 4 AC1 20 GLN A 120 GLN A 135 TRP A 136 VAL A 137
SITE 5 AC1 20 HIS A 140 HOH A 439 HOH A 520 HOH A 525
SITE 1 AC2 8 TYR A 19 ASP A 177 VAL A 179 HOH A 433
SITE 2 AC2 8 HOH A 452 HOH A 458 LYS D 3 HOH D 202
SITE 1 AC3 6 GLU A 86 ARG A 112 HOH A 436 HOH A 442
SITE 2 AC3 6 HOH A 500 ARG B 46
SITE 1 AC4 10 TRP A 136 VAL A 137 ILE A 138 GLY A 139
SITE 2 AC4 10 ASP A 167 ASN A 168 VAL A 183 HOH A 426
SITE 3 AC4 10 HOH A 444 SER D 1
SITE 1 AC5 21 TRP B 20 MET B 30 GLY B 69 GLY B 71
SITE 2 AC5 21 ARG B 74 ILE B 75 ASP B 91 ILE B 92
SITE 3 AC5 21 THR B 93 PHE B 96 CYS B 117 GLY B 118
SITE 4 AC5 21 LEU B 119 GLN B 120 GLN B 135 TRP B 136
SITE 5 AC5 21 VAL B 137 HIS B 140 HOH B 444 HOH B 479
SITE 6 AC5 21 HOH B 486
SITE 1 AC6 11 TRP B 136 VAL B 137 ILE B 138 GLY B 139
SITE 2 AC6 11 ASP B 167 ASN B 168 VAL B 183 CYS B 184
SITE 3 AC6 11 HOH B 407 HOH B 422 SER E 1
CRYST1 107.259 107.259 205.416 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 0.009323 0.005383 0.000000 0.00000
SCALE2 0.000000 0.010766 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004868 0.00000
(ATOM LINES ARE NOT SHOWN.)
END