HEADER LYASE 16-JAN-06 2FPC
TITLE STRUCTURE OF STRICTOSIDINE SYNTHASE, THE BIOSYNTHETIC ENTRY TO THE
TITLE 2 MONOTERPENOID INDOLE ALKALOID FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRICTOSIDINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.3.3.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;
SOURCE 3 ORGANISM_COMMON: SERPENTWOOD;
SOURCE 4 ORGANISM_TAXID: 4060;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE-2
KEYWDS SIX BLADED BETA PROPELLER FOLD, STR1, SYNTHASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PANJIKAR
REVDAT 6 03-APR-24 2FPC 1 HETSYN
REVDAT 5 29-JUL-20 2FPC 1 COMPND REMARK HETNAM SITE
REVDAT 5 2 1 ATOM
REVDAT 4 18-OCT-17 2FPC 1 REMARK
REVDAT 3 13-JUL-11 2FPC 1 VERSN
REVDAT 2 24-FEB-09 2FPC 1 VERSN
REVDAT 1 23-MAY-06 2FPC 0
JRNL AUTH X.MA,S.PANJIKAR,J.KOEPKE,E.LORIS,J.STOCKIGT
JRNL TITL THE STRUCTURE OF RAUVOLFIA SERPENTINA STRICTOSIDINE SYNTHASE
JRNL TITL 2 IS A NOVEL SIX-BLADED BETA-PROPELLER FOLD IN PLANT PROTEINS
JRNL REF PLANT CELL V. 18 907 2006
JRNL REFN ISSN 1040-4651
JRNL PMID 16531499
JRNL DOI 10.1105/TPC.105.038018
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 19104
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 787
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1372
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4764
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 50.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.62000
REMARK 3 B22 (A**2) : 4.62000
REMARK 3 B33 (A**2) : -6.93000
REMARK 3 B12 (A**2) : 2.31000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.371
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.255
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.451
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4952 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6740 ; 1.833 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 602 ; 7.145 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 734 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3812 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2993 ; 0.256 ; 0.200
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): 320 ; 0.196 ; 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): 36 ; 0.273 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.104 ; 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): 2996 ; 0.685 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4850 ; 1.346 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1956 ; 3.464 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1890 ; 5.524 ;10.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 35 A 331 2
REMARK 3 1 B 35 B 331 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1188 ; 0.08 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1149 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1188 ; 0.56 ; 1.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1149 ; 1.49 ; 2.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1001 A 1001 2
REMARK 3 1 B 2001 B 2001 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 27 ; 0.12 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 27 ; 4.72 ; 2.50
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 32 A 333
REMARK 3 ORIGIN FOR THE GROUP (A): 94.9327 8.8336 0.1442
REMARK 3 T TENSOR
REMARK 3 T11: 0.0158 T22: 0.0832
REMARK 3 T33: 0.1756 T12: 0.0362
REMARK 3 T13: 0.0057 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 2.0230 L22: 1.1925
REMARK 3 L33: 5.0175 L12: 0.5350
REMARK 3 L13: -0.3015 L23: 0.2264
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: 0.1167 S13: 0.0065
REMARK 3 S21: -0.0500 S22: 0.1362 S23: 0.1868
REMARK 3 S31: -0.2123 S32: -0.3754 S33: -0.0683
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 32 B 333
REMARK 3 ORIGIN FOR THE GROUP (A): 129.5683 34.2319 10.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2504 T22: 0.1865
REMARK 3 T33: 0.3127 T12: -0.0709
REMARK 3 T13: 0.0251 T23: 0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 5.7788 L22: 1.5035
REMARK 3 L33: 5.4473 L12: 1.2411
REMARK 3 L13: -2.4898 L23: -0.0548
REMARK 3 S TENSOR
REMARK 3 S11: 0.1075 S12: -0.3728 S13: 0.5501
REMARK 3 S21: 0.0544 S22: -0.0222 S23: -0.0816
REMARK 3 S31: -0.3606 S32: 0.6687 S33: -0.0853
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8057
REMARK 200 MONOCHROMATOR : SILICON 111
REMARK 200 OPTICS : DOUBLE CRYSTAL SI[111]
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19104
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
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: MOLREP
REMARK 200 STARTING MODEL: NATIVE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE, 100MM HEPES-NA, 2MM SECOLOGANIN, PH 7.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.30350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.89915
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.35633
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 74.30350
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 42.89915
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.35633
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 74.30350
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 42.89915
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.35633
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 85.79829
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 80.71267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 85.79829
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 80.71267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 85.79829
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 80.71267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 LEU A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 PRO A 29
REMARK 465 ILE A 30
REMARK 465 LEU A 31
REMARK 465 ASP A 334
REMARK 465 LYS A 335
REMARK 465 LYS A 336
REMARK 465 GLY A 337
REMARK 465 ASN A 338
REMARK 465 SER A 339
REMARK 465 PHE A 340
REMARK 465 VAL A 341
REMARK 465 SER A 342
REMARK 465 SER A 343
REMARK 465 HIS A 344
REMARK 465 SER B 23
REMARK 465 LEU B 24
REMARK 465 ALA B 25
REMARK 465 LEU B 26
REMARK 465 SER B 27
REMARK 465 SER B 28
REMARK 465 PRO B 29
REMARK 465 ILE B 30
REMARK 465 LEU B 31
REMARK 465 ASP B 334
REMARK 465 LYS B 335
REMARK 465 LYS B 336
REMARK 465 GLY B 337
REMARK 465 ASN B 338
REMARK 465 SER B 339
REMARK 465 PHE B 340
REMARK 465 VAL B 341
REMARK 465 SER B 342
REMARK 465 SER B 343
REMARK 465 HIS B 344
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 O SER B 327 O HOH B 2033 2.14
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 MET A 180 SD MET A 180 CE 0.433
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 106 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 193 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 288 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 63 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP B 94 CB - CG - OD2 ANGL. DEV. = 5.7 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 SER A 40 -132.37 46.64
REMARK 500 PHE A 77 -58.73 -128.80
REMARK 500 ASN A 91 17.42 55.46
REMARK 500 ARG A 103 107.18 -165.48
REMARK 500 HIS A 124 -142.58 45.31
REMARK 500 ASP A 143 27.96 45.41
REMARK 500 TRP A 149 85.17 -153.48
REMARK 500 TYR A 151 -57.15 -126.85
REMARK 500 ASP A 172 -166.22 -106.85
REMARK 500 VAL A 208 67.57 67.53
REMARK 500 SER A 269 62.13 -108.23
REMARK 500 PRO A 302 31.01 -94.44
REMARK 500 PRO B 39 -179.91 -67.90
REMARK 500 SER B 40 -124.02 43.91
REMARK 500 PHE B 77 -66.65 -123.24
REMARK 500 ARG B 103 112.90 -164.93
REMARK 500 ASN B 114 66.45 36.00
REMARK 500 HIS B 124 -153.02 52.23
REMARK 500 ASP B 143 25.12 44.02
REMARK 500 TRP B 149 89.44 -151.11
REMARK 500 TYR B 151 -51.86 -122.31
REMARK 500 ASP B 172 -166.49 -111.14
REMARK 500 ASP B 173 -41.83 -22.47
REMARK 500 LYS B 185 59.59 -119.24
REMARK 500 VAL B 208 72.70 62.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FP8 RELATED DB: PDB
REMARK 900 RELATED ID: 2FP9 RELATED DB: PDB
REMARK 900 RELATED ID: 2FPB RELATED DB: PDB
DBREF 2FPC A 23 344 UNP P68175 STSY_RAUSE 23 344
DBREF 2FPC B 23 344 UNP P68175 STSY_RAUSE 23 344
SEQRES 1 A 322 SER LEU ALA LEU SER SER PRO ILE LEU LYS GLU ILE LEU
SEQRES 2 A 322 ILE GLU ALA PRO SER TYR ALA PRO ASN SER PHE THR PHE
SEQRES 3 A 322 ASP SER THR ASN LYS GLY PHE TYR THR SER VAL GLN ASP
SEQRES 4 A 322 GLY ARG VAL ILE LYS TYR GLU GLY PRO ASN SER GLY PHE
SEQRES 5 A 322 VAL ASP PHE ALA TYR ALA SER PRO TYR TRP ASN LYS ALA
SEQRES 6 A 322 PHE CYS GLU ASN SER THR ASP ALA GLU LYS ARG PRO LEU
SEQRES 7 A 322 CYS GLY ARG THR TYR ASP ILE SER TYR ASN LEU GLN ASN
SEQRES 8 A 322 ASN GLN LEU TYR ILE VAL ASP CYS TYR TYR HIS LEU SER
SEQRES 9 A 322 VAL VAL GLY SER GLU GLY GLY HIS ALA THR GLN LEU ALA
SEQRES 10 A 322 THR SER VAL ASP GLY VAL PRO PHE LYS TRP LEU TYR ALA
SEQRES 11 A 322 VAL THR VAL ASP GLN ARG THR GLY ILE VAL TYR PHE THR
SEQRES 12 A 322 ASP VAL SER THR LEU TYR ASP ASP ARG GLY VAL GLN GLN
SEQRES 13 A 322 ILE MET ASP THR SER ASP LYS THR GLY ARG LEU ILE LYS
SEQRES 14 A 322 TYR ASP PRO SER THR LYS GLU THR THR LEU LEU LEU LYS
SEQRES 15 A 322 GLU LEU HIS VAL PRO GLY GLY ALA GLU VAL SER ALA ASP
SEQRES 16 A 322 SER SER PHE VAL LEU VAL ALA GLU PHE LEU SER HIS GLN
SEQRES 17 A 322 ILE VAL LYS TYR TRP LEU GLU GLY PRO LYS LYS GLY THR
SEQRES 18 A 322 ALA GLU VAL LEU VAL LYS ILE PRO ASN PRO GLY ASN ILE
SEQRES 19 A 322 LYS ARG ASN ALA ASP GLY HIS PHE TRP VAL SER SER SER
SEQRES 20 A 322 GLU GLU LEU ASP GLY ASN MET HIS GLY ARG VAL ASP PRO
SEQRES 21 A 322 LYS GLY ILE LYS PHE ASP GLU PHE GLY ASN ILE LEU GLU
SEQRES 22 A 322 VAL ILE PRO LEU PRO PRO PRO PHE ALA GLY GLU HIS PHE
SEQRES 23 A 322 GLU GLN ILE GLN GLU HIS ASP GLY LEU LEU TYR ILE GLY
SEQRES 24 A 322 THR LEU PHE HIS GLY SER VAL GLY ILE LEU VAL TYR ASP
SEQRES 25 A 322 LYS LYS GLY ASN SER PHE VAL SER SER HIS
SEQRES 1 B 322 SER LEU ALA LEU SER SER PRO ILE LEU LYS GLU ILE LEU
SEQRES 2 B 322 ILE GLU ALA PRO SER TYR ALA PRO ASN SER PHE THR PHE
SEQRES 3 B 322 ASP SER THR ASN LYS GLY PHE TYR THR SER VAL GLN ASP
SEQRES 4 B 322 GLY ARG VAL ILE LYS TYR GLU GLY PRO ASN SER GLY PHE
SEQRES 5 B 322 VAL ASP PHE ALA TYR ALA SER PRO TYR TRP ASN LYS ALA
SEQRES 6 B 322 PHE CYS GLU ASN SER THR ASP ALA GLU LYS ARG PRO LEU
SEQRES 7 B 322 CYS GLY ARG THR TYR ASP ILE SER TYR ASN LEU GLN ASN
SEQRES 8 B 322 ASN GLN LEU TYR ILE VAL ASP CYS TYR TYR HIS LEU SER
SEQRES 9 B 322 VAL VAL GLY SER GLU GLY GLY HIS ALA THR GLN LEU ALA
SEQRES 10 B 322 THR SER VAL ASP GLY VAL PRO PHE LYS TRP LEU TYR ALA
SEQRES 11 B 322 VAL THR VAL ASP GLN ARG THR GLY ILE VAL TYR PHE THR
SEQRES 12 B 322 ASP VAL SER THR LEU TYR ASP ASP ARG GLY VAL GLN GLN
SEQRES 13 B 322 ILE MET ASP THR SER ASP LYS THR GLY ARG LEU ILE LYS
SEQRES 14 B 322 TYR ASP PRO SER THR LYS GLU THR THR LEU LEU LEU LYS
SEQRES 15 B 322 GLU LEU HIS VAL PRO GLY GLY ALA GLU VAL SER ALA ASP
SEQRES 16 B 322 SER SER PHE VAL LEU VAL ALA GLU PHE LEU SER HIS GLN
SEQRES 17 B 322 ILE VAL LYS TYR TRP LEU GLU GLY PRO LYS LYS GLY THR
SEQRES 18 B 322 ALA GLU VAL LEU VAL LYS ILE PRO ASN PRO GLY ASN ILE
SEQRES 19 B 322 LYS ARG ASN ALA ASP GLY HIS PHE TRP VAL SER SER SER
SEQRES 20 B 322 GLU GLU LEU ASP GLY ASN MET HIS GLY ARG VAL ASP PRO
SEQRES 21 B 322 LYS GLY ILE LYS PHE ASP GLU PHE GLY ASN ILE LEU GLU
SEQRES 22 B 322 VAL ILE PRO LEU PRO PRO PRO PHE ALA GLY GLU HIS PHE
SEQRES 23 B 322 GLU GLN ILE GLN GLU HIS ASP GLY LEU LEU TYR ILE GLY
SEQRES 24 B 322 THR LEU PHE HIS GLY SER VAL GLY ILE LEU VAL TYR ASP
SEQRES 25 B 322 LYS LYS GLY ASN SER PHE VAL SER SER HIS
HET SCG A1001 27
HET SCG B2001 27
HETNAM SCG SECOLOGANIN
HETSYN SCG METHYL (2S,3R,4S)-2-(BETA-D-GLUCOPYRANOSYLOXY)-4-(2-
HETSYN 2 SCG OXOETHYL)-3-VINYL-3,4-DIHYDRO-2H-PYRAN-5-CARBOXYLATE
FORMUL 3 SCG 2(C17 H24 O10)
FORMUL 5 HOH *102(H2 O)
HELIX 1 1 ASN A 85 GLU A 90 1 6
HELIX 2 2 ASP A 94 GLU A 96 5 3
HELIX 3 3 LYS A 97 GLY A 102 1 6
HELIX 4 4 GLY A 175 THR A 182 1 8
HELIX 5 5 LEU A 227 HIS A 229 5 3
HELIX 6 6 ASN B 85 GLU B 90 1 6
HELIX 7 7 ASP B 94 GLU B 96 5 3
HELIX 8 8 LYS B 97 GLY B 102 1 6
HELIX 9 9 GLY B 175 SER B 183 1 9
SHEET 1 A 8 GLN A 310 HIS A 314 0
SHEET 2 A 8 LEU A 317 GLY A 321 -1 O TYR A 319 N GLN A 312
SHEET 3 A 8 SER A 327 VAL A 332 -1 O GLY A 329 N ILE A 320
SHEET 4 A 8 GLU A 33 GLU A 37 -1 N ILE A 34 O ILE A 330
SHEET 5 A 8 GLU B 33 GLU B 37 1 O GLU B 33 N GLU A 33
SHEET 6 A 8 SER B 327 VAL B 332 -1 O VAL B 328 N ILE B 36
SHEET 7 A 8 LEU B 317 GLY B 321 -1 N LEU B 318 O LEU B 331
SHEET 8 A 8 GLN B 310 HIS B 314 -1 N GLN B 312 O TYR B 319
SHEET 1 B 5 SER A 45 THR A 47 0
SHEET 2 B 5 PHE A 55 SER A 58 -1 O TYR A 56 N THR A 47
SHEET 3 B 5 ARG A 63 TYR A 67 -1 O TYR A 67 N PHE A 55
SHEET 4 B 5 PHE A 74 TYR A 79 -1 O VAL A 75 N LYS A 66
SHEET 5 B 5 GLY A 133 HIS A 134 1 O GLY A 133 N PHE A 77
SHEET 1 C 4 THR A 104 ASN A 110 0
SHEET 2 C 4 GLN A 115 ASP A 120 -1 O GLN A 115 N ASN A 110
SHEET 3 C 4 HIS A 124 VAL A 128 -1 O SER A 126 N ILE A 118
SHEET 4 C 4 THR A 136 ALA A 139 -1 O THR A 136 N VAL A 127
SHEET 1 D 2 SER A 141 VAL A 142 0
SHEET 2 D 2 VAL A 145 PRO A 146 -1 O VAL A 145 N VAL A 142
SHEET 1 E 4 LEU A 150 VAL A 155 0
SHEET 2 E 4 VAL A 162 ASP A 166 -1 O THR A 165 N TYR A 151
SHEET 3 E 4 GLY A 187 TYR A 192 -1 O TYR A 192 N VAL A 162
SHEET 4 E 4 THR A 199 LEU A 206 -1 O LEU A 206 N GLY A 187
SHEET 1 F 4 PRO A 209 VAL A 214 0
SHEET 2 F 4 PHE A 220 GLU A 225 -1 O LEU A 222 N GLU A 213
SHEET 3 F 4 GLN A 230 TRP A 235 -1 O VAL A 232 N VAL A 223
SHEET 4 F 4 ALA A 244 VAL A 248 -1 O GLU A 245 N LYS A 233
SHEET 1 G 4 PRO A 253 ARG A 258 0
SHEET 2 G 4 PHE A 264 GLU A 271 -1 O TRP A 265 N LYS A 257
SHEET 3 G 4 VAL A 280 PHE A 287 -1 O PHE A 287 N PHE A 264
SHEET 4 G 4 ILE A 293 PRO A 298 -1 O ILE A 297 N GLY A 284
SHEET 1 H 5 PHE B 46 THR B 47 0
SHEET 2 H 5 PHE B 55 SER B 58 -1 O TYR B 56 N THR B 47
SHEET 3 H 5 ARG B 63 TYR B 67 -1 O TYR B 67 N PHE B 55
SHEET 4 H 5 PHE B 74 TYR B 79 -1 O VAL B 75 N LYS B 66
SHEET 5 H 5 GLY B 133 HIS B 134 1 O GLY B 133 N PHE B 77
SHEET 1 I 4 THR B 104 ASN B 110 0
SHEET 2 I 4 GLN B 115 ASP B 120 -1 O GLN B 115 N ASN B 110
SHEET 3 I 4 HIS B 124 VAL B 128 -1 O SER B 126 N ILE B 118
SHEET 4 I 4 THR B 136 ALA B 139 -1 O THR B 136 N VAL B 127
SHEET 1 J 2 SER B 141 VAL B 142 0
SHEET 2 J 2 VAL B 145 PRO B 146 -1 O VAL B 145 N VAL B 142
SHEET 1 K 4 LEU B 150 VAL B 155 0
SHEET 2 K 4 VAL B 162 ASP B 166 -1 O TYR B 163 N THR B 154
SHEET 3 K 4 GLY B 187 TYR B 192 -1 O TYR B 192 N VAL B 162
SHEET 4 K 4 THR B 199 LEU B 206 -1 O LEU B 206 N GLY B 187
SHEET 1 L 4 PRO B 209 VAL B 214 0
SHEET 2 L 4 PHE B 220 GLU B 225 -1 O LEU B 222 N GLU B 213
SHEET 3 L 4 GLN B 230 TRP B 235 -1 O TYR B 234 N VAL B 221
SHEET 4 L 4 ALA B 244 LYS B 249 -1 O GLU B 245 N LYS B 233
SHEET 1 M 4 PRO B 253 ARG B 258 0
SHEET 2 M 4 PHE B 264 GLU B 271 -1 O TRP B 265 N LYS B 257
SHEET 3 M 4 VAL B 280 PHE B 287 -1 O ASP B 281 N GLU B 270
SHEET 4 M 4 ILE B 293 PRO B 298 -1 O LEU B 294 N LYS B 286
SSBOND 1 CYS A 89 CYS A 101 1555 1555 2.05
SSBOND 2 CYS B 89 CYS B 101 1555 1555 2.04
CISPEP 1 PRO A 301 PRO A 302 0 7.47
CISPEP 2 PRO B 301 PRO B 302 0 4.19
CRYST1 148.607 148.607 121.069 90.00 90.00 120.00 H 3 18
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006729 0.003885 0.000000 0.00000
SCALE2 0.000000 0.007770 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
