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HEADER HYDROLASE 12-MAY-17 5XM6
TITLE THE OVERALL STRUCTURE OF VREH2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.3.2.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIGNA RADIATA;
SOURCE 3 ORGANISM_COMMON: MUNG BEAN;
SOURCE 4 ORGANISM_TAXID: 157791;
SOURCE 5 GENE: VREH3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.L.LI,X.D.KONG,H.L.YU,Y.P.SHANG,J.H.ZHOU,J.H.XU
REVDAT 1 05-SEP-18 5XM6 0
JRNL AUTH F.L.LI,X.D.KONG,Q.CHEN,Y.C.ZHENG,Q.XU,F.F.CHEN,L.Q.FAN,
JRNL AUTH 2 G.Q.LIN,J.H.ZHOU,H.L.YU,J.H.XU
JRNL TITL REGIOSELECTIVITY ENGINEERING OF EPOXIDE HYDROLASE:
JRNL TITL 2 NEAR-PERFECT ENANTIOCONVERGENCE THROUGH A SINGLE SITE
JRNL TITL 3 MUTATION
JRNL REF ACS CATALYSIS V. 8 8314 2018
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B02622
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 50310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2556
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.5382 - 6.5463 0.99 2898 144 0.1795 0.2078
REMARK 3 2 6.5463 - 5.1992 1.00 2731 151 0.1909 0.2088
REMARK 3 3 5.1992 - 4.5429 1.00 2698 136 0.1522 0.2026
REMARK 3 4 4.5429 - 4.1280 1.00 2695 161 0.1494 0.1785
REMARK 3 5 4.1280 - 3.8323 1.00 2649 156 0.1607 0.1971
REMARK 3 6 3.8323 - 3.6065 1.00 2659 141 0.1756 0.2154
REMARK 3 7 3.6065 - 3.4260 1.00 2628 142 0.1794 0.1903
REMARK 3 8 3.4260 - 3.2769 1.00 2658 143 0.1818 0.2248
REMARK 3 9 3.2769 - 3.1508 1.00 2629 128 0.1976 0.2862
REMARK 3 10 3.1508 - 3.0421 1.00 2625 138 0.1912 0.2529
REMARK 3 11 3.0421 - 2.9470 1.00 2619 138 0.1964 0.2413
REMARK 3 12 2.9470 - 2.8628 1.00 2624 143 0.1983 0.2603
REMARK 3 13 2.8628 - 2.7875 1.00 2610 151 0.1914 0.2446
REMARK 3 14 2.7875 - 2.7195 1.00 2600 135 0.1968 0.2530
REMARK 3 15 2.7195 - 2.6577 1.00 2620 137 0.1967 0.2618
REMARK 3 16 2.6577 - 2.6011 1.00 2611 128 0.2129 0.2948
REMARK 3 17 2.6011 - 2.5491 1.00 2614 150 0.2056 0.2811
REMARK 3 18 2.5491 - 2.5010 0.99 2586 134 0.2096 0.2893
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7906
REMARK 3 ANGLE : 1.119 10757
REMARK 3 CHIRALITY : 0.077 1132
REMARK 3 PLANARITY : 0.006 1392
REMARK 3 DIHEDRAL : 14.136 2868
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5XM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003764.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-16
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 : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 27.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 29.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: CCP4I 6.3.0
REMARK 200 STARTING MODEL: 2CJP
REMARK 200
REMARK 200 REMARK: RHOMBUS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, PEG500MME, HEPES, MOPS,
REMARK 280 SODIUM NITRATE, AMMONIUM SULFATE, DISODIUM HYDROGEN PHOSPHATE.,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 118.48350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.59000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.24175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.59000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.59000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 177.72525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.59000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.59000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 59.24175
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.59000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.59000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 177.72525
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 118.48350
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -33
REMARK 465 GLY A -32
REMARK 465 SER A -31
REMARK 465 SER A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 GLY A -21
REMARK 465 LEU A -20
REMARK 465 VAL A -19
REMARK 465 PRO A -18
REMARK 465 ARG A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET B -33
REMARK 465 GLY B -32
REMARK 465 SER B -31
REMARK 465 SER B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 SER B -23
REMARK 465 SER B -22
REMARK 465 GLY B -21
REMARK 465 LEU B -20
REMARK 465 VAL B -19
REMARK 465 PRO B -18
REMARK 465 ARG B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET C -33
REMARK 465 GLY C -32
REMARK 465 SER C -31
REMARK 465 SER C -30
REMARK 465 HIS C -29
REMARK 465 HIS C -28
REMARK 465 HIS C -27
REMARK 465 HIS C -26
REMARK 465 HIS C -25
REMARK 465 HIS C -24
REMARK 465 SER C -23
REMARK 465 SER C -22
REMARK 465 GLY C -21
REMARK 465 LEU C -20
REMARK 465 VAL C -19
REMARK 465 PRO C -18
REMARK 465 ARG C -17
REMARK 465 GLY C -16
REMARK 465 SER C -15
REMARK 465 HIS C -14
REMARK 465 MET C -13
REMARK 465 ALA C -12
REMARK 465 SER C -11
REMARK 465 MET C -10
REMARK 465 THR C -9
REMARK 465 GLY C -8
REMARK 465 GLY C -7
REMARK 465 GLN C -6
REMARK 465 GLN C -5
REMARK 465 MET C -4
REMARK 465 GLY C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
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 HOH C 511 O HOH C 517 1.81
REMARK 500 O HOH B 434 O HOH B 563 1.81
REMARK 500 OE2 GLU A 305 O HOH A 401 1.82
REMARK 500 O HOH A 609 O HOH A 610 1.84
REMARK 500 O HOH C 430 O HOH C 437 1.84
REMARK 500 O HOH B 573 O HOH B 599 1.87
REMARK 500 O HOH B 587 O HOH B 608 1.87
REMARK 500 O HOH A 527 O HOH B 548 1.88
REMARK 500 O HOH B 626 O HOH B 632 1.92
REMARK 500 O HOH B 610 O HOH B 617 1.94
REMARK 500 OD1 ASN C 197 O HOH C 401 1.97
REMARK 500 O HOH B 476 O HOH B 533 1.98
REMARK 500 O HOH C 456 O HOH C 480 1.98
REMARK 500 O HOH B 586 O HOH B 606 1.98
REMARK 500 O HOH C 472 O HOH C 484 2.01
REMARK 500 O HOH B 537 O HOH B 619 2.02
REMARK 500 O HOH C 502 O HOH C 513 2.03
REMARK 500 O HOH A 505 O HOH A 577 2.03
REMARK 500 O HOH A 571 O HOH B 470 2.04
REMARK 500 O HOH A 566 O HOH A 594 2.06
REMARK 500 O HOH A 459 O HOH A 559 2.09
REMARK 500 O HOH B 618 O HOH B 626 2.11
REMARK 500 O HOH A 540 O HOH B 499 2.11
REMARK 500 OE1 GLU A 35 O HOH A 402 2.11
REMARK 500 OD1 ASN A 300 O HOH A 403 2.12
REMARK 500 O HOH B 592 O HOH B 606 2.13
REMARK 500 OE1 GLU B 159 O HOH B 401 2.16
REMARK 500 ND2 ASN C 175 O GLY C 195 2.17
REMARK 500 OE1 GLU C 10 O HOH C 402 2.17
REMARK 500 O HOH B 560 O HOH B 572 2.18
REMARK 500 OE1 GLN B 281 O HOH B 402 2.19
REMARK 500 O LYS B 156 O HOH B 403 2.19
REMARK 500 O HOH A 412 O HOH A 544 2.19
REMARK 500 O HOH A 611 O HOH C 505 2.19
REMARK 500 O HOH B 436 O HOH B 532 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 458 O HOH C 473 6554 1.87
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 PRO A 34 78.27 -102.26
REMARK 500 GLU A 35 -158.14 -115.96
REMARK 500 ASP A 101 -128.48 56.49
REMARK 500 SER A 125 -52.09 72.22
REMARK 500 ALA A 296 -146.97 -93.25
REMARK 500 ALA A 303 51.48 -112.05
REMARK 500 PRO B 34 78.35 -101.86
REMARK 500 GLU B 35 -157.77 -112.84
REMARK 500 ASP B 101 -128.76 61.31
REMARK 500 SER B 125 -55.99 70.67
REMARK 500 THR B 194 71.09 45.92
REMARK 500 ALA B 296 -152.05 -100.83
REMARK 500 ALA B 303 51.17 -118.57
REMARK 500 LYS B 317 4.50 -68.04
REMARK 500 PRO C 34 71.66 -101.89
REMARK 500 GLU C 35 -155.45 -103.68
REMARK 500 ASP C 101 -123.35 62.74
REMARK 500 SER C 125 -61.94 75.99
REMARK 500 VAL C 167 -27.43 75.64
REMARK 500 PHE C 196 -41.77 100.02
REMARK 500 LEU C 268 26.96 45.74
REMARK 500 GLU C 288 152.81 178.62
REMARK 500 ALA C 296 -140.82 -94.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 5XM6 A 1 318 UNP A0A0G3F3K2_VIGRA
DBREF2 5XM6 A A0A0G3F3K2 1 318
DBREF1 5XM6 B 1 318 UNP A0A0G3F3K2_VIGRA
DBREF2 5XM6 B A0A0G3F3K2 1 318
DBREF1 5XM6 C 1 318 UNP A0A0G3F3K2_VIGRA
DBREF2 5XM6 C A0A0G3F3K2 1 318
SEQADV 5XM6 MET A -33 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -32 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -31 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -30 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -29 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -28 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -27 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -26 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -25 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -24 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -23 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -22 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -21 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 LEU A -20 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 VAL A -19 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 PRO A -18 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG A -17 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -16 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -15 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS A -14 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET A -13 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ALA A -12 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A -11 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET A -10 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 THR A -9 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -8 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -7 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN A -6 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN A -5 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET A -4 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -3 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG A -2 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY A -1 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER A 0 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLU A 3 UNP A0A0G3F3K GLY 3 ENGINEERED MUTATION
SEQADV 5XM6 ILE A 4 UNP A0A0G3F3K VAL 4 ENGINEERED MUTATION
SEQADV 5XM6 HIS A 114 UNP A0A0G3F3K ARG 114 ENGINEERED MUTATION
SEQADV 5XM6 MET B -33 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -32 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -31 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -30 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -29 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -28 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -27 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -26 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -25 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -24 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -23 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -22 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -21 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 LEU B -20 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 VAL B -19 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 PRO B -18 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG B -17 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -16 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -15 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS B -14 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET B -13 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ALA B -12 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B -11 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET B -10 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 THR B -9 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -8 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -7 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN B -6 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN B -5 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET B -4 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -3 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG B -2 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY B -1 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER B 0 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLU B 3 UNP A0A0G3F3K GLY 3 ENGINEERED MUTATION
SEQADV 5XM6 ILE B 4 UNP A0A0G3F3K VAL 4 ENGINEERED MUTATION
SEQADV 5XM6 HIS B 114 UNP A0A0G3F3K ARG 114 ENGINEERED MUTATION
SEQADV 5XM6 MET C -33 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -32 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -31 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -30 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -29 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -28 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -27 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -26 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -25 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -24 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -23 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -22 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -21 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 LEU C -20 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 VAL C -19 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 PRO C -18 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG C -17 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -16 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -15 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 HIS C -14 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET C -13 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ALA C -12 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C -11 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET C -10 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 THR C -9 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -8 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -7 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN C -6 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLN C -5 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 MET C -4 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -3 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 ARG C -2 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLY C -1 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 SER C 0 UNP A0A0G3F3K EXPRESSION TAG
SEQADV 5XM6 GLU C 3 UNP A0A0G3F3K GLY 3 ENGINEERED MUTATION
SEQADV 5XM6 ILE C 4 UNP A0A0G3F3K VAL 4 ENGINEERED MUTATION
SEQADV 5XM6 HIS C 114 UNP A0A0G3F3K ARG 114 ENGINEERED MUTATION
SEQRES 1 A 352 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 352 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 352 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 A 352 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 A 352 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 A 352 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 A 352 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 A 352 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER
SEQRES 9 A 352 ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU
SEQRES 10 A 352 ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE
SEQRES 11 A 352 LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR
SEQRES 12 A 352 LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL
SEQRES 13 A 352 CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE
SEQRES 14 A 352 ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP
SEQRES 15 A 352 TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU
SEQRES 16 A 352 ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS
SEQRES 17 A 352 ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE
SEQRES 18 A 352 PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET
SEQRES 19 A 352 PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU
SEQRES 20 A 352 ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR
SEQRES 21 A 352 GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP
SEQRES 22 A 352 GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL
SEQRES 23 A 352 PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR
SEQRES 24 A 352 THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY
SEQRES 25 A 352 PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL
SEQRES 26 A 352 GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA
SEQRES 27 A 352 GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS
SEQRES 28 A 352 PHE
SEQRES 1 B 352 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 352 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 352 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 B 352 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 B 352 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 B 352 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 B 352 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 B 352 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER
SEQRES 9 B 352 ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU
SEQRES 10 B 352 ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE
SEQRES 11 B 352 LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR
SEQRES 12 B 352 LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL
SEQRES 13 B 352 CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE
SEQRES 14 B 352 ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP
SEQRES 15 B 352 TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU
SEQRES 16 B 352 ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS
SEQRES 17 B 352 ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE
SEQRES 18 B 352 PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET
SEQRES 19 B 352 PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU
SEQRES 20 B 352 ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR
SEQRES 21 B 352 GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP
SEQRES 22 B 352 GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL
SEQRES 23 B 352 PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR
SEQRES 24 B 352 THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY
SEQRES 25 B 352 PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL
SEQRES 26 B 352 GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA
SEQRES 27 B 352 GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS
SEQRES 28 B 352 PHE
SEQRES 1 C 352 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 352 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 352 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 C 352 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 C 352 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 C 352 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 C 352 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 C 352 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER
SEQRES 9 C 352 ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU
SEQRES 10 C 352 ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE
SEQRES 11 C 352 LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR
SEQRES 12 C 352 LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL
SEQRES 13 C 352 CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE
SEQRES 14 C 352 ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP
SEQRES 15 C 352 TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU
SEQRES 16 C 352 ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS
SEQRES 17 C 352 ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE
SEQRES 18 C 352 PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET
SEQRES 19 C 352 PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU
SEQRES 20 C 352 ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR
SEQRES 21 C 352 GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP
SEQRES 22 C 352 GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL
SEQRES 23 C 352 PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR
SEQRES 24 C 352 THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY
SEQRES 25 C 352 PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL
SEQRES 26 C 352 GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA
SEQRES 27 C 352 GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS
SEQRES 28 C 352 PHE
FORMUL 4 HOH *572(H2 O)
HELIX 1 AA1 LEU A 36 SER A 39 5 4
HELIX 2 AA2 TRP A 40 SER A 49 1 10
HELIX 3 AA3 SER A 70 TYR A 74 5 5
HELIX 4 AA4 THR A 75 GLY A 91 1 17
HELIX 5 AA5 ASP A 101 HIS A 114 1 14
HELIX 6 AA6 ARG A 136 GLY A 146 1 11
HELIX 7 AA7 TYR A 149 PHE A 154 1 6
HELIX 8 AA8 GLY A 158 GLY A 168 1 11
HELIX 9 AA9 GLY A 168 THR A 179 1 12
HELIX 10 AB1 THR A 209 GLY A 224 1 16
HELIX 11 AB2 PHE A 225 ASN A 234 1 10
HELIX 12 AB3 ASN A 234 THR A 242 1 9
HELIX 13 AB4 ALA A 243 SER A 246 5 4
HELIX 14 AB5 ASN A 269 GLY A 277 1 9
HELIX 15 AB6 GLY A 277 VAL A 283 1 7
HELIX 16 AB7 PHE A 298 ALA A 303 1 6
HELIX 17 AB8 ALA A 303 LYS A 316 1 14
HELIX 18 AB9 LEU B 36 SER B 39 5 4
HELIX 19 AC1 TRP B 40 SER B 49 1 10
HELIX 20 AC2 SER B 70 TYR B 74 5 5
HELIX 21 AC3 THR B 75 GLY B 91 1 17
HELIX 22 AC4 ASP B 101 HIS B 114 1 14
HELIX 23 AC5 ARG B 136 GLY B 146 1 11
HELIX 24 AC6 TYR B 149 PHE B 154 1 6
HELIX 25 AC7 GLY B 158 GLY B 168 1 11
HELIX 26 AC8 GLY B 168 THR B 178 1 11
HELIX 27 AC9 THR B 209 GLY B 224 1 16
HELIX 28 AD1 PHE B 225 ARG B 233 1 9
HELIX 29 AD2 ASN B 234 THR B 242 1 9
HELIX 30 AD3 ALA B 243 SER B 246 5 4
HELIX 31 AD4 ASN B 269 GLY B 277 1 9
HELIX 32 AD5 GLY B 277 VAL B 283 1 7
HELIX 33 AD6 PHE B 298 ALA B 303 1 6
HELIX 34 AD7 ALA B 303 LYS B 316 1 14
HELIX 35 AD8 LEU C 36 SER C 39 5 4
HELIX 36 AD9 TRP C 40 ARG C 50 1 11
HELIX 37 AE1 SER C 70 TYR C 74 5 5
HELIX 38 AE2 THR C 75 LEU C 90 1 16
HELIX 39 AE3 ASP C 101 HIS C 114 1 14
HELIX 40 AE4 ARG C 136 GLY C 146 1 11
HELIX 41 AE5 TYR C 149 PHE C 154 1 6
HELIX 42 AE6 GLY C 158 GLU C 166 1 9
HELIX 43 AE7 GLY C 168 THR C 179 1 12
HELIX 44 AE8 THR C 209 GLY C 224 1 16
HELIX 45 AE9 PHE C 225 ARG C 233 1 9
HELIX 46 AF1 ASN C 234 THR C 242 1 9
HELIX 47 AF2 ALA C 243 SER C 246 5 4
HELIX 48 AF3 ASN C 269 GLY C 277 1 9
HELIX 49 AF4 GLY C 277 VAL C 283 1 7
HELIX 50 AF5 PHE C 298 ALA C 303 1 6
HELIX 51 AF6 ALA C 303 LYS C 316 1 14
SHEET 1 AA1 8 GLU A 5 VAL A 11 0
SHEET 2 AA1 8 ILE A 14 LYS A 21 -1 O VAL A 18 N ARG A 7
SHEET 3 AA1 8 ARG A 53 PRO A 57 -1 O ALA A 56 N ALA A 19
SHEET 4 AA1 8 VAL A 26 LEU A 30 1 N VAL A 27 O ARG A 53
SHEET 5 AA1 8 VAL A 95 HIS A 100 1 O PHE A 96 N LEU A 28
SHEET 6 AA1 8 VAL A 118 LEU A 124 1 O VAL A 122 N LEU A 97
SHEET 7 AA1 8 VAL A 254 GLY A 259 1 O ILE A 257 N CYS A 123
SHEET 8 AA1 8 LEU A 286 GLN A 292 1 O GLN A 292 N THR A 258
SHEET 1 AA2 8 GLU B 5 VAL B 11 0
SHEET 2 AA2 8 ILE B 14 LYS B 21 -1 O VAL B 18 N ARG B 7
SHEET 3 AA2 8 ARG B 53 PRO B 57 -1 O ALA B 56 N ALA B 19
SHEET 4 AA2 8 VAL B 26 LEU B 30 1 N VAL B 27 O ARG B 53
SHEET 5 AA2 8 VAL B 95 HIS B 100 1 O PHE B 96 N LEU B 28
SHEET 6 AA2 8 VAL B 118 LEU B 124 1 O VAL B 122 N LEU B 97
SHEET 7 AA2 8 VAL B 254 GLY B 259 1 O ILE B 257 N CYS B 123
SHEET 8 AA2 8 LEU B 286 GLN B 292 1 O ILE B 290 N PHE B 256
SHEET 1 AA3 8 GLU C 5 VAL C 11 0
SHEET 2 AA3 8 ILE C 14 LYS C 21 -1 O VAL C 18 N ARG C 7
SHEET 3 AA3 8 ARG C 53 PRO C 57 -1 O ALA C 56 N ALA C 19
SHEET 4 AA3 8 VAL C 26 LEU C 30 1 N VAL C 27 O VAL C 55
SHEET 5 AA3 8 VAL C 95 HIS C 100 1 O PHE C 96 N LEU C 28
SHEET 6 AA3 8 VAL C 118 LEU C 124 1 O VAL C 122 N LEU C 97
SHEET 7 AA3 8 VAL C 254 GLY C 259 1 O LYS C 255 N TYR C 121
SHEET 8 AA3 8 LEU C 286 GLN C 292 1 O GLN C 292 N THR C 258
CISPEP 1 PHE A 33 PRO A 34 0 -6.97
CISPEP 2 GLY A 195 PHE A 196 0 16.36
CISPEP 3 PRO A 201 ASN A 202 0 -7.18
CISPEP 4 PHE B 33 PRO B 34 0 -4.01
CISPEP 5 GLY B 193 THR B 194 0 19.60
CISPEP 6 PHE C 33 PRO C 34 0 -7.05
CRYST1 109.180 109.180 236.967 90.00 90.00 90.00 P 41 21 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 0.009159 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004220 0.00000
TER 2560 PHE A 318
TER 5120 PHE B 318
TER 7680 PHE C 318
MASTER 433 0 0 51 24 0 0 6 8249 3 0 84
END |