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HEADER HYDROLASE 14-MAY-17 5XMD
TITLE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE VREH1 FROM VIGNA RADIATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIGNA RADIATA;
SOURCE 3 ORGANISM_COMMON: MUNG BEAN;
SOURCE 4 ORGANISM_TAXID: 157791;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS EPOXIDE HYDROLASE ENANTIOCONVERGENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.KONG,J.H.XU,J.H.ZHOU
REVDAT 1 16-MAY-18 5XMD 0
JRNL AUTH X.D.KONG,J.H.XU,J.H.ZHOU
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYL REDUCTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 82530
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 (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4127
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 41.3251 - 6.1313 0.97 2976 158 0.1490 0.1658
REMARK 3 2 6.1313 - 4.8691 0.99 2948 141 0.1538 0.1702
REMARK 3 3 4.8691 - 4.2543 0.99 2895 148 0.1295 0.1497
REMARK 3 4 4.2543 - 3.8656 0.97 2830 159 0.1446 0.1615
REMARK 3 5 3.8656 - 3.5887 0.91 2676 144 0.1513 0.1959
REMARK 3 6 3.5887 - 3.3772 0.92 2669 134 0.1775 0.2410
REMARK 3 7 3.3772 - 3.2082 0.96 2796 141 0.1881 0.2279
REMARK 3 8 3.2082 - 3.0686 0.95 2768 148 0.1990 0.2544
REMARK 3 9 3.0686 - 2.9505 0.93 2688 163 0.2116 0.2394
REMARK 3 10 2.9505 - 2.8487 0.92 2624 148 0.2140 0.2657
REMARK 3 11 2.8487 - 2.7596 0.92 2690 117 0.2062 0.2652
REMARK 3 12 2.7596 - 2.6808 0.90 2581 150 0.1983 0.2397
REMARK 3 13 2.6808 - 2.6102 0.91 2615 147 0.1977 0.2721
REMARK 3 14 2.6102 - 2.5465 0.90 2592 146 0.1884 0.2980
REMARK 3 15 2.5465 - 2.4886 0.92 2601 152 0.1973 0.2407
REMARK 3 16 2.4886 - 2.4357 0.91 2645 136 0.2012 0.2520
REMARK 3 17 2.4357 - 2.3870 0.92 2664 119 0.1976 0.2633
REMARK 3 18 2.3870 - 2.3419 0.92 2624 141 0.1948 0.2784
REMARK 3 19 2.3419 - 2.3001 0.92 2690 121 0.2013 0.2311
REMARK 3 20 2.3001 - 2.2611 0.94 2662 126 0.2088 0.3032
REMARK 3 21 2.2611 - 2.2247 0.93 2710 139 0.2204 0.2826
REMARK 3 22 2.2247 - 2.1904 0.94 2686 125 0.2231 0.2493
REMARK 3 23 2.1904 - 2.1582 0.94 2664 138 0.2087 0.2771
REMARK 3 24 2.1582 - 2.1278 0.94 2765 138 0.2115 0.2668
REMARK 3 25 2.1278 - 2.0991 0.95 2695 155 0.2265 0.3292
REMARK 3 26 2.0991 - 2.0718 0.95 2656 149 0.2246 0.2751
REMARK 3 27 2.0718 - 2.0459 0.95 2785 143 0.2346 0.3145
REMARK 3 28 2.0459 - 2.0213 0.95 2713 164 0.2504 0.2967
REMARK 3 29 2.0213 - 1.9978 0.89 2495 137 0.2642 0.3102
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.26
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 10281
REMARK 3 ANGLE : 1.047 13986
REMARK 3 CHIRALITY : 0.074 1502
REMARK 3 PLANARITY : 0.005 1795
REMARK 3 DIHEDRAL : 14.142 3741
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 5XMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003775.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-11
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 : 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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82570
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.72100
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: PHASER
REMARK 200 STARTING MODEL: 2CJP
REMARK 200
REMARK 200 REMARK: PLATE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M HEPES PH 6.5-7.0,
REMARK 280 0.2M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 25.94600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -51.89200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -92.43649
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -25.94600
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -123.94899
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 ASN A 167
REMARK 465 ASN A 168
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 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 SER C 166
REMARK 465 ASN C 167
REMARK 465 ASN C 168
REMARK 465 GLU C 191
REMARK 465 GLY C 192
REMARK 465 VAL C 193
REMARK 465 ALA C 194
REMARK 465 LEU C 195
REMARK 465 PRO C 196
REMARK 465 SER C 197
REMARK 465 GLY C 198
REMARK 465 SER C 199
REMARK 465 LEU C 200
REMARK 465 PRO C 201
REMARK 465 SER C 202
REMARK 465 ARG C 203
REMARK 465 MET D -33
REMARK 465 GLY D -32
REMARK 465 SER D -31
REMARK 465 SER D -30
REMARK 465 HIS D -29
REMARK 465 HIS D -28
REMARK 465 HIS D -27
REMARK 465 HIS D -26
REMARK 465 HIS D -25
REMARK 465 HIS D -24
REMARK 465 SER D -23
REMARK 465 SER D -22
REMARK 465 GLY D -21
REMARK 465 LEU D -20
REMARK 465 VAL D -19
REMARK 465 PRO D -18
REMARK 465 ARG D -17
REMARK 465 GLY D -16
REMARK 465 SER D -15
REMARK 465 HIS D -14
REMARK 465 MET D -13
REMARK 465 ALA D -12
REMARK 465 SER D -11
REMARK 465 MET D -10
REMARK 465 THR D -9
REMARK 465 GLY D -8
REMARK 465 GLY D -7
REMARK 465 GLN D -6
REMARK 465 GLN D -5
REMARK 465 MET D -4
REMARK 465 GLY D -3
REMARK 465 ARG D -2
REMARK 465 GLY D -1
REMARK 465 GLY D 192
REMARK 465 VAL D 193
REMARK 465 ALA D 194
REMARK 465 LEU D 195
REMARK 465 PRO D 196
REMARK 465 SER D 197
REMARK 465 GLY D 198
REMARK 465 SER D 199
REMARK 465 LEU D 200
REMARK 465 PRO D 201
REMARK 465 SER D 202
REMARK 465 ARG D 203
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 202 O HOH B 401 2.01
REMARK 500 O HOH B 438 O HOH B 525 2.15
REMARK 500 O HOH B 495 O HOH B 516 2.16
REMARK 500 O HOH A 515 O HOH A 549 2.17
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 B 475 O HOH D 512 2444 2.18
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 GLU A 35 -160.07 -122.01
REMARK 500 ASP A 101 -133.99 59.48
REMARK 500 SER A 125 -58.47 76.77
REMARK 500 TYR A 164 -75.27 -76.38
REMARK 500 ALA A 297 -156.12 -94.73
REMARK 500 GLU B 35 -164.85 -124.35
REMARK 500 ASP B 101 -128.12 60.68
REMARK 500 SER B 125 -49.70 75.87
REMARK 500 ASN B 168 39.75 -156.13
REMARK 500 VAL B 193 15.43 -148.35
REMARK 500 SER B 202 87.90 76.63
REMARK 500 ALA B 297 -152.64 -94.89
REMARK 500 PHE B 299 59.06 -94.11
REMARK 500 SER C 0 120.04 77.34
REMARK 500 GLU C 35 -169.39 -115.92
REMARK 500 SER C 72 1.99 -69.06
REMARK 500 ASP C 101 -128.50 57.89
REMARK 500 SER C 125 -50.10 77.26
REMARK 500 PRO C 185 108.81 -50.35
REMARK 500 PRO C 189 -110.53 -69.45
REMARK 500 ALA C 297 -153.71 -93.53
REMARK 500 GLU D 35 -162.94 -124.10
REMARK 500 ASP D 101 -133.63 57.77
REMARK 500 SER D 125 -44.42 76.44
REMARK 500 ASN D 169 87.19 -162.31
REMARK 500 ALA D 297 -149.92 -89.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 285 SHOULD BE PRO AND WAS CONFIRMED BY SEQUENCING OF THE
REMARK 999 ORIGINAL CONSTRUCT. THE CONFLICT SHOULD BE DUE TO MISTAKE IN
REMARK 999 SEQUENCE REFERENCE E5L4L1_VIGRA.
DBREF 5XMD A 1 319 UNP E5L4L1 E5L4L1_VIGRA 1 319
DBREF 5XMD B 1 319 UNP E5L4L1 E5L4L1_VIGRA 1 319
DBREF 5XMD C 1 319 UNP E5L4L1 E5L4L1_VIGRA 1 319
DBREF 5XMD D 1 319 UNP E5L4L1 E5L4L1_VIGRA 1 319
SEQADV 5XMD MET A -33 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -32 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -31 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -30 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -29 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -28 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -27 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -26 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -25 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -24 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -23 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -22 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -21 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD LEU A -20 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD VAL A -19 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO A -18 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG A -17 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -16 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -15 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS A -14 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET A -13 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ALA A -12 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A -11 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET A -10 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD THR A -9 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -8 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -7 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN A -6 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN A -5 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET A -4 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -3 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG A -2 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY A -1 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER A 0 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO A 285 UNP E5L4L1 HIS 285 SEE SEQUENCE DETAILS
SEQADV 5XMD MET B -33 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -32 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -31 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -30 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -29 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -28 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -27 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -26 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -25 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -24 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -23 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -22 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -21 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD LEU B -20 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD VAL B -19 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO B -18 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG B -17 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -16 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -15 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS B -14 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET B -13 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ALA B -12 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B -11 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET B -10 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD THR B -9 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -8 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -7 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN B -6 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN B -5 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET B -4 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -3 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG B -2 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY B -1 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER B 0 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO B 285 UNP E5L4L1 HIS 285 SEE SEQUENCE DETAILS
SEQADV 5XMD MET C -33 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -32 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -31 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -30 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -29 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -28 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -27 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -26 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -25 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -24 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -23 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -22 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -21 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD LEU C -20 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD VAL C -19 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO C -18 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG C -17 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -16 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -15 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS C -14 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET C -13 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ALA C -12 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C -11 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET C -10 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD THR C -9 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -8 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -7 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN C -6 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN C -5 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET C -4 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -3 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG C -2 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY C -1 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER C 0 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO C 285 UNP E5L4L1 HIS 285 SEE SEQUENCE DETAILS
SEQADV 5XMD MET D -33 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -32 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -31 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -30 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -29 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -28 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -27 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -26 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -25 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -24 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -23 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -22 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -21 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD LEU D -20 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD VAL D -19 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO D -18 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG D -17 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -16 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -15 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD HIS D -14 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET D -13 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ALA D -12 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D -11 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET D -10 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD THR D -9 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -8 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -7 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN D -6 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLN D -5 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD MET D -4 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -3 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD ARG D -2 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD GLY D -1 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD SER D 0 UNP E5L4L1 EXPRESSION TAG
SEQADV 5XMD PRO D 285 UNP E5L4L1 HIS 285 SEE SEQUENCE DETAILS
SEQRES 1 A 353 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 353 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 353 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 A 353 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 A 353 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 A 353 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 A 353 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 A 353 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER
SEQRES 9 A 353 ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE
SEQRES 10 A 353 VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE
SEQRES 11 A 353 LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR
SEQRES 12 A 353 LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL
SEQRES 13 A 353 CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL
SEQRES 14 A 353 ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP
SEQRES 15 A 353 TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU
SEQRES 16 A 353 ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE
SEQRES 17 A 353 LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE
SEQRES 18 A 353 LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU
SEQRES 19 A 353 PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP
SEQRES 20 A 353 VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU
SEQRES 21 A 353 THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN
SEQRES 22 A 353 TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS
SEQRES 23 A 353 VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL
SEQRES 24 A 353 TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY
SEQRES 25 A 353 ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL
SEQRES 26 A 353 VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA
SEQRES 27 A 353 ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS
SEQRES 28 A 353 LYS PHE
SEQRES 1 B 353 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 353 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 353 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 B 353 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 B 353 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 B 353 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 B 353 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 B 353 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER
SEQRES 9 B 353 ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE
SEQRES 10 B 353 VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE
SEQRES 11 B 353 LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR
SEQRES 12 B 353 LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL
SEQRES 13 B 353 CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL
SEQRES 14 B 353 ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP
SEQRES 15 B 353 TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU
SEQRES 16 B 353 ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE
SEQRES 17 B 353 LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE
SEQRES 18 B 353 LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU
SEQRES 19 B 353 PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP
SEQRES 20 B 353 VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU
SEQRES 21 B 353 THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN
SEQRES 22 B 353 TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS
SEQRES 23 B 353 VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL
SEQRES 24 B 353 TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY
SEQRES 25 B 353 ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL
SEQRES 26 B 353 VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA
SEQRES 27 B 353 ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS
SEQRES 28 B 353 LYS PHE
SEQRES 1 C 353 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 353 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 353 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 C 353 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 C 353 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 C 353 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 C 353 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 C 353 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER
SEQRES 9 C 353 ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE
SEQRES 10 C 353 VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE
SEQRES 11 C 353 LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR
SEQRES 12 C 353 LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL
SEQRES 13 C 353 CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL
SEQRES 14 C 353 ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP
SEQRES 15 C 353 TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU
SEQRES 16 C 353 ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE
SEQRES 17 C 353 LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE
SEQRES 18 C 353 LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU
SEQRES 19 C 353 PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP
SEQRES 20 C 353 VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU
SEQRES 21 C 353 THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN
SEQRES 22 C 353 TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS
SEQRES 23 C 353 VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL
SEQRES 24 C 353 TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY
SEQRES 25 C 353 ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL
SEQRES 26 C 353 VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA
SEQRES 27 C 353 ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS
SEQRES 28 C 353 LYS PHE
SEQRES 1 D 353 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 353 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 D 353 GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU
SEQRES 4 D 353 HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL
SEQRES 5 D 353 ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS
SEQRES 6 D 353 GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE
SEQRES 7 D 353 LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO
SEQRES 8 D 353 ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER
SEQRES 9 D 353 ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE
SEQRES 10 D 353 VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE
SEQRES 11 D 353 LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR
SEQRES 12 D 353 LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL
SEQRES 13 D 353 CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL
SEQRES 14 D 353 ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP
SEQRES 15 D 353 TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU
SEQRES 16 D 353 ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE
SEQRES 17 D 353 LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE
SEQRES 18 D 353 LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU
SEQRES 19 D 353 PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP
SEQRES 20 D 353 VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU
SEQRES 21 D 353 THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN
SEQRES 22 D 353 TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS
SEQRES 23 D 353 VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL
SEQRES 24 D 353 TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY
SEQRES 25 D 353 ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL
SEQRES 26 D 353 VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA
SEQRES 27 D 353 ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS
SEQRES 28 D 353 LYS PHE
FORMUL 5 HOH *543(H2 O)
HELIX 1 AA1 SER A 0 ILE A 4 5 5
HELIX 2 AA2 LEU A 36 SER A 39 5 4
HELIX 3 AA3 TRP A 40 SER A 49 1 10
HELIX 4 AA4 SER A 70 TYR A 74 5 5
HELIX 5 AA5 THR A 75 LEU A 90 1 16
HELIX 6 AA6 ASP A 101 ARG A 114 1 14
HELIX 7 AA7 ARG A 136 GLY A 146 1 11
HELIX 8 AA8 TYR A 149 PHE A 154 1 6
HELIX 9 AA9 GLY A 158 SER A 166 1 9
HELIX 10 AB1 ILE A 170 ASN A 180 1 11
HELIX 11 AB2 LEU A 195 LEU A 200 5 6
HELIX 12 AB3 SER A 210 GLY A 225 1 16
HELIX 13 AB4 LEU A 226 ARG A 234 1 9
HELIX 14 AB5 ASN A 235 THR A 243 1 9
HELIX 15 AB6 ALA A 244 THR A 247 5 4
HELIX 16 AB7 GLY A 270 SER A 277 1 8
HELIX 17 AB8 GLY A 278 VAL A 284 1 7
HELIX 18 AB9 PHE A 299 ALA A 304 1 6
HELIX 19 AC1 ALA A 304 LYS A 317 1 14
HELIX 20 AC2 SER B 0 ILE B 4 5 5
HELIX 21 AC3 LEU B 36 SER B 39 5 4
HELIX 22 AC4 TRP B 40 SER B 49 1 10
HELIX 23 AC5 SER B 70 TYR B 74 5 5
HELIX 24 AC6 THR B 75 GLY B 91 1 17
HELIX 25 AC7 ASP B 101 ARG B 114 1 14
HELIX 26 AC8 ARG B 136 GLY B 146 1 11
HELIX 27 AC9 TYR B 149 PHE B 154 1 6
HELIX 28 AD1 GLY B 158 GLY B 165 1 8
HELIX 29 AD2 ASN B 169 ASN B 180 1 12
HELIX 30 AD3 PRO B 196 LEU B 200 5 5
HELIX 31 AD4 SER B 210 GLY B 225 1 16
HELIX 32 AD5 LEU B 226 ARG B 234 1 9
HELIX 33 AD6 ASN B 235 THR B 243 1 9
HELIX 34 AD7 ALA B 244 THR B 247 5 4
HELIX 35 AD8 ASP B 263 SER B 268 1 6
HELIX 36 AD9 GLY B 270 SER B 277 1 8
HELIX 37 AE1 GLY B 278 VAL B 284 1 7
HELIX 38 AE2 PHE B 299 ALA B 304 1 6
HELIX 39 AE3 ALA B 304 LYS B 317 1 14
HELIX 40 AE4 SER C 0 ILE C 4 5 5
HELIX 41 AE5 LEU C 36 SER C 39 5 4
HELIX 42 AE6 TRP C 40 SER C 49 1 10
HELIX 43 AE7 SER C 70 TYR C 74 5 5
HELIX 44 AE8 THR C 75 LEU C 90 1 16
HELIX 45 AE9 ASP C 101 ARG C 114 1 14
HELIX 46 AF1 ARG C 136 GLY C 146 1 11
HELIX 47 AF2 TYR C 149 GLN C 155 1 7
HELIX 48 AF3 GLY C 158 GLY C 165 1 8
HELIX 49 AF4 ILE C 170 ASN C 180 1 11
HELIX 50 AF5 SER C 210 GLY C 225 1 16
HELIX 51 AF6 LEU C 226 ARG C 234 1 9
HELIX 52 AF7 ASN C 235 THR C 243 1 9
HELIX 53 AF8 ALA C 244 THR C 247 5 4
HELIX 54 AF9 GLY C 270 SER C 277 1 8
HELIX 55 AG1 GLY C 278 VAL C 284 1 7
HELIX 56 AG2 PHE C 299 ALA C 304 1 6
HELIX 57 AG3 ALA C 304 LYS C 317 1 14
HELIX 58 AG4 LYS C 318 PHE C 319 5 2
HELIX 59 AG5 SER D 0 ILE D 4 5 5
HELIX 60 AG6 LEU D 36 SER D 39 5 4
HELIX 61 AG7 TRP D 40 SER D 49 1 10
HELIX 62 AG8 SER D 70 TYR D 74 5 5
HELIX 63 AG9 THR D 75 LEU D 90 1 16
HELIX 64 AH1 ASP D 101 ARG D 114 1 14
HELIX 65 AH2 ARG D 136 GLY D 146 1 11
HELIX 66 AH3 TYR D 149 PHE D 154 1 6
HELIX 67 AH4 GLY D 158 SER D 166 1 9
HELIX 68 AH5 ASN D 169 ASN D 180 1 12
HELIX 69 AH6 SER D 210 GLY D 225 1 16
HELIX 70 AH7 LEU D 226 ARG D 234 1 9
HELIX 71 AH8 ASN D 235 THR D 243 1 9
HELIX 72 AH9 ALA D 244 THR D 247 5 4
HELIX 73 AI1 ASP D 263 SER D 268 1 6
HELIX 74 AI2 GLY D 270 SER D 277 1 8
HELIX 75 AI3 GLY D 278 VAL D 284 1 7
HELIX 76 AI4 PHE D 299 ALA D 304 1 6
HELIX 77 AI5 ALA D 304 LYS D 317 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 MET A 16 N VAL A 9
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 PHE A 29 O VAL A 55
SHEET 5 AA1 8 VAL A 95 HIS A 100 1 O VAL A 98 N LEU A 28
SHEET 6 AA1 8 ILE A 118 LEU A 124 1 O VAL A 122 N LEU A 97
SHEET 7 AA1 8 VAL A 255 GLY A 260 1 O ILE A 258 N CYS A 123
SHEET 8 AA1 8 VAL A 291 GLN A 293 1 O GLN A 293 N THR A 259
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 PHE B 29 O VAL B 55
SHEET 5 AA2 8 VAL B 95 HIS B 100 1 O PHE B 96 N LEU B 28
SHEET 6 AA2 8 ILE B 118 LEU B 124 1 O VAL B 122 N LEU B 97
SHEET 7 AA2 8 VAL B 255 GLY B 260 1 O ILE B 258 N CYS B 123
SHEET 8 AA2 8 LEU B 287 GLN B 293 1 O GLN B 293 N THR B 259
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 PHE C 29 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 ILE C 118 LEU C 124 1 O VAL C 122 N LEU C 97
SHEET 7 AA3 8 VAL C 255 GLY C 260 1 O ILE C 258 N CYS C 123
SHEET 8 AA3 8 VAL C 291 GLN C 293 1 O GLN C 293 N THR C 259
SHEET 1 AA4 8 GLU D 5 VAL D 11 0
SHEET 2 AA4 8 ILE D 14 LYS D 21 -1 O MET D 16 N VAL D 9
SHEET 3 AA4 8 ARG D 53 PRO D 57 -1 O ALA D 56 N ALA D 19
SHEET 4 AA4 8 VAL D 26 LEU D 30 1 N PHE D 29 O VAL D 55
SHEET 5 AA4 8 VAL D 95 HIS D 100 1 O PHE D 96 N LEU D 28
SHEET 6 AA4 8 ILE D 118 LEU D 124 1 O VAL D 122 N LEU D 97
SHEET 7 AA4 8 VAL D 255 GLY D 260 1 O ILE D 258 N CYS D 123
SHEET 8 AA4 8 LEU D 287 GLN D 293 1 O GLN D 293 N THR D 259
CISPEP 1 PHE A 33 PRO A 34 0 -6.43
CISPEP 2 PHE B 33 PRO B 34 0 -5.24
CISPEP 3 PHE C 33 PRO C 34 0 -5.35
CISPEP 4 PHE D 33 PRO D 34 0 -10.39
CRYST1 101.691 51.892 124.294 90.00 94.27 90.00 P 1 21 1 8
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 0.009834 0.000000 0.000734 0.00000
SCALE2 0.000000 0.019271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008068 0.00000
TER 2550 PHE A 319
TER 5101 PHE B 319
TER 7531 PHE C 319
TER 10005 PHE D 319
MASTER 467 0 0 77 32 0 0 610512 4 0 112
END |