HEADER TRANSPORT PROTEIN 12-MAY-15 4ZRQ
TITLE E88 DELETION MUTANT OF CD320 IN COMPLEX WITH TC2
CAVEAT 4ZRQ CNC A 501 HAS WRONG CHIRALITY AT ATOM C3 CNC B 501 HAS WRONG
CAVEAT 2 4ZRQ CHIRALITY AT ATOM C3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCOBALAMIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TC-2,TRANSCOBALAMIN II,TCII;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CD320 ANTIGEN;
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: RESIDUES 53-171;
COMPND 10 SYNONYM: 8D6 ANTIGEN,FDC-SIGNALING MOLECULE 8D6,FDC-SM-8D6,
COMPND 11 TRANSCOBALAMIN RECEPTOR,TCBLR;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TCN2, TC2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: UNIDENTIFIED BACULOVIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: CD320, 8D6A, UNQ198/PRO224;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: UNIDENTIFIED BACULOVIRUS
KEYWDS LDLR-R, VITAMIN TRANSPORTER, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ALAM,K.P.LOCHER
REVDAT 4 25-AUG-21 4ZRQ 1 CAVEAT COMPND HETNAM FORMUL
REVDAT 3 10-OCT-18 4ZRQ 1 COMPND SOURCE
REVDAT 2 27-JUL-16 4ZRQ 1 JRNL
REVDAT 1 20-JUL-16 4ZRQ 0
JRNL AUTH A.ALAM,J.S.WOO,J.SCHMITZ,B.PRINZ,K.ROOT,F.CHEN,J.S.BLOCH,
JRNL AUTH 2 R.ZENOBI,K.P.LOCHER
JRNL TITL STRUCTURAL BASIS OF TRANSCOBALAMIN RECOGNITION BY HUMAN
JRNL TITL 2 CD320 RECEPTOR.
JRNL REF NAT COMMUN V. 7 12100 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27411955
JRNL DOI 10.1038/NCOMMS12100
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54979
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2731
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 29.4359 - 7.0270 0.99 2856 161 0.1456 0.1555
REMARK 3 2 7.0270 - 5.5901 1.00 2732 135 0.1936 0.2405
REMARK 3 3 5.5901 - 4.8871 1.00 2645 167 0.1770 0.2148
REMARK 3 4 4.8871 - 4.4419 1.00 2663 129 0.1499 0.1895
REMARK 3 5 4.4419 - 4.1244 1.00 2649 113 0.1638 0.1810
REMARK 3 6 4.1244 - 3.8818 1.00 2617 149 0.1670 0.1992
REMARK 3 7 3.8818 - 3.6878 1.00 2599 137 0.1958 0.2192
REMARK 3 8 3.6878 - 3.5276 1.00 2615 127 0.2076 0.2376
REMARK 3 9 3.5276 - 3.3920 1.00 2582 127 0.2290 0.2778
REMARK 3 10 3.3920 - 3.2751 1.00 2595 144 0.2439 0.2797
REMARK 3 11 3.2751 - 3.1728 1.00 2557 145 0.2442 0.2768
REMARK 3 12 3.1728 - 3.0822 1.00 2584 142 0.2607 0.2967
REMARK 3 13 3.0822 - 3.0011 1.00 2607 133 0.2587 0.3019
REMARK 3 14 3.0011 - 2.9280 1.00 2593 108 0.2624 0.3016
REMARK 3 15 2.9280 - 2.8615 1.00 2551 161 0.2808 0.3093
REMARK 3 16 2.8615 - 2.8006 1.00 2559 130 0.2788 0.3394
REMARK 3 17 2.8006 - 2.7446 1.00 2583 122 0.2756 0.2960
REMARK 3 18 2.7446 - 2.6929 1.00 2556 147 0.2851 0.3417
REMARK 3 19 2.6929 - 2.6448 1.00 2555 119 0.2939 0.3073
REMARK 3 20 2.6448 - 2.6000 1.00 2550 135 0.3081 0.3898
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.47
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 : 0.007 7702
REMARK 3 ANGLE : 1.886 10490
REMARK 3 CHIRALITY : 0.122 1178
REMARK 3 PLANARITY : 0.008 1332
REMARK 3 DIHEDRAL : 13.699 2808
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 409 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1962 -47.2355 -39.7263
REMARK 3 T TENSOR
REMARK 3 T11: 0.5598 T22: 0.3196
REMARK 3 T33: 0.2860 T12: 0.0504
REMARK 3 T13: 0.0045 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 3.0841 L22: 1.7106
REMARK 3 L33: 2.9400 L12: 1.3772
REMARK 3 L13: 1.5916 L23: 0.7957
REMARK 3 S TENSOR
REMARK 3 S11: 0.1932 S12: -0.2816 S13: -0.0873
REMARK 3 S21: 0.2175 S22: -0.1365 S23: 0.0455
REMARK 3 S31: 0.1309 S32: 0.0117 S33: -0.0538
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 409 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7640 -28.8161 -0.9100
REMARK 3 T TENSOR
REMARK 3 T11: 0.3985 T22: 0.4652
REMARK 3 T33: 0.2952 T12: 0.0163
REMARK 3 T13: -0.0113 T23: 0.0730
REMARK 3 L TENSOR
REMARK 3 L11: 2.3661 L22: 3.0353
REMARK 3 L33: 4.5354 L12: 1.5827
REMARK 3 L13: 1.4207 L23: 1.7117
REMARK 3 S TENSOR
REMARK 3 S11: -0.1539 S12: 0.0987 S13: 0.1789
REMARK 3 S21: -0.3773 S22: 0.0914 S23: 0.0356
REMARK 3 S31: -0.0690 S32: 0.2212 S33: 0.0673
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 53 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6599 -68.1179 -27.0565
REMARK 3 T TENSOR
REMARK 3 T11: 1.3868 T22: 1.1503
REMARK 3 T33: 1.7086 T12: 0.1842
REMARK 3 T13: -0.1072 T23: 0.3592
REMARK 3 L TENSOR
REMARK 3 L11: 7.1465 L22: 8.1804
REMARK 3 L33: 5.7063 L12: 6.0698
REMARK 3 L13: 1.5943 L23: -1.6735
REMARK 3 S TENSOR
REMARK 3 S11: 0.1239 S12: -1.4070 S13: -2.8628
REMARK 3 S21: 1.9065 S22: -0.3786 S23: -2.3962
REMARK 3 S31: 1.3346 S32: 0.7814 S33: 0.2550
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7629 -40.8478 -38.4217
REMARK 3 T TENSOR
REMARK 3 T11: 0.8006 T22: 1.0188
REMARK 3 T33: 0.7890 T12: -0.0070
REMARK 3 T13: 0.0530 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 6.8087 L22: 7.8048
REMARK 3 L33: 2.0091 L12: -3.9920
REMARK 3 L13: -5.2405 L23: 4.1239
REMARK 3 S TENSOR
REMARK 3 S11: 0.4724 S12: 0.2942 S13: -0.0213
REMARK 3 S21: -0.6662 S22: 0.0643 S23: -1.8256
REMARK 3 S31: -0.9970 S32: 1.3860 S33: -0.5179
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 53 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1109 -53.1267 -16.3080
REMARK 3 T TENSOR
REMARK 3 T11: 1.0147 T22: 1.4243
REMARK 3 T33: 1.2252 T12: 0.1416
REMARK 3 T13: 0.1372 T23: -0.3821
REMARK 3 L TENSOR
REMARK 3 L11: 4.5830 L22: 9.9825
REMARK 3 L33: 6.2584 L12: 4.3647
REMARK 3 L13: -3.8232 L23: 0.5897
REMARK 3 S TENSOR
REMARK 3 S11: -0.3264 S12: 1.8625 S13: -1.5796
REMARK 3 S21: -1.0258 S22: 0.7125 S23: -2.3199
REMARK 3 S31: 0.9619 S32: 0.7462 S33: -0.3887
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 129 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4167 -59.8983 -3.2384
REMARK 3 T TENSOR
REMARK 3 T11: 1.1167 T22: 0.7521
REMARK 3 T33: 0.6902 T12: -0.1511
REMARK 3 T13: -0.1287 T23: 0.1058
REMARK 3 L TENSOR
REMARK 3 L11: 4.3452 L22: 6.7478
REMARK 3 L33: 3.8454 L12: -3.6515
REMARK 3 L13: 1.3321 L23: -2.2009
REMARK 3 S TENSOR
REMARK 3 S11: 0.3482 S12: -0.5253 S13: -1.4076
REMARK 3 S21: -0.1183 S22: 0.4472 S23: 0.4027
REMARK 3 S31: 2.0794 S32: -0.4207 S33: -0.7922
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 3651
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 594
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54979
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.434
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 1.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, L-PROLINE, HEPES, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 178.17050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.20200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.20200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 267.25575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.20200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.20200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 89.08525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.20200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.20200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 267.25575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.20200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.20200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 89.08525
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 178.17050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 69
REMARK 465 ALA A 70
REMARK 465 PHE A 71
REMARK 465 SER A 72
REMARK 465 GLU A 73
REMARK 465 ASP A 74
REMARK 465 ASP A 75
REMARK 465 GLY A 76
REMARK 465 ASP A 77
REMARK 465 GLY B 68
REMARK 465 SER B 69
REMARK 465 ALA B 70
REMARK 465 PHE B 71
REMARK 465 SER B 72
REMARK 465 GLU B 73
REMARK 465 ASP B 74
REMARK 465 ASP B 75
REMARK 465 GLY B 76
REMARK 465 ASP B 77
REMARK 465 GLU C 87
REMARK 465 GLU C 88
REMARK 465 CYS C 89
REMARK 465 ARG C 90
REMARK 465 ILE C 91
REMARK 465 GLU C 92
REMARK 465 PRO C 93
REMARK 465 CYS C 94
REMARK 465 THR C 95
REMARK 465 GLN C 96
REMARK 465 LYS C 97
REMARK 465 GLY C 98
REMARK 465 GLN C 99
REMARK 465 CYS C 100
REMARK 465 PRO C 101
REMARK 465 PRO C 102
REMARK 465 PRO C 103
REMARK 465 PRO C 104
REMARK 465 GLY C 105
REMARK 465 LEU C 106
REMARK 465 PRO C 107
REMARK 465 CYS C 108
REMARK 465 PRO C 109
REMARK 465 CYS C 110
REMARK 465 THR C 111
REMARK 465 GLY C 112
REMARK 465 VAL C 113
REMARK 465 SER C 114
REMARK 465 ASP C 115
REMARK 465 CYS C 116
REMARK 465 SER C 117
REMARK 465 GLY C 118
REMARK 465 GLY C 119
REMARK 465 THR C 120
REMARK 465 ASP C 121
REMARK 465 LYS C 122
REMARK 465 LYS C 123
REMARK 465 LEU C 124
REMARK 465 ARG C 125
REMARK 465 ASN C 126
REMARK 465 CYS C 127
REMARK 465 SER C 128
REMARK 465 GLU D 87
REMARK 465 GLU D 88
REMARK 465 CYS D 89
REMARK 465 ARG D 90
REMARK 465 ILE D 91
REMARK 465 GLU D 92
REMARK 465 PRO D 93
REMARK 465 CYS D 94
REMARK 465 THR D 95
REMARK 465 GLN D 96
REMARK 465 LYS D 97
REMARK 465 GLY D 98
REMARK 465 GLN D 99
REMARK 465 CYS D 100
REMARK 465 PRO D 101
REMARK 465 PRO D 102
REMARK 465 PRO D 103
REMARK 465 PRO D 104
REMARK 465 GLY D 105
REMARK 465 LEU D 106
REMARK 465 PRO D 107
REMARK 465 CYS D 108
REMARK 465 PRO D 109
REMARK 465 CYS D 110
REMARK 465 THR D 111
REMARK 465 GLY D 112
REMARK 465 VAL D 113
REMARK 465 SER D 114
REMARK 465 ASP D 115
REMARK 465 CYS D 116
REMARK 465 SER D 117
REMARK 465 GLY D 118
REMARK 465 GLY D 119
REMARK 465 THR D 120
REMARK 465 ASP D 121
REMARK 465 LYS D 122
REMARK 465 LYS D 123
REMARK 465 LEU D 124
REMARK 465 ARG D 125
REMARK 465 ASN D 126
REMARK 465 CYS D 127
REMARK 465 SER D 128
REMARK 465 GLU D 171
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 79 CG CD OE1 NE2
REMARK 470 HIS A 126 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 129 CG CD CE NZ
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 GLN B 79 CG CD OE1 NE2
REMARK 470 HIS B 126 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 129 CG CD CE NZ
REMARK 470 GLU B 299 CG CD OE1 OE2
REMARK 470 LYS C 58 CG CD CE NZ
REMARK 470 GLN C 60 CG CD OE1 NE2
REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 66 CG CD1 CD2
REMARK 470 ARG C 73 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 76 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 129 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 171 CG CD OE1 OE2
REMARK 470 LYS D 58 CG CD CE NZ
REMARK 470 GLN D 60 CG CD OE1 NE2
REMARK 470 ARG D 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 73 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 76 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP C 82 OG SER C 84 1.92
REMARK 500 NE2 GLN B 389 O HOH B 603 1.94
REMARK 500 OE2 GLU B 1 O HOH B 601 2.09
REMARK 500 ND1 HIS A 104 OD2 ASP C 77 2.10
REMARK 500 OE1 GLU B 353 O HOH B 604 2.12
REMARK 500 O63 CNC B 501 O HOH B 605 2.16
REMARK 500 O44 CNC B 501 O HOH B 606 2.17
REMARK 500 SG CYS A 65 CB CYS A 78 2.18
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 CYS A 78 CB CYS A 78 SG 0.200
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 ILE B 329 CG1 - CB - CG2 ANGL. DEV. = -27.6 DEGREES
REMARK 500 LYS B 343 CD - CE - NZ ANGL. DEV. = -18.7 DEGREES
REMARK 500 ASP B 382 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU C 70 CA - CB - CG ANGL. DEV. = 23.1 DEGREES
REMARK 500 SER C 81 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 CYS D 67 CA - CB - SG ANGL. DEV. = 7.1 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 GLN A 79 -81.56 -119.05
REMARK 500 THR A 134 -88.51 -109.97
REMARK 500 THR B 134 -88.31 -110.20
REMARK 500 PHE B 168 64.88 -105.44
REMARK 500 ARG C 62 -7.19 82.43
REMARK 500 ASP C 75 43.07 -88.37
REMARK 500 SER C 81 -77.53 14.31
REMARK 500 SER C 84 86.24 -66.58
REMARK 500 THR D 57 46.87 -103.65
REMARK 500 ASP D 75 39.46 -90.67
REMARK 500 SER D 84 55.85 -115.36
REMARK 500 THR D 169 -63.01 -106.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 166 PRO B 167 -149.17
REMARK 500 CYS C 80 SER C 81 135.46
REMARK 500 THR D 57 LYS D 58 146.84
REMARK 500 THR D 169 ASN D 170 -134.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP C 72 O
REMARK 620 2 ASP C 75 OD1 76.4
REMARK 620 3 ASP C 77 O 142.8 79.6
REMARK 620 4 ASP C 79 OD2 74.4 76.2 72.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP C 150 O
REMARK 620 2 ASP C 153 OD1 78.0
REMARK 620 3 HIS C 155 O 166.0 88.1
REMARK 620 4 ASP C 157 OD2 102.0 97.7 81.4
REMARK 620 5 ASP C 163 OD2 104.7 170.5 88.8 90.6
REMARK 620 6 GLU C 164 OE2 89.4 70.7 84.2 161.9 100.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP D 72 O
REMARK 620 2 ASP D 75 OD1 89.5
REMARK 620 3 ASP D 77 O 176.8 89.4
REMARK 620 4 ASP D 79 OD2 99.7 87.5 83.3
REMARK 620 5 ASP D 85 OD1 72.0 160.0 109.5 88.5
REMARK 620 6 ASP D 85 OD2 118.0 141.8 64.4 63.5 50.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP D 150 O
REMARK 620 2 ASP D 153 OD1 80.4
REMARK 620 3 HIS D 155 O 167.5 87.1
REMARK 620 4 ASP D 157 OD2 100.9 95.7 81.2
REMARK 620 5 ASP D 163 OD2 109.1 168.8 83.2 88.2
REMARK 620 6 GLU D 164 OE2 90.8 75.2 85.0 163.8 98.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CNC A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CNC B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZRP RELATED DB: PDB
DBREF 4ZRQ A 1 409 UNP P20062 TCO2_HUMAN 19 427
DBREF 4ZRQ B 1 409 UNP P20062 TCO2_HUMAN 19 427
DBREF 4ZRQ C 53 171 UNP Q9NPF0 CD320_HUMAN 53 171
DBREF 4ZRQ D 53 171 UNP Q9NPF0 CD320_HUMAN 53 171
SEQADV 4ZRQ GLN A 209 UNP P20062 ARG 227 CONFLICT
SEQADV 4ZRQ GLN B 209 UNP P20062 ARG 227 CONFLICT
SEQADV 4ZRQ C UNP Q9NPF0 GLU 86 DELETION
SEQADV 4ZRQ D UNP Q9NPF0 GLU 86 DELETION
SEQRES 1 A 409 GLU MET CYS GLU ILE PRO GLU MET ASP SER HIS LEU VAL
SEQRES 2 A 409 GLU LYS LEU GLY GLN HIS LEU LEU PRO TRP MET ASP ARG
SEQRES 3 A 409 LEU SER LEU GLU HIS LEU ASN PRO SER ILE TYR VAL GLY
SEQRES 4 A 409 LEU ARG LEU SER SER LEU GLN ALA GLY THR LYS GLU ASP
SEQRES 5 A 409 LEU TYR LEU HIS SER LEU LYS LEU GLY TYR GLN GLN CYS
SEQRES 6 A 409 LEU LEU GLY SER ALA PHE SER GLU ASP ASP GLY ASP CYS
SEQRES 7 A 409 GLN GLY LYS PRO SER MET GLY GLN LEU ALA LEU TYR LEU
SEQRES 8 A 409 LEU ALA LEU ARG ALA ASN CYS GLU PHE VAL ARG GLY HIS
SEQRES 9 A 409 LYS GLY ASP ARG LEU VAL SER GLN LEU LYS TRP PHE LEU
SEQRES 10 A 409 GLU ASP GLU LYS ARG ALA ILE GLY HIS ASP HIS LYS GLY
SEQRES 11 A 409 HIS PRO HIS THR SER TYR TYR GLN TYR GLY LEU GLY ILE
SEQRES 12 A 409 LEU ALA LEU CYS LEU HIS GLN LYS ARG VAL HIS ASP SER
SEQRES 13 A 409 VAL VAL ASP LYS LEU LEU TYR ALA VAL GLU PRO PHE HIS
SEQRES 14 A 409 GLN GLY HIS HIS SER VAL ASP THR ALA ALA MET ALA GLY
SEQRES 15 A 409 LEU ALA PHE THR CYS LEU LYS ARG SER ASN PHE ASN PRO
SEQRES 16 A 409 GLY ARG ARG GLN ARG ILE THR MET ALA ILE ARG THR VAL
SEQRES 17 A 409 GLN GLU GLU ILE LEU LYS ALA GLN THR PRO GLU GLY HIS
SEQRES 18 A 409 PHE GLY ASN VAL TYR SER THR PRO LEU ALA LEU GLN PHE
SEQRES 19 A 409 LEU MET THR SER PRO MET ARG GLY ALA GLU LEU GLY THR
SEQRES 20 A 409 ALA CYS LEU LYS ALA ARG VAL ALA LEU LEU ALA SER LEU
SEQRES 21 A 409 GLN ASP GLY ALA PHE GLN ASN ALA LEU MET ILE SER GLN
SEQRES 22 A 409 LEU LEU PRO VAL LEU ASN HIS LYS THR TYR ILE ASP LEU
SEQRES 23 A 409 ILE PHE PRO ASP CYS LEU ALA PRO ARG VAL MET LEU GLU
SEQRES 24 A 409 PRO ALA ALA GLU THR ILE PRO GLN THR GLN GLU ILE ILE
SEQRES 25 A 409 SER VAL THR LEU GLN VAL LEU SER LEU LEU PRO PRO TYR
SEQRES 26 A 409 ARG GLN SER ILE SER VAL LEU ALA GLY SER THR VAL GLU
SEQRES 27 A 409 ASP VAL LEU LYS LYS ALA HIS GLU LEU GLY GLY PHE THR
SEQRES 28 A 409 TYR GLU THR GLN ALA SER LEU SER GLY PRO TYR LEU THR
SEQRES 29 A 409 SER VAL MET GLY LYS ALA ALA GLY GLU ARG GLU PHE TRP
SEQRES 30 A 409 GLN LEU LEU ARG ASP PRO ASN THR PRO LEU LEU GLN GLY
SEQRES 31 A 409 ILE ALA ASP TYR ARG PRO LYS ASP GLY GLU THR ILE GLU
SEQRES 32 A 409 LEU ARG LEU VAL SER TRP
SEQRES 1 B 409 GLU MET CYS GLU ILE PRO GLU MET ASP SER HIS LEU VAL
SEQRES 2 B 409 GLU LYS LEU GLY GLN HIS LEU LEU PRO TRP MET ASP ARG
SEQRES 3 B 409 LEU SER LEU GLU HIS LEU ASN PRO SER ILE TYR VAL GLY
SEQRES 4 B 409 LEU ARG LEU SER SER LEU GLN ALA GLY THR LYS GLU ASP
SEQRES 5 B 409 LEU TYR LEU HIS SER LEU LYS LEU GLY TYR GLN GLN CYS
SEQRES 6 B 409 LEU LEU GLY SER ALA PHE SER GLU ASP ASP GLY ASP CYS
SEQRES 7 B 409 GLN GLY LYS PRO SER MET GLY GLN LEU ALA LEU TYR LEU
SEQRES 8 B 409 LEU ALA LEU ARG ALA ASN CYS GLU PHE VAL ARG GLY HIS
SEQRES 9 B 409 LYS GLY ASP ARG LEU VAL SER GLN LEU LYS TRP PHE LEU
SEQRES 10 B 409 GLU ASP GLU LYS ARG ALA ILE GLY HIS ASP HIS LYS GLY
SEQRES 11 B 409 HIS PRO HIS THR SER TYR TYR GLN TYR GLY LEU GLY ILE
SEQRES 12 B 409 LEU ALA LEU CYS LEU HIS GLN LYS ARG VAL HIS ASP SER
SEQRES 13 B 409 VAL VAL ASP LYS LEU LEU TYR ALA VAL GLU PRO PHE HIS
SEQRES 14 B 409 GLN GLY HIS HIS SER VAL ASP THR ALA ALA MET ALA GLY
SEQRES 15 B 409 LEU ALA PHE THR CYS LEU LYS ARG SER ASN PHE ASN PRO
SEQRES 16 B 409 GLY ARG ARG GLN ARG ILE THR MET ALA ILE ARG THR VAL
SEQRES 17 B 409 GLN GLU GLU ILE LEU LYS ALA GLN THR PRO GLU GLY HIS
SEQRES 18 B 409 PHE GLY ASN VAL TYR SER THR PRO LEU ALA LEU GLN PHE
SEQRES 19 B 409 LEU MET THR SER PRO MET ARG GLY ALA GLU LEU GLY THR
SEQRES 20 B 409 ALA CYS LEU LYS ALA ARG VAL ALA LEU LEU ALA SER LEU
SEQRES 21 B 409 GLN ASP GLY ALA PHE GLN ASN ALA LEU MET ILE SER GLN
SEQRES 22 B 409 LEU LEU PRO VAL LEU ASN HIS LYS THR TYR ILE ASP LEU
SEQRES 23 B 409 ILE PHE PRO ASP CYS LEU ALA PRO ARG VAL MET LEU GLU
SEQRES 24 B 409 PRO ALA ALA GLU THR ILE PRO GLN THR GLN GLU ILE ILE
SEQRES 25 B 409 SER VAL THR LEU GLN VAL LEU SER LEU LEU PRO PRO TYR
SEQRES 26 B 409 ARG GLN SER ILE SER VAL LEU ALA GLY SER THR VAL GLU
SEQRES 27 B 409 ASP VAL LEU LYS LYS ALA HIS GLU LEU GLY GLY PHE THR
SEQRES 28 B 409 TYR GLU THR GLN ALA SER LEU SER GLY PRO TYR LEU THR
SEQRES 29 B 409 SER VAL MET GLY LYS ALA ALA GLY GLU ARG GLU PHE TRP
SEQRES 30 B 409 GLN LEU LEU ARG ASP PRO ASN THR PRO LEU LEU GLN GLY
SEQRES 31 B 409 ILE ALA ASP TYR ARG PRO LYS ASP GLY GLU THR ILE GLU
SEQRES 32 B 409 LEU ARG LEU VAL SER TRP
SEQRES 1 C 118 SER CYS PRO PRO THR LYS PHE GLN CYS ARG THR SER GLY
SEQRES 2 C 118 LEU CYS VAL PRO LEU THR TRP ARG CYS ASP ARG ASP LEU
SEQRES 3 C 118 ASP CYS SER ASP GLY SER ASP GLU GLU CYS ARG ILE GLU
SEQRES 4 C 118 PRO CYS THR GLN LYS GLY GLN CYS PRO PRO PRO PRO GLY
SEQRES 5 C 118 LEU PRO CYS PRO CYS THR GLY VAL SER ASP CYS SER GLY
SEQRES 6 C 118 GLY THR ASP LYS LYS LEU ARG ASN CYS SER ARG LEU ALA
SEQRES 7 C 118 CYS LEU ALA GLY GLU LEU ARG CYS THR LEU SER ASP ASP
SEQRES 8 C 118 CYS ILE PRO LEU THR TRP ARG CYS ASP GLY HIS PRO ASP
SEQRES 9 C 118 CYS PRO ASP SER SER ASP GLU LEU GLY CYS GLY THR ASN
SEQRES 10 C 118 GLU
SEQRES 1 D 118 SER CYS PRO PRO THR LYS PHE GLN CYS ARG THR SER GLY
SEQRES 2 D 118 LEU CYS VAL PRO LEU THR TRP ARG CYS ASP ARG ASP LEU
SEQRES 3 D 118 ASP CYS SER ASP GLY SER ASP GLU GLU CYS ARG ILE GLU
SEQRES 4 D 118 PRO CYS THR GLN LYS GLY GLN CYS PRO PRO PRO PRO GLY
SEQRES 5 D 118 LEU PRO CYS PRO CYS THR GLY VAL SER ASP CYS SER GLY
SEQRES 6 D 118 GLY THR ASP LYS LYS LEU ARG ASN CYS SER ARG LEU ALA
SEQRES 7 D 118 CYS LEU ALA GLY GLU LEU ARG CYS THR LEU SER ASP ASP
SEQRES 8 D 118 CYS ILE PRO LEU THR TRP ARG CYS ASP GLY HIS PRO ASP
SEQRES 9 D 118 CYS PRO ASP SER SER ASP GLU LEU GLY CYS GLY THR ASN
SEQRES 10 D 118 GLU
HET CNC A 501 93
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 504 6
HET CNC B 501 93
HET GOL B 502 6
HET CA C 201 1
HET CA C 202 1
HET CA D 201 1
HET CA D 202 1
HETNAM CNC CYANOCOBALAMIN
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 CNC 2(C63 H89 CO N14 O14 P 2+)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 11 CA 4(CA 2+)
FORMUL 15 HOH *44(H2 O)
HELIX 1 AA1 ASP A 9 LEU A 21 1 13
HELIX 2 AA2 PRO A 22 ARG A 26 5 5
HELIX 3 AA3 ASN A 33 LEU A 42 1 10
HELIX 4 AA4 GLY A 48 LEU A 66 1 19
HELIX 5 AA5 SER A 83 ASN A 97 1 15
HELIX 6 AA6 ARG A 102 GLY A 125 1 24
HELIX 7 AA7 SER A 135 HIS A 149 1 15
HELIX 8 AA8 HIS A 154 GLU A 166 1 13
HELIX 9 AA9 SER A 174 ASN A 192 1 19
HELIX 10 AB1 ASN A 194 GLY A 196 5 3
HELIX 11 AB2 ARG A 197 ALA A 215 1 19
HELIX 12 AB3 SER A 227 THR A 237 1 11
HELIX 13 AB4 GLU A 244 ASP A 262 1 19
HELIX 14 AB5 ASN A 267 ASN A 279 1 13
HELIX 15 AB6 THR A 282 ILE A 287 5 6
HELIX 16 AB7 THR A 336 LEU A 347 1 12
HELIX 17 AB8 ASP B 9 LEU B 21 1 13
HELIX 18 AB9 PRO B 22 ARG B 26 5 5
HELIX 19 AC1 ASN B 33 LEU B 42 1 10
HELIX 20 AC2 GLY B 48 LEU B 67 1 20
HELIX 21 AC3 SER B 83 ALA B 96 1 14
HELIX 22 AC4 ARG B 102 GLY B 125 1 24
HELIX 23 AC5 SER B 135 HIS B 149 1 15
HELIX 24 AC6 HIS B 154 GLU B 166 1 13
HELIX 25 AC7 SER B 174 SER B 191 1 18
HELIX 26 AC8 ASN B 194 GLY B 196 5 3
HELIX 27 AC9 ARG B 197 ALA B 215 1 19
HELIX 28 AD1 SER B 227 MET B 236 1 10
HELIX 29 AD2 GLU B 244 ASP B 262 1 19
HELIX 30 AD3 ASN B 267 ASN B 279 1 13
HELIX 31 AD4 THR B 282 ILE B 287 5 6
HELIX 32 AD5 THR B 336 LEU B 347 1 12
HELIX 33 AD6 THR C 149 ARG C 151 5 3
HELIX 34 AD7 SER C 161 LEU C 165 5 5
HELIX 35 AD8 THR D 149 ARG D 151 5 3
HELIX 36 AD9 SER D 161 LEU D 165 5 5
SHEET 1 AA1 2 LEU A 45 GLN A 46 0
SHEET 2 AA1 2 VAL A 296 MET A 297 1 O VAL A 296 N GLN A 46
SHEET 1 AA2 5 TYR A 325 LEU A 332 0
SHEET 2 AA2 5 ILE A 311 VAL A 318 -1 N VAL A 314 O ILE A 329
SHEET 3 AA2 5 THR A 401 SER A 408 1 O ILE A 402 N THR A 315
SHEET 4 AA2 5 GLU A 375 ARG A 381 -1 N GLN A 378 O ARG A 405
SHEET 5 AA2 5 THR A 385 PRO A 386 -1 O THR A 385 N ARG A 381
SHEET 1 AA3 3 TYR A 352 GLN A 355 0
SHEET 2 AA3 3 TYR A 362 VAL A 366 -1 O TYR A 362 N GLN A 355
SHEET 3 AA3 3 LYS A 369 ALA A 370 -1 O LYS A 369 N VAL A 366
SHEET 1 AA4 2 LEU B 45 GLN B 46 0
SHEET 2 AA4 2 VAL B 296 MET B 297 1 O VAL B 296 N GLN B 46
SHEET 1 AA5 5 TYR B 325 LEU B 332 0
SHEET 2 AA5 5 ILE B 311 VAL B 318 -1 N VAL B 314 O ILE B 329
SHEET 3 AA5 5 THR B 401 SER B 408 1 O ILE B 402 N THR B 315
SHEET 4 AA5 5 GLU B 375 ARG B 381 -1 N GLN B 378 O ARG B 405
SHEET 5 AA5 5 THR B 385 PRO B 386 -1 O THR B 385 N ARG B 381
SHEET 1 AA6 3 TYR B 352 GLN B 355 0
SHEET 2 AA6 3 TYR B 362 VAL B 366 -1 O TYR B 362 N GLN B 355
SHEET 3 AA6 3 LYS B 369 ALA B 370 -1 O LYS B 369 N VAL B 366
SHEET 1 AA7 2 GLU C 136 ARG C 138 0
SHEET 2 AA7 2 CYS C 145 PRO C 147 -1 O ILE C 146 N LEU C 137
SHEET 1 AA8 2 GLU D 136 ARG D 138 0
SHEET 2 AA8 2 CYS D 145 PRO D 147 -1 O ILE D 146 N LEU D 137
SSBOND 1 CYS A 3 CYS A 249 1555 1555 2.03
SSBOND 2 CYS A 65 CYS A 78 1555 1555 2.09
SSBOND 3 CYS A 98 CYS A 291 1555 1555 2.03
SSBOND 4 CYS A 147 CYS A 187 1555 1555 2.03
SSBOND 5 CYS B 3 CYS B 249 1555 1555 2.03
SSBOND 6 CYS B 65 CYS B 78 1555 1555 2.04
SSBOND 7 CYS B 98 CYS B 291 1555 1555 2.03
SSBOND 8 CYS B 147 CYS B 187 1555 1555 2.03
SSBOND 9 CYS C 54 CYS C 67 1555 1555 2.04
SSBOND 10 CYS C 61 CYS C 80 1555 1555 2.05
SSBOND 11 CYS C 132 CYS C 145 1555 1555 2.03
SSBOND 12 CYS C 139 CYS C 158 1555 1555 2.03
SSBOND 13 CYS C 152 CYS C 167 1555 1555 2.03
SSBOND 14 CYS D 54 CYS D 67 1555 1555 2.07
SSBOND 15 CYS D 61 CYS D 80 1555 1555 2.03
SSBOND 16 CYS D 132 CYS D 145 1555 1555 2.03
SSBOND 17 CYS D 139 CYS D 158 1555 1555 2.03
SSBOND 18 CYS D 152 CYS D 167 1555 1555 2.03
LINK O TRP C 72 CA CA C 202 1555 1555 2.80
LINK OD1 ASP C 75 CA CA C 202 1555 1555 2.51
LINK O ASP C 77 CA CA C 202 1555 1555 2.57
LINK OD2 ASP C 79 CA CA C 202 1555 1555 2.37
LINK O TRP C 150 CA CA C 201 1555 1555 2.34
LINK OD1 ASP C 153 CA CA C 201 1555 1555 2.45
LINK O HIS C 155 CA CA C 201 1555 1555 2.35
LINK OD2 ASP C 157 CA CA C 201 1555 1555 2.41
LINK OD2 ASP C 163 CA CA C 201 1555 1555 2.32
LINK OE2 GLU C 164 CA CA C 201 1555 1555 2.48
LINK O TRP D 72 CA CA D 202 1555 1555 2.73
LINK OD1 ASP D 75 CA CA D 202 1555 1555 2.30
LINK O ASP D 77 CA CA D 202 1555 1555 2.52
LINK OD2 ASP D 79 CA CA D 202 1555 1555 2.52
LINK OD1 ASP D 85 CA CA D 202 1555 1555 2.26
LINK OD2 ASP D 85 CA CA D 202 1555 1555 2.80
LINK O TRP D 150 CA CA D 201 1555 1555 2.30
LINK OD1 ASP D 153 CA CA D 201 1555 1555 2.38
LINK O HIS D 155 CA CA D 201 1555 1555 2.31
LINK OD2 ASP D 157 CA CA D 201 1555 1555 2.38
LINK OD2 ASP D 163 CA CA D 201 1555 1555 2.46
LINK OE2 GLU D 164 CA CA D 201 1555 1555 2.37
CISPEP 1 LEU A 322 PRO A 323 0 -4.40
CISPEP 2 ASP A 382 PRO A 383 0 1.32
CISPEP 3 ARG B 241 GLY B 242 0 5.99
CISPEP 4 LEU B 322 PRO B 323 0 -4.82
CISPEP 5 ASP B 382 PRO B 383 0 3.76
CISPEP 6 ARG C 73 CYS C 74 0 -12.50
CISPEP 7 CYS C 167 GLY C 168 0 6.11
CISPEP 8 ARG D 73 CYS D 74 0 -16.41
SITE 1 AC1 27 GLY A 85 GLN A 86 THR A 134 TYR A 137
SITE 2 AC1 27 GLN A 138 ASP A 176 ASN A 224 TYR A 226
SITE 3 AC1 27 SER A 227 MET A 270 GLN A 273 SER A 357
SITE 4 AC1 27 LEU A 358 SER A 359 GLY A 360 PRO A 361
SITE 5 AC1 27 TYR A 362 LEU A 363 PHE A 376 TRP A 377
SITE 6 AC1 27 GLN A 378 LEU A 379 LEU A 387 LEU A 388
SITE 7 AC1 27 GLY A 390 TRP A 409 HOH A 605
SITE 1 AC2 5 SER A 174 THR A 177 TRP A 409 HOH A 609
SITE 2 AC2 5 HOH A 610
SITE 1 AC3 5 HIS A 169 HIS A 172 HIS A 173 GLU A 211
SITE 2 AC3 5 HOH A 612
SITE 1 AC4 5 GLY A 372 GLU A 373 GLU A 375 GLY B 372
SITE 2 AC4 5 GLU B 375
SITE 1 AC5 28 GLY B 85 GLN B 86 THR B 134 TYR B 137
SITE 2 AC5 28 GLN B 138 ASP B 176 ASN B 224 TYR B 226
SITE 3 AC5 28 SER B 227 MET B 270 GLN B 273 SER B 357
SITE 4 AC5 28 LEU B 358 SER B 359 GLY B 360 PRO B 361
SITE 5 AC5 28 TYR B 362 LEU B 363 PHE B 376 TRP B 377
SITE 6 AC5 28 GLN B 378 LEU B 379 LEU B 387 LEU B 388
SITE 7 AC5 28 GLY B 390 TRP B 409 HOH B 606 HOH B 607
SITE 1 AC6 7 GLN B 63 ARG B 102 GLY B 103 LYS B 105
SITE 2 AC6 7 ASP D 77 LEU D 78 ASP D 79
SITE 1 AC7 6 TRP C 150 ASP C 153 HIS C 155 ASP C 157
SITE 2 AC7 6 ASP C 163 GLU C 164
SITE 1 AC8 6 TRP C 72 CYS C 74 ASP C 75 ASP C 77
SITE 2 AC8 6 ASP C 79 ASP C 85
SITE 1 AC9 6 TRP D 150 ASP D 153 HIS D 155 ASP D 157
SITE 2 AC9 6 ASP D 163 GLU D 164
SITE 1 AD1 5 TRP D 72 ASP D 75 ASP D 77 ASP D 79
SITE 2 AD1 5 ASP D 85
CRYST1 98.404 98.404 356.341 90.00 90.00 90.00 P 43 21 2 16
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 0.010162 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END